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  • Rats  (70)
  • Transfection  (59)
  • American Association for the Advancement of Science (AAAS)  (123)
  • American Institute of Physics (AIP)
  • Oxford University Press
  • 1995-1999
  • 1990-1994  (123)
  • 1993  (123)
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  • American Association for the Advancement of Science (AAAS)  (123)
  • American Institute of Physics (AIP)
  • Oxford University Press
  • Springer  (3)
Years
  • 1995-1999
  • 1990-1994  (123)
Year
  • 1
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    Role of intracellular calcium in NI-35-evoked collapse of neuronal growth cones (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-01-01
    Description: A myelin-associated protein from the central nervous system, the neurite growth inhibitor NI-35, inhibits regeneration of lesioned neuronal fiber tracts in vivo and growth of neurites in vitro. Growth cones of cultured rat dorsal root ganglion neurons arrested their growth and collapsed when exposed to liposomes containing NI-35. Before morphological changes, the concentration of free intracellular calcium ([Ca2+]i) showed a rapid and large increase in growth cones exposed to liposomes containing NI-35. Neither an increase in [Ca2+]i nor collapse of growth cones was detected in the presence of antibodies to NI-35. Dantrolene, an inhibitor of calcium release from caffeine-sensitive intracellular calcium stores, protected growth cones from collapse evoked by NI-35. Depletion of these caffeine-sensitive intracellular calcium stores prevented the increase in [Ca2+]i evoked by NI-35. The NI-35-evoked cascade of intracellular messengers that mediates collapse of growth cones includes the crucial step of calcium release from intracellular stores.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bandtlow, C E -- Schmidt, M F -- Hassinger, T D -- Schwab, M E -- Kater, S B -- NS24683/NS/NINDS NIH HHS/ -- NS28323/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1993 Jan 1;259(5091):80-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Brain Research Institute, University of Zurich, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8418499" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Caffeine/pharmacology ; Calcium/*metabolism ; Cells, Cultured ; Drug Carriers ; Fura-2 ; Ganglia, Spinal/*physiology ; Growth Inhibitors/*pharmacology ; Kinetics ; Liposomes ; Nerve Fibers/drug effects/*physiology/ultrastructure ; Neurons/drug effects/*physiology/ultrastructure ; Rats
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 2
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    Rate and mechanism of nonhomologous recombination during a single cycle of retroviral replication (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-01-08
    Description: Oncogenes discovered in retroviruses such as Rous sarcoma virus were generated by transduction of cellular proto-oncogenes into the viral genome. Several different kinds of junctions between the viral and proto-oncogene sequences have been found in different viruses. A system of retrovirus vectors and a protocol that mimicked this transduction during a single cycle of retrovirus replication was developed. The transduction involved the formation of a chimeric viral-cellular RNA, strand switching of the reverse transcription growing point from an infectious retrovirus to the chimeric RNA, and often a subsequent deletion during the rest of viral DNA synthesis. A short region of sequence identity was frequently used for the strand switching. The rate of this process was about 0.1 to 1 percent of the rate of homologous retroviral recombination.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zhang, J -- Temin, H M -- CA-07175/CA/NCI NIH HHS/ -- CA-22443/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1993 Jan 8;259(5092):234-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉McArdle Laboratory for Cancer Research, University of Wisconsin-Madison 53706.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8421784" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; *Cinnamates ; *DNA Replication ; DNA, Viral/chemistry/genetics ; Drug Resistance/genetics ; Genes, Viral ; Genetic Vectors ; Hygromycin B/analogs & derivatives ; Kinetics ; Mice ; Molecular Sequence Data ; Moloney murine leukemia virus/genetics ; Neomycin ; Plasmids ; *Proto-Oncogenes ; RNA, Viral/analysis/genetics ; *Recombination, Genetic ; Repetitive Sequences, Nucleic Acid ; Retroviridae/*genetics/physiology ; Transfection ; *Virus Replication
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 3
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    Mutations in the glucose-6-phosphatase gene that cause glycogen storage disease type 1a (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-10-22
    Description: Glycogen storage disease (GSD) type 1a is caused by the deficiency of D-glucose-6-phosphatase (G6Pase), the key enzyme in glucose homeostasis. Despite both a high incidence and morbidity, the molecular mechanisms underlying this deficiency have eluded characterization. In the present study, the molecular and biochemical characterization of the human G6Pase complementary DNA, its gene, and the expressed protein, which is indistinguishable from human microsomal G6Pase, are reported. Several mutations in the G6Pase gene of affected individuals that completely inactivate the enzyme have been identified. These results establish the molecular basis of this disease and open the way for future gene therapy.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lei, K J -- Shelly, L L -- Pan, C J -- Sidbury, J B -- Chou, J Y -- New York, N.Y. -- Science. 1993 Oct 22;262(5133):580-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Human Genetics Branch, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8211187" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Cell Line ; DNA, Complementary/genetics ; Exons ; Glucose-6-Phosphatase/*genetics/metabolism ; Glycogen Storage Disease Type I/enzymology/*genetics ; Glycosylation ; Humans ; Liver/enzymology ; Mice ; Molecular Sequence Data ; *Mutation ; Protein Conformation ; Transfection
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 4
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    Expression cloning and signaling properties of the rat glucagon receptor (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-03-12
    Description: Glucagon and the glucagon receptor are a primary source of control over blood glucose concentrations and are especially important to studies of diabetes in which the loss of control over blood glucose concentrations clinically defines the disease. A complementary DNA clone for the glucagon receptor was isolated by an expression cloning strategy, and the receptor protein was expressed in several kidney cell lines. The cloned receptor bound glucagon and caused an increase in the intracellular concentration of adenosine 3', 5'-monophosphate (cAMP). The cloned glucagon receptor also transduced a signal that led to an increased concentration of intracellular calcium. The glucagon receptor is similar to the calcitonin and parathyroid hormone receptors. It can transduce signals leading to the accumulation of two different second messengers, cAMP and calcium.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jelinek, L J -- Lok, S -- Rosenberg, G B -- Smith, R A -- Grant, F J -- Biggs, S -- Bensch, P A -- Kuijper, J L -- Sheppard, P O -- Sprecher, C A -- New York, N.Y. -- Science. 1993 Mar 12;259(5101):1614-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉ZymoGenetics Inc., Seattle, WA 98105.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8384375" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Calcium/pharmacology ; Cell Line ; Cloning, Molecular ; Cricetinae ; Cyclic AMP/metabolism ; Glucagon/metabolism/*pharmacology ; Kidney ; Kinetics ; Liver/*metabolism ; Molecular Sequence Data ; Rats ; Receptors, Gastrointestinal Hormone/genetics/metabolism/*physiology ; Receptors, Glucagon ; *Signal Transduction ; Transfection
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 5
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    Inhibition by cAMP of Ras-dependent activation of Raf (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-11-12
    Description: Activation of the Raf and extracellular signal-regulated kinases (ERKs) (or mitogen-activated protein kinases) are key events in mitogenic signalling, but little is known about interactions with other signaling pathways. Agents that raise levels of intracellular cyclic adenosine 3',5'-monophosphate (cAMP) blocked DNA synthesis and signal transduction in Rat1 cells exposed to epidermal growth factor (EGF) or lysophosphatidic acid. In the case of EGF, receptor tyrosine kinase activity and association with the signaling molecules Grb2 and Shc were unaffected by cAMP. Likewise, EGF-dependent accumulation of the guanosine 5'-triphosphate-bound form of Ras was unaffected. In contrast, activation of Raf-1 and ERK kinases was inhibited. Thus, cAMP appears to inhibit signal transmission from Ras by preventing Ras-dependent activation of Raf-1.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cook, S J -- McCormick, F -- UO1 CA51992-03/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1993 Nov 12;262(5136):1069-72.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Onyx Pharmaceuticals, Richmond, CA 94806.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7694367" target="_blank"〉PubMed〈/a〉
    Keywords: 1-Methyl-3-isobutylxanthine/pharmacology ; Animals ; Bucladesine/pharmacology ; Calcium-Calmodulin-Dependent Protein Kinases/*metabolism ; Cell Line ; Cholera Toxin/pharmacology ; Cyclic AMP/*pharmacology ; Cyclic AMP-Dependent Protein Kinases/metabolism ; Enzyme Activation ; Epidermal Growth Factor/pharmacology ; Interphase ; Lysophospholipids/pharmacology ; Mitogen-Activated Protein Kinase 1 ; Mitogen-Activated Protein Kinase 3 ; *Mitogen-Activated Protein Kinases ; Phosphorylation ; Protein-Tyrosine Kinases/*metabolism ; Proto-Oncogene Proteins/*metabolism ; Proto-Oncogene Proteins c-raf ; Proto-Oncogene Proteins p21(ras)/*metabolism ; Rats ; Receptor, Epidermal Growth Factor/metabolism ; *Signal Transduction
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 6
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    Induction of G alpha i2-specific antisense RNA in vivo inhibits neonatal growth (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-05-14
    Description: Guanosine triphosphate-binding regulatory proteins (G proteins) are key elements in transmembrane signaling and have been implicated as regulators of more complex biological processes such as differentiation and development. The G protein G alpha i2 is capable of mediating the inhibitory control of adenylylcyclase and regulates stem cell differentiation to primitive endoderm. Here an antisense RNA to G alpha i2 was expressed in a hybrid RNA construct whose expression was both tissue-specific and induced at birth. Transgenic mice in which the antisense construct was expressed displayed a lack of normal development in targeted organs that correlated with the absence of G alpha i2. The loss of G alpha i2 expression in adipose tissue of the transgenic mice was correlated with a rise in basal levels of adenosine 3',5'-monophosphate (cAMP) and the loss of receptor-mediated inhibition of adenylylcyclase. These data expand our understanding of G protein function in vivo and demonstrate the necessity for G alpha i2 in the development of liver and fat.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Moxham, C M -- Hod, Y -- Malbon, C C -- New York, N.Y. -- Science. 1993 May 14;260(5110):991-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Pharmacology, State University of New York (SUNY)/Stony Brook 11794-8651.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8493537" target="_blank"〉PubMed〈/a〉
    Keywords: Adipose Tissue/*growth & development/metabolism ; Animals ; Animals, Newborn/growth & development ; Base Sequence ; Body Weight ; GTP-Binding Proteins/biosynthesis/genetics/*physiology ; Growth/drug effects/*physiology ; Kidney/growth & development/metabolism ; Liver/*growth & development/metabolism ; Mice ; Mice, Transgenic ; Molecular Sequence Data ; Phosphoenolpyruvate Carboxykinase (GTP)/genetics ; RNA, Antisense/*genetics ; Transfection
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 7
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    Uncovering of functional alternative CTLA-4 counter-receptor in B7-deficient mice (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-11-05
    Description: B7 delivers a costimulatory signal through CD28, resulting in interleukin-2 secretion and T cell proliferation. Blockade of this pathway results in T cell anergy. The in vivo role of B7 was evaluated with B7-deficient mice. These mice had a 70 percent decrease in costimulation of the response to alloantigen. Despite lacking B7 expression, activated B cells from these mice bound CTLA-4 and GL1 monoclonal antibody, demonstrating that alternative CTLA-4 ligand or ligands exist. These receptors are functionally important because the residual allogenic mixed lymphocyte responses were blocked by CTLA4Ig. Characterization of these CTLA-4 ligands should lead to strategies for manipulating the immune response.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Freeman, G J -- Borriello, F -- Hodes, R J -- Reiser, H -- Hathcock, K S -- Laszlo, G -- McKnight, A J -- Kim, J -- Du, L -- Lombard, D B -- CA 40216/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1993 Nov 5;262(5135):907-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Hematologic Malignancies, Dana-Farber Cancer Institute, Boston, MA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7694362" target="_blank"〉PubMed〈/a〉
    Keywords: Abatacept ; Animals ; Antigens, CD ; Antigens, CD80/genetics/*immunology/metabolism ; Antigens, Differentiation/immunology/*metabolism ; B-Lymphocytes/*immunology ; Base Sequence ; CTLA-4 Antigen ; Cell Line ; *Immunoconjugates ; Interleukin-2/secretion ; Isoantigens/immunology ; Lymphocyte Activation ; Lymphocyte Culture Test, Mixed ; Mice ; Mice, Inbred BALB C ; Mice, Inbred C57BL ; Mice, Knockout ; Molecular Sequence Data ; Mutation ; T-Lymphocytes/*immunology ; Transfection
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 8
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    Blood-brain barrier penetration and in vivo activity of an NGF conjugate (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-01-15
    Description: Nerve growth factor (NGF) is essential for the survival of both peripheral ganglion cells and central cholinergic neurons of the basal forebrain. The accelerated loss of central cholinergic neurons during Alzheimer's disease may be a determinant of dementia in these patients and may therefore suggest a therapeutic role for NGF. However, NGF does not significantly penetrate the blood-brain barrier, which makes its clinical utility dependent on invasive neurosurgical procedures. When conjugated to an antibody to the transferrin receptor, however, NGF crossed the blood-brain barrier after peripheral injection. This conjugated NGF increased the survival of both cholinergic and noncholinergic neurons of the medial septal nucleus that had been transplanted into the anterior chamber of the rat eye. This approach may prove useful for the treatment of Alzheimer's disease and other neurological disorders that are amenable to treatment by proteins that do not readily cross the blood-brain barrier.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Friden, P M -- Walus, L R -- Watson, P -- Doctrow, S R -- Kozarich, J W -- Backman, C -- Bergman, H -- Hoffer, B -- Bloom, F -- Granholm, A C -- NS29601-01/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1993 Jan 15;259(5093):373-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Alkermes, Inc., Cambridge, MA 02139.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8420006" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Anterior Chamber/metabolism ; Antibodies/*metabolism ; *Blood-Brain Barrier ; Brain/blood supply/metabolism ; Capillaries ; Cell Line ; Cross-Linking Reagents ; Dose-Response Relationship, Drug ; Drug Carriers ; Immunohistochemistry ; Nerve Growth Factors/administration & dosage/*pharmacokinetics/pharmacology ; Rats ; Rats, Sprague-Dawley ; Receptors, Transferrin/*immunology
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 9
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    Selective and ATP-dependent translocation of peptides by the MHC-encoded transporter (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-08-06
    Description: Major histocompatibility complex (MHC) class I molecules present peptides derived from nuclear and cytosolic proteins to CD8+ T cells. These peptides are translocated into the lumen of the endoplasmic reticulum (ER) to associate with class I molecules. Two MHC-encoded putative transporter proteins, TAP1 and TAP2, are required for efficient assembly of class I molecules and presentation of endogenous peptides. Expression of TAP1 and TAP2 in a mutant cell line resulted in the delivery of an 11-amino acid oligomer model peptide to the ER. Peptide translocation depended on the sequence of the peptide, was adenosine triphosphate (ATP)-dependent, required ATP hydrolysis, and was inhibited in a concentration-dependent manner.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Neefjes, J J -- Momburg, F -- Hammerling, G J -- New York, N.Y. -- Science. 1993 Aug 6;261(5122):769-71.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉The Netherlands Cancer Institute, Amsterdam.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8342042" target="_blank"〉PubMed〈/a〉
    Keywords: *ATP-Binding Cassette Transporters ; Adenosine Triphosphate/*metabolism ; Amino Acid Sequence ; Animals ; Biological Transport ; Carrier Proteins/*metabolism ; Cell Line ; Cell Membrane Permeability ; Endoplasmic Reticulum/metabolism ; Glycosylation ; Histocompatibility Antigens Class II/*metabolism ; Molecular Sequence Data ; Oligopeptides/*metabolism ; Rats ; T-Lymphocytes, Cytotoxic/*metabolism ; Transfection
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 10
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    Higher level organization of individual gene transcription and RNA splicing (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-02-26
    Description: Visualization of fibronectin and neurotensin messenger RNAs within mammalian interphase nuclei was achieved by fluorescence hybridization with genomic, complementary DNA, and intron-specific probes. Unspliced transcripts accumulated in one or two sites per nucleus. Fibronectin RNA frequently accumulated in elongated tracks that overlapped and extended well beyond the site of transcription. Splicing appears to occur directly within this RNA track, as evidenced by an unambiguous spatial separation of intron-containing and spliced transcripts. Excised introns for neurotensin RNA appear free to diffuse. The transcription and processing site of the fibronectin gene localized to the nuclear interior and was associated with larger transcript domains in over 88 percent of the cells. These results support a view of nuclear function closely integrated with structure.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Xing, Y -- Johnson, C V -- Dobner, P R -- Lawrence, J B -- R01 HG00251/HG/NHGRI NIH HHS/ -- R01 HL33307/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1993 Feb 26;259(5099):1326-30.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology, University of Massachusetts Medical Center, Worcester 01655.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8446901" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Nucleus/metabolism/*ultrastructure ; Fibronectins/genetics ; Gene Expression ; In Vitro Techniques ; Introns ; Microscopy, Fluorescence ; Neurotensin/genetics ; PC12 Cells ; Poly A/metabolism ; *RNA Processing, Post-Transcriptional ; RNA Splicing ; RNA, Messenger/*metabolism ; Rats ; Spliceosomes/metabolism ; *Transcription, Genetic
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 11
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    An adenovirus vector for gene transfer into neurons and glia in the brain (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-02-12
    Description: The efficient introduction of genetic material into quiescent nerve cells is important in the study of brain function and for gene therapy of neurological disorders. A replication-deficient adenoviral vector that contained a reporter gene encoding beta-galactosidase infected rat nerve cells in vitro and in vivo. beta-Galactosidase was expressed in almost all sympathetic neurons and astrocytes in culture. After stereotactic inoculations into the rat hippocampus and the substantia nigra, beta-galactosidase activity was detected for 2 months. Infected cells were identified as microglial cells, astrocytes, or neurons with anatomical, morphological, and immunohistochemical criteria. No obvious cytopathic effect was observed.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Le Gal La Salle, G -- Robert, J J -- Berrard, S -- Ridoux, V -- Stratford-Perricaudet, L D -- Perricaudet, M -- Mallet, J -- New York, N.Y. -- Science. 1993 Feb 12;259(5097):988-90.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institut Alfred Fessard, Unite Propre de Recherche 2212, Centre National de la Recherche Scientifique (CNRS), Gif sur Yvette, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8382374" target="_blank"〉PubMed〈/a〉
    Keywords: Adenoviridae/*genetics ; Animals ; Astrocytes/metabolism/microbiology ; Avian Sarcoma Viruses/genetics ; Brain/*cytology ; DNA/genetics ; Gene Expression ; *Genetic Vectors ; Hippocampus/cytology/metabolism ; Neuroglia/*metabolism/microbiology ; Neurons/*metabolism/microbiology ; Promoter Regions, Genetic/genetics ; Rats ; Substantia Nigra/cytology/metabolism ; *Transfection ; beta-Galactosidase/genetics
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 12
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    Retinoic acid stimulates regeneration of mammalian auditory hair cells (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-04-30
    Description: Sensorineural hearing loss resulting from the loss of auditory hair cells is thought to be irreversible in mammals. This study provides evidence that retinoic acid can stimulate the regeneration in vitro of mammalian auditory hair cells in ototoxic-poisoned organ of Corti explants in the rat. In contrast, treatment with retinoic acid does not stimulate the formation of extra hair cells in control cultures of Corti's organ. Retinoic acid-stimulated hair cell regeneration can be blocked by cytosine arabinoside, which suggests that a period of mitosis is required for the regeneration of auditory hair cells in this system. These results provide hope for a recovery of hearing function in mammals after auditory hair cell damage.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lefebvre, P P -- Malgrange, B -- Staecker, H -- Moonen, G -- Van de Water, T R -- DC00088/DC/NIDCD NIH HHS/ -- NS07098/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1993 Apr 30;260(5108):692-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Human Physiology and Pathophysiology, University of Liege, Belgium.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8480180" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cytarabine/pharmacology ; Hair Cells, Auditory/*drug effects/physiology/ultrastructure ; Microscopy, Electron ; Neomycin/toxicity ; Organ Culture Techniques ; Organ of Corti/*drug effects/physiology/ultrastructure ; Rats ; Regeneration/*drug effects ; Tretinoin/*pharmacology
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  • 13
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    Effects of cAMP simulate a late stage of LTP in hippocampal CA1 neurons (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-06-11
    Description: Hippocampal long-term potentiation (LTP) is thought to serve as an elementary mechanism for the establishment of certain forms of explicit memory in the mammalian brain. As is the case with behavioral memory, LTP in the CA1 region has stages: a short-term early potentiation lasting 1 to 3 hours, which is independent of protein synthesis, precedes a later, longer lasting stage (L-LTP), which requires protein synthesis. Inhibitors of cyclic adenosine monophosphate (cAMP)-dependent protein kinase (PKA) blocked L-LTP, and analogs of cAMP induced a potentiation that blocked naturally induced L-LTP. The action of the cAMP analog was blocked by inhibitors of protein synthesis. Thus, activation of PKA may be a component of the mechanism that generates L-LTP.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Frey, U -- Huang, Y Y -- Kandel, E R -- GM32099/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1993 Jun 11;260(5114):1661-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for Neurobiology and Behavior, Howard Hughes Medical Institute, College of Physicians and Surgeons, Columbia University, New York, NY 10032.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8389057" target="_blank"〉PubMed〈/a〉
    Keywords: Action Potentials/drug effects/physiology ; Animals ; Cyclic AMP/*physiology ; Hippocampus/cytology/drug effects/*physiology ; In Vitro Techniques ; Male ; Memory/physiology ; Neurons/drug effects/*physiology ; Protein Kinases/physiology ; Rats ; Rats, Sprague-Dawley ; Receptors, N-Methyl-D-Aspartate/physiology ; Second Messenger Systems/physiology ; Time Factors
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 14
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    GDNF: a glial cell line-derived neurotrophic factor for midbrain dopaminergic neurons (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-05-21
    Description: A potent neurotrophic factor that enhances survival of midbrain dopaminergic neurons was purified and cloned. Glial cell line-derived neurotrophic factor (GDNF) is a glycosylated, disulfide-bonded homodimer that is a distantly related member of the transforming growth factor-beta superfamily. In embryonic midbrain cultures, recombinant human GDNF promoted the survival and morphological differentiation of dopaminergic neurons and increased their high-affinity dopamine uptake. These effects were relatively specific; GDNF did not increase total neuron or astrocyte numbers nor did it increase transmitter uptake by gamma-aminobutyric-containing and serotonergic neurons. GDNF may have utility in the treatment of Parkinson's disease, which is marked by progressive degeneration of midbrain dopaminergic neurons.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lin, L F -- Doherty, D H -- Lile, J D -- Bektesh, S -- Collins, F -- New York, N.Y. -- Science. 1993 May 21;260(5111):1130-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Synergen, Inc., Boulder, CO 80301.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8493557" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Astrocytes/cytology/drug effects ; Base Sequence ; Cell Differentiation/drug effects ; Cell Line ; Cell Survival/drug effects ; Cells, Cultured ; Cloning, Molecular ; Dopamine/*biosynthesis ; Glial Cell Line-Derived Neurotrophic Factor ; Humans ; Mesencephalon/cytology/*drug effects/metabolism ; Molecular Sequence Data ; Molecular Weight ; *Nerve Growth Factors ; Nerve Tissue Proteins/chemistry/genetics/isolation & purification/*pharmacology ; Neuroglia/*metabolism ; Neurons/cytology/*drug effects/metabolism ; Parkinson Disease/drug therapy ; Rats
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  • 15
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    IL-6-induced homodimerization of gp130 and associated activation of a tyrosine kinase (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-06-18
    Description: The biological functions of interleukin-6 (IL-6) are mediated through a signal-transducing component of the IL-6 receptor, gp130, which is associated with the ligand-occupied IL-6 receptor (IL-6R) protein. Binding of IL-6 to IL-6R induced disulfide-linked homodimerization of gp130. Tyrosine kinase activity was associated with dimerized but not monomeric gp130 protein. Substitution of serine for proline residues 656 and 658 in the cytoplasmic motif abolished tyrosine kinase activation and cellular responses but not homodimerization of gp130. The IL-6-induced gp130 homodimer appears to be similar in function to the heterodimer formed between the leukemia inhibitory factor (LIF) receptor (LIFR) and gp130 in response to the LIF or ciliary neurotrophic factor (CNTF). Thus, a general first step in IL-6-related cytokine signaling may be the dimerization of signal-transducing molecules and activation of associated tyrosine kinases.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Murakami, M -- Hibi, M -- Nakagawa, N -- Nakagawa, T -- Yasukawa, K -- Yamanishi, K -- Taga, T -- Kishimoto, T -- New York, N.Y. -- Science. 1993 Jun 18;260(5115):1808-10.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute for Molecular and Cellular Biology, Osaka University, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8511589" target="_blank"〉PubMed〈/a〉
    Keywords: *Antigens, CD ; Cytokine Receptor gp130 ; Enzyme Activation ; Haptoglobins/biosynthesis ; Humans ; Interleukin-6/*metabolism/pharmacology ; Macromolecular Substances ; Membrane Glycoproteins/chemistry/*metabolism ; Phosphorylation ; Protein-Tyrosine Kinases/*metabolism ; Receptors, Immunologic/*metabolism ; Receptors, Interleukin-6 ; *Signal Transduction ; Transfection ; Tumor Cells, Cultured
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  • 16
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    Molecular cloning of an apolipoprotein B messenger RNA editing protein (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-06-18
    Description: Mammalian apolipoprotein B (apo B) exists in two forms, each the product of a single gene. The shorter form, apo B48, arises by posttranscriptional RNA editing whereby cytidine deamination produces a UAA termination codon. A full-length complementary DNA clone encoding an apo B messenger RNA editing protein (REPR) was isolated from rat small intestine. The 229-residue protein contains consensus phosphorylation sites and leucine zipper domains. HepG2 cell extracts acquire editing activity when mixed with REPR from oocyte extracts. REPR is essential for apo B messenger RNA editing, and the isolation and characterization of REPR may lead to the identification of other eukaryotic RNA editing proteins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Teng, B -- Burant, C F -- Davidson, N O -- DK-42086/DK/NIDDK NIH HHS/ -- HL-38180/HL/NHLBI NIH HHS/ -- KO-4 HL-02166/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1993 Jun 18;260(5115):1816-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine, University of Chicago, IL 60637.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8511591" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Apolipoproteins B/*genetics ; Base Sequence ; Cell Line ; *Cloning, Molecular ; Cytidine Deaminase/chemistry/*genetics ; Humans ; Intestine, Small/chemistry ; Leucine Zippers ; Molecular Sequence Data ; Molecular Weight ; Open Reading Frames ; Phosphorylation ; *RNA Editing ; Rats ; Tumor Cells, Cultured
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 17
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    Dormancy of inhibitory interneurons in a model of temporal lobe epilepsy (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-01-01
    Description: In humans temporal lobe epilepsy (TLE) is characterized by recurrent seizures, neuronal hyperexcitability, and selective loss of certain neuronal populations in the hippocampus. Animal models of the condition indicate that a diminution of inhibition mediated by gamma-aminobutyric acid (GABA) accounts for the altered function, and it has been hypothesized that the diminution arises because GABAergic basket interneurons are "dormant" as a result of their being disconnected from excitatory inputs. In hippocampal slices, inhibitory postsynaptic potentials (IPSPs) were elicited in CA1 pyramidal cells by activation of basket cells; responses from an animal model of TLE were compared to those from control tissue. IPSPs evoked indirectly by activation of terminals that then excited basket cells were reduced in the epileptic tissue, whereas IPSPs evoked by direct activation of basket cells, when excitatory neurotransmission was blocked, were not different from controls. These results provide support for the "dormant basket cell" hypothesis and have implications for the pathophysiology and treatment of human TLE.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bekenstein, J W -- Lothman, E W -- New York, N.Y. -- Science. 1993 Jan 1;259(5091):97-100.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurology, University of Virginia Health Sciences Center, Charlottesville 22908.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8093417" target="_blank"〉PubMed〈/a〉
    Keywords: 6-Cyano-7-nitroquinoxaline-2,3-dione ; Action Potentials ; Animals ; Baclofen/analogs & derivatives/pharmacology ; Electric Stimulation ; Epilepsy, Temporal Lobe/*physiopathology ; Evoked Potentials ; Hippocampus/*physiology/*physiopathology ; In Vitro Techniques ; Interneurons/drug effects/*physiology ; Male ; Membrane Potentials ; Picrotoxin/pharmacology ; Pyramidal Tracts/drug effects/*physiology ; Quinoxalines/pharmacology ; Rats ; Rats, Sprague-Dawley ; Receptors, GABA-A/physiology ; Receptors, N-Methyl-D-Aspartate/physiology ; Status Epilepticus/*physiopathology
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  • 18
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    Tumor rejection after direct costimulation of CD8+ T cells by B7-transfected melanoma cells (1993)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1993-01-15
    Description: A variety of tumors are potentially immunogenic but do not stimulate an effective anti-tumor immune response in vivo. Tumors may be capable of delivering antigen-specific signals to T cells, but may not deliver the costimulatory signals necessary for full activation of T cells. Expression of the costimulatory ligand B7 on melanoma cells was found to induce the rejection of a murine melanoma in vivo. This rejection was mediated by CD8+ T cells; CD4+ T cells were not required. These results suggest that B7 expression renders tumor cells capable of effective antigen presentation, leading to their eradication in vivo.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Townsend, S E -- Allison, J P -- CA57986/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1993 Jan 15;259(5093):368-70.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Cell Biology, University of California, Berkeley 94720.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7678351" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigen-Presenting Cells/immunology ; Antigens, CD80 ; Antigens, Surface/genetics/*immunology ; CD4-Positive T-Lymphocytes/immunology ; Cross Reactions ; Female ; Gene Expression Regulation ; Genetic Vectors ; Ligands ; *Lymphocyte Activation ; Melanoma/*immunology ; Mice ; Mice, Inbred BALB C ; Mice, Inbred C3H ; Mice, Nude ; T-Lymphocytes, Regulatory/*immunology ; Transfection ; Tumor Cells, Cultured
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 19
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    Primers for mitochondrial DNA replication generated by endonuclease G (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-08-06
    Description: Endonuclease G (Endo G) is widely distributed among animals and cleaves DNA at double-stranded (dG)n.(dC)n and at single-stranded (dC)n tracts. Endo G is synthesized as a propeptide with an amino-terminal presequence that targets the nuclease to mitochondria. Endo G can also be detected in extranucleolar chromatin. In addition to deoxyribonuclease activities, Endo G also has ribonuclease (RNase) and RNase H activities and specifically cleaves mouse mitochondrial RNA and DNA-RNA substrates containing the origin of heavy-strand DNA replication (OH). The cleavage sites match those found in vivo, indicating that Endo G is capable of generating the RNA primers required by DNA polymerase gamma to initiate replication of mitochondrial DNA.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cote, J -- Ruiz-Carrillo, A -- New York, N.Y. -- Science. 1993 Aug 6;261(5122):765-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cancer Research Center, Medical School of Laval University, L'Hotel-Dieu de Quebec, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7688144" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Cell Line ; Cell Nucleus/enzymology ; DNA/genetics ; *DNA Replication ; DNA, Mitochondrial/*metabolism ; Endodeoxyribonucleases/chemistry/genetics/*metabolism ; Genetic Vectors ; Mitochondria/enzymology ; Molecular Sequence Data ; RNA/*metabolism ; Ribonuclease H/metabolism ; Ribonucleases/metabolism ; Transfection
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  • 20
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    Enhancement by histamine of NMDA-mediated synaptic transmission in the hippocampus (1993)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1993-07-02
    Description: Histamine is a neuromodulator in the brain, and the hippocampus is one of the regions of the brain that is innervated by histaminergic neurons. When applied to cultured hippocampal neurons, histamine selectively increased by up to tenfold the amplitude of the component of synaptic transmission that was mediated by N-methyl-D-aspartate (NMDA) receptors. Spontaneous miniature synaptic currents and the current elicited by applied NMDA also were enhanced, indicating that the histamine effect was expressed primarily postsynaptically. These results suggest that histamine may modulate processes involving NMDA receptors, such as the induction of long-term potentiation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bekkers, J M -- New York, N.Y. -- Science. 1993 Jul 2;261(5117):104-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Neuroscience, John Curtin School of Medical Research, Australian National Univresity, Canberra, ACT.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8391168" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Animals, Newborn ; Cells, Cultured ; Guanosine 5'-O-(3-Thiotriphosphate)/pharmacology ; Hippocampus/cytology/drug effects/*physiology ; Histamine/*pharmacology ; Ion Channel Gating/drug effects ; N-Methylaspartate/*metabolism/pharmacology ; Rats ; Receptors, Histamine/physiology ; Receptors, N-Methyl-D-Aspartate/metabolism ; Synapses/*physiology ; Synaptic Transmission/*drug effects ; Virulence Factors, Bordetella/pharmacology
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  • 21
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    Complexes of Ras.GTP with Raf-1 and mitogen-activated protein kinase kinase (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-06-11
    Description: The guanosine triphosphate (GTP)-binding protein Ras functions in regulating growth and differentiation; however, little is known about the protein interactions that bring about its biological activity. Wild-type Ras or mutant forms of Ras were covalently attached to an insoluble matrix and then used to examine the interaction of signaling proteins with Ras. Forms of Ras activated either by mutation (Gly12Val) or by binding of the GTP analog, guanylyl-imidodiphosphate (GMP-PNP) interacted specifically with Raf-1 whereas an effector domain mutant, Ile36Ala, failed to interact with Raf-1. Mitogen-activated protein kinase (MAP kinase) activity was only associated with activated forms of Ras. The specific interaction of activated Ras with active MAP kinase kinase (MAPKK) was confirmed by direct assays. Thus the forming of complexes containing MAPKK activity and Raf-1 protein are dependent upon the activity of Ras.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Moodie, S A -- Willumsen, B M -- Weber, M J -- Wolfman, A -- CA 39076/CA/NCI NIH HHS/ -- CA 40042/CA/NCI NIH HHS/ -- GM 41220/GM/NIGMS NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1993 Jun 11;260(5114):1658-61.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology, Cleveland Clinic Foundation, OH 44106.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8503013" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Brain/metabolism ; Guanosine Triphosphate/*metabolism ; Guanylyl Imidodiphosphate/metabolism ; In Vitro Techniques ; Mitogen-Activated Protein Kinase 1 ; Mitogen-Activated Protein Kinase Kinases ; Mutation ; Phosphorylation ; Protein Binding ; Protein Kinases/*metabolism ; Protein-Serine-Threonine Kinases/metabolism ; Protein-Tyrosine Kinases/metabolism ; Proto-Oncogene Proteins/*metabolism ; Proto-Oncogene Proteins c-raf ; Proto-Oncogene Proteins p21(ras)/*metabolism ; Rats ; Signal Transduction/physiology
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  • 22
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    Interleukin-2 receptor gamma chain: a functional component of the interleukin-4 receptor (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-12-17
    Description: The interleukin-2 (IL-2) receptor gamma chain (IL-2R gamma) is an essential component of high- and intermediate-affinity IL-2 receptors. IL-2R gamma was demonstrated to be a component of the IL-4 receptor on the basis of chemical cross-linking data, the ability of IL-2R gamma to augment IL-4 binding affinity, and the requirement for IL-2R gamma in IL-4-mediated phosphorylation of insulin receptor substrate-1. The observation that IL-2R gamma is a functional component of the IL-4 receptor, together with the finding that IL-2R gamma associates with the IL-7 receptor, begins to elucidate why deficiency of this common gamma chain (gamma c) has a profound effect on lymphoid function and development, as seen in X-linked severe combined immunodeficiency.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Russell, S M -- Keegan, A D -- Harada, N -- Nakamura, Y -- Noguchi, M -- Leland, P -- Friedmann, M C -- Miyajima, A -- Puri, R K -- Paul, W E -- New York, N.Y. -- Science. 1993 Dec 17;262(5141):1880-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Section on Pulmonary and Molecular Immunology, National Heart, Lung, and Blood Institute, NIH, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8266078" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Cell Line ; Cell Line, Transformed ; Genetic Linkage ; Humans ; Insulin Receptor Substrate Proteins ; Interleukin-4/metabolism ; L Cells (Cell Line) ; Mice ; Molecular Sequence Data ; Phosphoproteins/metabolism ; Phosphorylation ; Receptors, Interleukin-2/chemistry/genetics/*metabolism ; Receptors, Interleukin-4 ; Receptors, Mitogen/chemistry/genetics/*metabolism ; Severe Combined Immunodeficiency/genetics/immunology ; Signal Transduction ; Transfection ; X Chromosome
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  • 23
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    GABA-activated chloride channels in secretory nerve endings (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-01-22
    Description: Neurotransmitters acting on presynaptic terminals regulate synaptic transmission and plasticity. Because of the difficulty of direct electrophysiological recording from small presynaptic terminals, little is known about the ion channels that mediate these actions or about the mechanisms by which transmitter secretion is altered. The patch-clamp technique is used to show that the predominant inhibitory presynaptic neurotransmitter, gamma-aminobutyric acid (GABA), activates a GABAA receptor and gates a chloride channel in the membranes of peptidergic nerve terminals of the posterior pituitary. The opening of a chloride channel by GABA weakly depolarizes the nerve terminal membrane and blocks action potentials. In this way, GABA limits secretion by retarding the spread of excitation into the terminal arborization.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zhang, S J -- Jackson, M B -- NS30016/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1993 Jan 22;259(5094):531-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physiology, University of Wisconsin Medical School, Madison 53706.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8380942" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Bicuculline/pharmacology ; Chlordiazepoxide/pharmacology ; Chloride Channels ; Chlorides/*metabolism ; GABA-A Receptor Antagonists ; Male ; Membrane Potentials/drug effects ; Membrane Proteins/drug effects/*physiology ; Muscimol/pharmacology ; Nerve Endings/drug effects/*physiology ; Picrotoxin/pharmacology ; Pituitary Gland, Posterior/drug effects/*physiology ; Rats ; Receptors, GABA-A/*physiology ; gamma-Aminobutyric Acid/*pharmacology
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 24
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    New test catches drug-resistant TB in the spotlight (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-05-07
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Barinaga, M -- New York, N.Y. -- Science. 1993 May 7;260(5109):750.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8484114" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphate/metabolism ; Antitubercular Agents/*pharmacology ; Drug Resistance, Microbial ; Luciferases/genetics/metabolism ; *Luminescent Measurements ; Microbial Sensitivity Tests/*methods ; Mycobacterium tuberculosis/*drug effects/genetics/metabolism ; Transfection
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  • 25
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    Naked DNA points way to vaccines (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-03-19
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cohen, J -- New York, N.Y. -- Science. 1993 Mar 19;259(5102):1691-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8456293" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; DNA, Viral/*genetics/therapeutic use ; Influenza A virus/*genetics/immunology ; Mice ; Nucleoproteins/genetics/immunology ; Orthomyxoviridae Infections/*prevention & control ; *RNA-Binding Proteins ; Transfection ; Viral Core Proteins/genetics/immunology ; Viral Vaccines/*genetics
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  • 26
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    Regulation of V(D)J recombination activator protein RAG-2 by phosphorylation (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-05-14
    Description: Antigen receptor genes are assembled by site-specific DNA rearrangement. The recombination activator genes RAG-1 and RAG-2 are essential for this process, termed V(D)J rearrangement. The activity and stability of the RAG-2 protein have now been shown to be regulated by phosphorylation. In fibroblasts RAG-2 was phosphorylated predominantly at two serine residues, one of which affected RAG-2 activity in vivo. The threonine at residue 490 was phosphorylated by p34cdc2 kinase in vitro; phosphorylation at this site in vivo was associated with rapid degradation of RAG-2. Instability was transferred to chimeric proteins by a 90-residue portion of RAG-2. Mutation of the p34cdc2 phosphorylation site of the tumor suppressor protein p53 conferred a similar phenotype, suggesting that this association between phosphorylation and degradation is a general mechanism.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lin, W C -- Desiderio, S -- CA16519/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1993 May 14;260(5110):953-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology and Genetics, Johns Hopkins University School of Medicine, Baltimore, MD 21205.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8493533" target="_blank"〉PubMed〈/a〉
    Keywords: 3T3 Cells ; Amino Acid Sequence ; Animals ; CDC2 Protein Kinase/metabolism ; Cell Line ; *DNA-Binding Proteins ; *Gene Rearrangement ; Humans ; Mice ; Molecular Sequence Data ; Mutation ; Nuclear Proteins ; Phosphorylation ; Proteins/chemistry/genetics/*metabolism ; Receptors, Antigen/*genetics ; Recombinant Fusion Proteins/metabolism ; Transfection ; Tumor Suppressor Protein p53/genetics
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    Association between brain temperature and dentate field potentials in exploring and swimming rats (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-02-26
    Description: Attempts to correlate behavioral learning with cellular changes, such as increased synaptic efficacy, have often relied on increased extracellular potentials as an index of enhanced synaptic strength. A recent example is the enlarged excitatory field potentials in the dentate gyrus of rats that are learning spatial relations by exploration. The altered hippocampal field potentials do not reflect learning-specific cellular changes but result from a concomitant rise in brain temperature that is caused by the associated muscular effort. Enhanced dentate field excitatory potentials followed both passive and active heating and were linearly related to the brain temperature. These temperature-related effects may mask any learning-induced changes in field potential.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Moser, E -- Mathiesen, I -- Andersen, P -- New York, N.Y. -- Science. 1993 Feb 26;259(5099):1324-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurophysiology, University of Oslo, Norway.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8446900" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Behavior, Animal/physiology ; Body Temperature ; Cerebellar Nuclei/*physiology ; Hippocampus/*physiology ; Male ; Membrane Potentials ; Physical Exertion ; Rats ; Swimming/physiology
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    Presentation of a viral T cell epitope expressed in the CDR3 region of a self immunoglobulin molecule (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-01-08
    Description: Synthetic peptides corresponding to microbial epitopes stimulate T cell immunity but their immunogenicity is poor and their half-lives are short. A viral epitope inserted into the complementarity-determining region 3 (CDR3) loop of the heavy chain of a self immunoglobulin (Ig) molecule was generated from the Ig context and was presented by I-Ed class II molecules to virus-specific, CD4+ T cells. Chimeric Ig-peptide was presented 100 to 1000 times more efficiently than free synthetic peptide and was able to prime virus-specific T cells in vivo. These features suggest that antigenized Ig can provide an improved and safe vaccine for the presentation of microbial and other peptides.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zaghouani, H -- Steinman, R -- Nonacs, R -- Shah, H -- Gerhard, W -- Bona, C -- AI13013/AI/NIAID NIH HHS/ -- AI18316/AI/NIAID NIH HHS/ -- AI24460/AI/NIAID NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1993 Jan 8;259(5092):224-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology, Mount Sinai School of Medicine, New York, NY 10029.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7678469" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antigen-Presenting Cells/*immunology ; Antigens, Viral/*immunology ; Arsenic/immunology ; *Arsenicals ; Base Sequence ; CD4-Positive T-Lymphocytes/immunology ; DNA/genetics ; Epitopes/*immunology ; Hemagglutinin Glycoproteins, Influenza Virus ; Hemagglutinins, Viral/genetics/immunology ; Histocompatibility Antigens Class II/immunology ; Immunoglobulin Heavy Chains/genetics/immunology ; Immunoglobulin Variable Region/genetics/immunology ; Immunoglobulins/genetics/*immunology ; Mice ; Mice, Inbred BALB C ; Molecular Sequence Data ; Mutagenesis ; Receptors, Fc/immunology ; Recombinant Fusion Proteins/immunology ; Transfection
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    Rat annexin V crystal structure: Ca(2+)-induced conformational changes (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-09-03
    Description: Annexins are a family of calcium- and phospholipid-binding proteins implicated in mediating membrane-related processes such as secretion, signal transduction, and ion channel activity. The crystal structure of rat annexin V was solved to 1.9 angstrom resolution by multiple isomorphous replacement. Unlike previously solved annexin V structures, all four domains bound calcium in this structure. Calcium binding in the third domain induced a large relocation of the calcium-binding loop regions, exposing the single tryptophan residue to the solvent. These alterations in annexin V suggest a role for domain 3 in calcium-triggered interaction with phospholipid membranes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Concha, N O -- Head, J F -- Kaetzel, M A -- Dedman, J R -- Seaton, B A -- R01-DK-41740/DK/NIDDK NIH HHS/ -- R01-NS-20357/NS/NINDS NIH HHS/ -- R29-GM-44554/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1993 Sep 3;261(5126):1321-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physiology, Boston University School of Medicine, MA 02118.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8362244" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Annexin A5/*chemistry/metabolism ; Binding Sites ; Calcium/*metabolism ; Computer Graphics ; Crystallization ; Humans ; Hydrogen Bonding ; Molecular Sequence Data ; Protein Conformation ; Rats ; Sequence Alignment ; Tryptophan/chemistry ; X-Ray Diffraction
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    Generation of a mouse strain that produces immunoglobulin kappa chains with human constant regions (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-11-19
    Description: Humanized antibodies are highly efficient as immunotherapeutic reagents and have many advantages over rodent antibodies. A mouse strain was generated by gene targeting to replace the mouse kappa light chain constant (C) region gene with the human C kappa gene. Mice homozygous for the replacement mutation (C kappa R) produced normal concentrations of serum antibodies, most of which carry chimeric kappa light chains, and mounted normal immune responses to hapten-protein conjugates. This technology provides a feasible option for the generation of high-affinity humanized antibodies by means of the powerful somatic hypermutation-selection mechanism.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zou, Y R -- Gu, H -- Rajewsky, K -- New York, N.Y. -- Science. 1993 Nov 19;262(5137):1271-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute for Genetics, University of Cologne, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8235658" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; B-Lymphocytes/*immunology ; Base Sequence ; Gene Rearrangement ; *Genes, Immunoglobulin ; Humans ; Immunoglobulin Constant Regions/*biosynthesis/genetics ; Immunoglobulin Isotypes/biosynthesis ; Immunoglobulin kappa-Chains/*biosynthesis/genetics ; Mice ; Mice, Transgenic ; Molecular Sequence Data ; Mutation ; Polymerase Chain Reaction ; Recombinant Fusion Proteins/biosynthesis ; Stem Cells ; Transfection
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    Delivery of Na+,K(+)-ATPase in polarized epithelial cells (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-04-23
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zurzolo, C -- Rodriguez-Boulan, E -- GM 34107/GM/NIGMS NIH HHS/ -- R01 GM034107/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1993 Apr 23;260(5107):550-2; author reply 554-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8386394" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Line ; Cell Membrane/*enzymology ; *Cell Polarity ; Epithelial Cells ; Rats ; *Sodium-Potassium-Exchanging ATPase/*metabolism
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    Cure of xenografted human carcinomas by BR96-doxorubicin immunoconjugates (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-07-09
    Description: Immunoconjugates (BR96-DOX) were prepared between chimeric monoclonal antibody BR96 and the anticancer drug doxorubicin. The monoclonal antibody binds an antigen related to Lewis Y that is abundantly expressed at the surface of cells from many human carcinomas; it has a high degree of tumor selectivity and is internalized after binding. BR96-DOX induced complete regressions and cures of xenografted human lung, breast, and colon carcinomas growing subcutaneously in athymic mice and cured 70 percent of mice bearing extensive metastases of a human lung carcinoma. Also, BR96-DOX cured 94 percent of athymic rats with subcutaneous human lung carcinoma, even though the rats, like humans and in contrast to mice, expressed the BR96 target antigen in normal tissues.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Trail, P A -- Willner, D -- Lasch, S J -- Henderson, A J -- Hofstead, S -- Casazza, A M -- Firestone, R A -- Hellstrom, I -- Hellstrom, K E -- New York, N.Y. -- Science. 1993 Jul 9;261(5118):212-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Bristol-Myers Squibb Pharmaceutical Research Institute, Princeton, NJ 08543.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8327892" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antibodies, Monoclonal/administration & dosage/immunology/*therapeutic use ; Antigens, Neoplasm/immunology ; Antigens, Surface/immunology ; Breast Neoplasms/drug therapy ; Colonic Neoplasms/drug therapy ; Doxorubicin/administration & dosage/*therapeutic use ; Humans ; Immunotoxins/administration & dosage/*therapeutic use ; Lung Neoplasms/drug therapy ; Mice ; Mice, Nude ; Neoplasm Transplantation ; Neoplasms, Experimental/*drug therapy ; Rats ; Rats, Nude
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    Optical time-of-flight and absorbance imaging of biologic media (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-03-05
    Description: Imaging the interior of living bodies with light may assist in the diagnosis and treatment of a number of clinical problems, which include the early detection of tumors and hypoxic cerebral injury. An existing picosecond time-of-flight and absorbance (TOFA) optical system has been used to image a model biologic system and a rat. Model measurements confirmed TOFA principles in systems with a high degree of photon scattering; rat images, which were constructed from the variable time delays experienced by a fixed fraction of early-arriving transmitted photons, revealed identifiable internal structure. A combination of light-based quantitative measurement and TOFA localization may have applications in continuous, noninvasive monitoring for structural imaging and spatial chemometric analysis in humans.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Benaron, D A -- Stevenson, D K -- RR-00081/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 1993 Mar 5;259(5100):1463-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pediatrics, Stanford University School of Medicine, Palo Alto, CA 94305.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8451643" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Humans ; Light ; Models, Theoretical ; Radiation ; Rats ; Spectrophotometry/instrumentation/*methods ; Time Factors
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    Interleukin-2 receptor gamma chain: a functional component of the interleukin-7 receptor (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-12-17
    Description: The interleukin-2 receptor gamma chain (IL-2R gamma) is a necessary component of functional IL-2 receptors. IL-2R gamma mutations result in X-linked severe combined immunodeficiency (XSCID) in humans, a disease characterized by the presence of few or no T cells. In contrast, SCID patients with IL-2 deficiency and IL-2-deficient mice have normal numbers of T cells, suggesting that IL-2R gamma is part of more than one cytokine receptor. By using chemical cross-linking, IL-2R gamma was shown to be physically associated with the IL-7 receptor. The presence of IL-2R gamma augmented both IL-7 binding affinity and the efficiency of internalization of IL-7. These findings may help explain the defects of XSCID. Given its role in more than one cytokine receptor system, the common gamma chain (gamma c) is proposed as the designation for IL-2R gamma.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Noguchi, M -- Nakamura, Y -- Russell, S M -- Ziegler, S F -- Tsang, M -- Cao, X -- Leonard, W J -- New York, N.Y. -- Science. 1993 Dec 17;262(5141):1877-80.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Section on Pulmonary and Molecular Immunology, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8266077" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; B-Lymphocytes/immunology ; Cell Line ; Genetic Linkage ; Interleukin-7/*metabolism ; L Cells (Cell Line) ; Mice ; Receptors, Interleukin/chemistry/genetics/*metabolism ; Receptors, Interleukin-2/chemistry/genetics/*metabolism ; Receptors, Interleukin-7 ; Severe Combined Immunodeficiency/genetics/immunology ; T-Lymphocytes/immunology ; Transfection ; X Chromosome
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    Interaction between transcription regulatory regions of prolactin chromatin (1993)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1993-07-09
    Description: The regulation of transcription requires complex interactions between proteins bound to DNA sequences that are often separated by hundreds of base pairs. As demonstrated by a nuclear ligation assay, the distal enhancer and the proximal promoter regions of the rat prolactin gene were found to be juxtaposed. By acting through its receptor bound to the distal enhancer, estrogen stimulated the interaction between the distal and proximal regulatory regions two- to threefold compared to control values. Thus, the chromatin structure of the prolactin gene may facilitate the occurrence of protein-protein interactions between transcription factors bound to widely separated regulatory elements.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cullen, K E -- Kladde, M P -- Seyfred, M A -- DK42731/DK/NIDDK NIH HHS/ -- T32HD07048/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 1993 Jul 9;261(5118):203-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, Vanderbilt University, Nashville, TN 37235.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8327891" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Cell Line ; Cell Nucleus/metabolism ; Chromatin/*chemistry/metabolism ; DNA/chemistry/metabolism ; Deoxyribonucleases, Type II Site-Specific ; *Enhancer Elements, Genetic ; Estrogens/metabolism ; Molecular Sequence Data ; Oligodeoxyribonucleotides ; Polymerase Chain Reaction ; Prolactin/*genetics ; *Promoter Regions, Genetic ; Protein Conformation ; Protein Folding ; Rats ; Receptors, Estrogen/metabolism ; Regulatory Sequences, Nucleic Acid ; *Transcription, Genetic
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    Antagonism of catecholamine receptor signaling by expression of cytoplasmic domains of the receptors (1993)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1993-03-05
    Description: The actions of many hormones and neurotransmitters are mediated by the members of a superfamily of receptors coupled to heterotrimeric guanine nucleotide-binding proteins (G proteins). These receptors are characterized by a highly conserved topographical arrangement in which seven transmembrane domains are connected by intracellular and extracellular loops. The interaction between these receptors and G proteins is mediated in large part by the third intracellular loop of the receptor. Coexpression of the third intracellular loop of the alpha 1B-adrenergic receptor with its parent receptor inhibited receptor-mediated activation of phospholipase C. The inhibition extended to the closely related alpha 1C-adrenergic receptor subtype, but not the phospholipase C-coupled M1 muscarinic acetylcholine receptor nor the adenylate cyclase-coupled D1A dopamine receptor. These results suggest that the receptor-G protein interface may represent a target for receptor antagonist drugs.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Luttrell, L M -- Ostrowski, J -- Cotecchia, S -- Kendall, H -- Lefkowitz, R J -- HL16037/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1993 Mar 5;259(5100):1453-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine, Duke University Medical Center, Durham, NC 27710.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8383880" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Cell Line ; Cloning, Molecular ; Cyclic AMP/metabolism ; Cytoplasm/metabolism ; GTP-Binding Proteins/*metabolism ; Globins/genetics ; Glutathione Transferase/genetics/metabolism ; Humans ; Inositol Phosphates/metabolism ; Kinetics ; Molecular Sequence Data ; Muscarinic Antagonists ; Oligodeoxyribonucleotides ; Plasmids ; Protein Structure, Secondary ; Receptors, Adrenergic, alpha/genetics/*metabolism ; Receptors, Dopamine D1/antagonists & inhibitors/genetics/*metabolism ; Receptors, Muscarinic/genetics/*metabolism ; Recombinant Fusion Proteins/metabolism ; *Signal Transduction ; Transfection ; Type C Phospholipases/metabolism
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    Inhibition of viral replication by interferon-gamma-induced nitric oxide synthase (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-09-10
    Description: Interferons (IFNs) induce antiviral activity in many cell types. The ability of IFN-gamma to inhibit replication of ectromelia, vaccinia, and herpes simplex-1 viruses in mouse macrophages correlated with the cells' production of nitric oxide (NO). Viral replication was restored in IFN-gamma-treated macrophages exposed to inhibitors of NO synthase. Conversely, epithelial cells with no detectable NO synthesis restricted viral replication when transfected with a complementary DNA encoding inducible NO synthase or treated with organic compounds that generate NO. In mice, an inhibitor of NO synthase converted resolving ectromelia virus infection into fulminant mousepox. Thus, induction of NO synthase can be necessary and sufficient for a substantial antiviral effect of IFN-gamma.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Karupiah, G -- Xie, Q W -- Buller, R M -- Nathan, C -- Duarte, C -- MacMicking, J D -- CA43610/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1993 Sep 10;261(5127):1445-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Viral Diseases, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7690156" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Oxidoreductases/*biosynthesis/metabolism ; Animals ; Arginine/analogs & derivatives/pharmacology ; Cell Line ; Cells, Cultured ; Ectromelia virus/drug effects/*physiology ; Ectromelia, Infectious/microbiology ; Enzyme Induction ; Female ; Humans ; Interferon-gamma/*pharmacology ; Macrophages/*microbiology ; Mice ; Mice, Inbred C57BL ; Nitric Oxide/metabolism/pharmacology ; Nitric Oxide Synthase ; Simplexvirus/drug effects/physiology ; Transfection ; Vaccinia virus/drug effects/physiology ; *Virus Replication/drug effects ; omega-N-Methylarginine
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    Biologists visit New Orleans (under an assumed name) (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-04-09
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Travis, J -- New York, N.Y. -- Science. 1993 Apr 9;260(5105):162-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8469970" target="_blank"〉PubMed〈/a〉
    Keywords: Aging/drug effects ; Animals ; Colonic Neoplasms/*genetics ; Flumazenil/*pharmacology ; *Genes, DCC ; Humans ; Memory/*drug effects ; Rats ; Societies, Scientific/organization & administration
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    The search for liver stem cells picks up (1993)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1993-03-26
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Travis, J -- New York, N.Y. -- Science. 1993 Mar 26;259(5103):1829.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8456311" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Differentiation ; Cell Division ; Humans ; Liver/*cytology ; Rats ; Stem Cells/*cytology
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    Malaria: focus on mosquito genes (1993)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1993-07-30
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Aldhous, P -- New York, N.Y. -- Science. 1993 Jul 30;261(5121):546-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8393586" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Animals, Genetically Modified ; Anopheles/*genetics/parasitology ; DNA Transposable Elements ; *Genes, Insect ; Genetic Engineering ; Humans ; Insect Vectors/*genetics/parasitology ; Malaria/*prevention & control/transmission ; Plasmodium/*physiology ; Transfection
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Multiple defects of immune cell function in mice with disrupted interferon-gamma genes (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-03-19
    Description: Interferon-gamma (IFN-gamma) is a pleiotrophic cytokine with immunomodulatory effects on a variety of immune cells. Mice with a targeted disruption of the IFN-gamma gene were generated. These mice developed normally and were healthy in the absence of pathogens. However, mice deficient in IFN-gamma had impaired production of macrophage antimicrobial products and reduced expression of macrophage major histocompatibility complex class II antigens. IFN-gamma-deficient mice were killed by a sublethal dose of the intracellular pathogen Mycobacterium bovis. Splenocytes exhibited uncontrolled proliferation in response to mitogen and alloantigen. After a mixed lymphocyte reaction, T cell cytolytic activity was enhanced against allogeneic target cells. Resting splenic natural killer cell activity was reduced in IFN-gamma-deficient mice. Thus, IFN-gamma is essential for the function of several cell types of the murine immune system.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dalton, D K -- Pitts-Meek, S -- Keshav, S -- Figari, I S -- Bradley, A -- Stewart, T A -- New York, N.Y. -- Science. 1993 Mar 19;259(5102):1739-42.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Genentech Inc., South San Francisco, CA 94080.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8456300" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Division ; Cytotoxicity, Immunologic ; Histocompatibility Antigens Class II/immunology ; *Immunity ; Interferon-gamma/*genetics/physiology ; Isoantigens/immunology ; Killer Cells, Natural/immunology ; Lymphocyte Culture Test, Mixed ; Macrophages/immunology ; Mice ; Mice, Inbred C57BL ; Mice, Transgenic ; Mutation ; Mycobacterium bovis ; Nitric Oxide/metabolism ; Spleen/cytology/immunology ; T-Lymphocytes/immunology ; Transfection ; Tuberculosis/immunology
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Inhibition of transcriptional regulator Yin-Yang-1 by association with c-Myc (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-12-17
    Description: Yin-Yang-1 (YY1) regulates the transcription of many genes, including the oncogenes c-fos and c-myc. Depending on the context, YY1 acts as a transcriptional repressor, a transcriptional activator, or a transcriptional initiator. The yeast two-hybrid system was used to screen a human complementary DNA (cDNA) library for proteins that associate with YY1, and a c-myc cDNA was isolated. Affinity chromatography confirmed that YY1 associates with c-Myc but not with Max. In cotransfections, c-Myc inhibits both the repressor and the activator functions of YY1, which suggests that one way c-Myc acts is by modulating the activity of YY1.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shrivastava, A -- Saleque, S -- Kalpana, G V -- Artandi, S -- Goff, S P -- Calame, K -- CA 38571/CA/NCI NIH HHS/ -- GM29361/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1993 Dec 17;262(5141):1889-92.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Molecular Biophysics, Columbia University College of Physicians and Surgeons, New York, NY 10032.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8266081" target="_blank"〉PubMed〈/a〉
    Keywords: 3T3 Cells ; Adenovirus E1A Proteins/metabolism ; Animals ; Basic Helix-Loop-Helix Leucine Zipper Transcription Factors ; Basic-Leucine Zipper Transcription Factors ; DNA-Binding Proteins/antagonists & inhibitors/genetics/*metabolism/pharmacology ; Erythroid-Specific DNA-Binding Factors ; Helix-Loop-Helix Motifs ; Humans ; Mice ; Proto-Oncogene Proteins c-myc/*metabolism/pharmacology ; Recombinant Fusion Proteins/metabolism ; Transcription Factors/antagonists & inhibitors/genetics/*metabolism/pharmacology ; Transfection ; Tumor Cells, Cultured ; Upstream Stimulatory Factors ; YY1 Transcription Factor ; *Zinc Fingers
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    Heterologous protection against influenza by injection of DNA encoding a viral protein (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-03-19
    Description: Cytotoxic T lymphocytes (CTLs) specific for conserved viral antigens can respond to different strains of virus, in contrast to antibodies, which are generally strain-specific. The generation of such CTLs in vivo usually requires endogenous expression of the antigen, as occurs in the case of virus infection. To generate a viral antigen for presentation to the immune system without the limitations of direct peptide delivery or viral vectors, plasmid DNA encoding influenza A nucleoprotein was injected into the quadriceps of BALB/c mice. This resulted in the generation of nucleoprotein-specific CTLs and protection from a subsequent challenge with a heterologous strain of influenza A virus, as measured by decreased viral lung titers, inhibition of mass loss, and increased survival.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ulmer, J B -- Donnelly, J J -- Parker, S E -- Rhodes, G H -- Felgner, P L -- Dwarki, V J -- Gromkowski, S H -- Deck, R R -- DeWitt, C M -- Friedman, A -- New York, N.Y. -- Science. 1993 Mar 19;259(5102):1745-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cancer Research, Merck Research Laboratories, West Point, PA 19486.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8456302" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; DNA, Viral/*genetics/therapeutic use ; Gene Expression ; Genetic Vectors ; Histocompatibility Antigens Class I/immunology ; Immunization ; Influenza A virus/*genetics/immunology/isolation & purification ; Lung/microbiology ; Mice ; Mice, Inbred BALB C ; Molecular Sequence Data ; Muscles/metabolism ; Nucleoproteins/*genetics/*immunology ; Orthomyxoviridae Infections/microbiology/*prevention & control ; Plasmids ; *RNA-Binding Proteins ; T-Lymphocytes, Cytotoxic/immunology ; Transfection ; Viral Core Proteins/*genetics/*immunology ; Viral Vaccines/*genetics
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    NF-kappa B activation by ultraviolet light not dependent on a nuclear signal (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-09-10
    Description: Exposure of mammalian cells to radiation triggers the ultraviolet (UV) response, which includes activation of activator protein-1 (AP-1) and nuclear factor kappa B (NF-kappa B). This was postulated to occur by induction of a nuclear signaling cascade by damaged DNA. Recently, induction of AP-1 by UV was shown to be mediated by a pathway involving Src tyrosine kinases and the Ha-Ras small guanosine triphosphate-binding protein, proteins located at the plasma membrane. It is demonstrated here that the same pathway mediates induction of NF-kappa B by UV. Because inactive NF-kappa B is stored in the cytosol, analysis of its activation directly tests the involvement of a nuclear-initiated signaling cascade. Enucleated cells are fully responsive to UV both in NF-kappa B induction and in activation of another key signaling event. Therefore, the UV response does not require a signal generated in the nucleus and is likely to be initiated at or near the plasma membrane.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Devary, Y -- Rosette, C -- DiDonato, J A -- Karin, M -- CA50528/CA/NCI NIH HHS/ -- ES04151/ES/NIEHS NIH HHS/ -- New York, N.Y. -- Science. 1993 Sep 10;261(5127):1442-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, School of Medicine, University of California at San Diego, La Jolla 92093.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8367725" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Animals ; Catechols/pharmacology ; Cell Nucleus/*physiology ; Cytosol/metabolism ; Genes, ras ; Genes, src ; HeLa Cells ; Humans ; NF-kappa B/*metabolism/radiation effects ; Nitriles/pharmacology ; PC12 Cells ; Phosphatidylcholines/metabolism ; Protein-Tyrosine Kinases/metabolism ; Proto-Oncogene Proteins/genetics ; Proto-Oncogene Proteins c-jun/metabolism ; Proto-Oncogene Proteins c-raf ; Reactive Oxygen Species/metabolism ; Signal Transduction ; Tetradecanoylphorbol Acetate/pharmacology ; Transfection ; Tumor Necrosis Factor-alpha/pharmacology ; *Tyrphostins ; *Ultraviolet Rays
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    Action of antiulcer drugs (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-11-26
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Panula, P -- Wasowicz, K -- New York, N.Y. -- Science. 1993 Nov 26;262(5138):1454; author reply 1454-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8248787" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Anti-Ulcer Agents/pharmacology ; Gastric Mucosa/*chemistry ; Histidine Decarboxylase/analysis ; Macrophages/chemistry ; Oligonucleotide Probes ; Rats ; Receptors, Cell Surface/analysis ; Receptors, Histamine H2/*analysis
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    Crystal structure of domains 3 and 4 of rat CD4: relation to the NH2-terminal domains (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-05-14
    Description: The CD4 antigen is a membrane glycoprotein of T lymphocytes that interacts with major histocompatibility complex class II antigens and is also a receptor for the human immunodeficiency virus. the extracellular portion of CD4 is predicted to fold into four immunoglobulin-like domains. The crystal structure of the third and fourth domains of rat CD4 was solved at 2.8 angstrom resolution and shows that both domains have immunoglobulin folds. Domain 3, however, lacks the disulfide between the beta sheets; this results in an expansion of the domain. There is a difference of 30 degrees in the orientation between domains 3 and 4 when compared with domains 1 and 2. The two CD4 fragment structures provide a basis from which models of the overall receptor can be proposed. These models suggest an extended structure comprising two rigid portions joined by a short and possibly flexible linker region.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Brady, R L -- Dodson, E J -- Dodson, G G -- Lange, G -- Davis, S J -- Williams, A F -- Barclay, A N -- New York, N.Y. -- Science. 1993 May 14;260(5110):979-83.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, University of York, United Kingdom.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8493535" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antigens, CD4/*chemistry ; Crystallization ; Humans ; Models, Molecular ; Molecular Sequence Data ; Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Rats ; Sequence Alignment ; X-Ray Diffraction
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    Released form of CNTF receptor alpha component as a soluble mediator of CNTF responses (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-03-19
    Description: The alpha component of the receptor for ciliary neurotrophic factor (CNTF) differs from other known growth factor receptors in that it is anchored to cell membranes by a glycosylphosphatidylinositol linkage. One possible function of this type of linkage is to allow for the regulated release of this receptor component. Cell lines not normally responsive to CNTF responded to treatment with a combination of CNTF and a soluble form of the CNTF alpha receptor component. These findings not only demonstrate that the CNTF receptor alpha chain is a required component of the functional CNTF receptor complex but also reveal that it can function in soluble form as part of a heterodimeric ligand. Potential physiological roles for the soluble CNTF receptor are suggested by its presence in cerebrospinal fluid and by its release from skeletal muscle in response to peripheral nerve injury.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Davis, S -- Aldrich, T H -- Ip, N Y -- Stahl, N -- Scherer, S -- Farruggella, T -- DiStefano, P S -- Curtis, R -- Panayotatos, N -- Gascan, H -- New York, N.Y. -- Science. 1993 Mar 19;259(5102):1736-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Regeneron Pharmaceuticals, Inc., Tarrytown, NY 10591.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7681218" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Differentiation/drug effects ; Cell Division/drug effects ; Cell Membrane/metabolism ; Ciliary Neurotrophic Factor ; Cloning, Molecular ; Gene Expression ; Glycosylphosphatidylinositols/metabolism ; Growth Inhibitors/pharmacology ; Hematopoietic Stem Cells/cytology/drug effects ; Humans ; Interleukin-6/pharmacology ; Leukemia Inhibitory Factor ; Lymphokines/pharmacology ; Mice ; Muscle Denervation ; Muscles/innervation/metabolism ; Nerve Tissue Proteins/*pharmacology ; Phosphatidylinositol Diacylglycerol-Lyase ; Phosphoric Diester Hydrolases/metabolism ; Phosphotyrosine ; RNA, Messenger/genetics ; Rats ; Receptor, Ciliary Neurotrophic Factor ; Receptors, Cell Surface/chemistry/*physiology ; Signal Transduction/physiology ; Tumor Cells, Cultured ; Tyrosine/analogs & derivatives/metabolism
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    Beta-adrenergic receptor kinase-2 and beta-arrestin-2 as mediators of odorant-induced desensitization (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-02-05
    Description: beta-Adrenergic receptor kinase (beta ARK) and beta-arrestin function in the homologous or agonist-activated desensitization of G protein-coupled receptors. The isoforms beta ARK-2 and beta-arrestin-2 are highly enriched in and localized to the dendritic knobs and cilia of the olfactory receptor neurons where the initial events of olfactory signal transduction occur. Odorants induce a rapid and transient elevation of adenosine 3',5'-monophosphate (cAMP), which activates a nonspecific cation channel and produces membrane depolarization. Preincubation of rat olfactory cilia with antibodies raised against beta ARK-2 and beta-arrestin-2 increased the odorant-induced elevation of cAMP and attenuated desensitization. These results suggest that beta ARK-2 and beta-arrestin-2 mediate agonist-dependent desensitization in olfaction.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dawson, T M -- Arriza, J L -- Jaworsky, D E -- Borisy, F F -- Attramadal, H -- Lefkowitz, R J -- Ronnett, G V -- NS 01578-01/NS/NINDS NIH HHS/ -- NS-02131/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1993 Feb 5;259(5096):825-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neuroscience, Johns Hopkins Medical Institutions, Baltimore, MD 21205.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8381559" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens/*metabolism ; *Arrestins ; Cells, Cultured ; Cyclic AMP/metabolism ; *Cyclic AMP-Dependent Protein Kinases ; Cytosol/metabolism ; Dendrites/physiology ; Eye Proteins/*metabolism ; G-Protein-Coupled Receptor Kinase 2 ; GTP-Binding Proteins/*metabolism ; Isoenzymes/metabolism ; Male ; Mechanoreceptors/*physiology ; Neurons/*physiology ; *Odors ; Olfactory Bulb/*physiology ; Protein Kinases/*metabolism ; Rats ; Rats, Sprague-Dawley ; Receptors, Adrenergic, beta/*physiology ; Signal Transduction ; *Smell ; Testis/physiology ; Turbinates/*physiology ; beta-Adrenergic Receptor Kinases
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    Proliferation of human smooth muscle cells promoted by lipoprotein(a) (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-06-11
    Description: Elevated blood concentrations of lipoprotein(a) [Lp(a)] and its constituent, apolipoprotein(a) [apo(a)], constitute a major risk factor for atherosclerosis, but their physiological activities remain obscure. Lp(a) and purified apo(a) stimulated the growth of human smooth muscle cells in culture. This effect resulted from inhibition of plasminogen activation, and consequently the activation by plasmin of latent transforming growth factor-beta, which is an inhibitor of smooth muscle cell growth. Because smooth muscle proliferation is one of the hallmarks of atherosclerotic lesions, these results point to a plausible mechanism for the atherogenic activity of Lp(a).〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Grainger, D J -- Kirschenlohr, H L -- Metcalfe, J C -- Weissberg, P L -- Wade, D P -- Lawn, R M -- Wellcome Trust/United Kingdom -- New York, N.Y. -- Science. 1993 Jun 11;260(5114):1655-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, University of Cambridge, United Kingdom.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8503012" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Apolipoproteins/physiology ; Apoprotein(a) ; Cell Division/drug effects/physiology ; Cells, Cultured ; Fibrinolysin/physiology ; Humans ; Lipoprotein(a)/*physiology ; Muscle, Smooth, Vascular/*cytology/metabolism ; Plasminogen Activators/metabolism ; Rats ; Tamoxifen/pharmacology ; Transforming Growth Factor beta/physiology
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    Antisense gene inhibition by oligonucleotides containing C-5 propyne pyrimidines (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-06-04
    Description: Phosphorothioate oligodeoxynucleotides containing the C-5 propyne analogs of uridine and cytidine bind RNA with high affinity and are potent antisense inhibitors of gene expression. In a cellular assay, gene-specific antisense inhibition occurred at nanomolar concentrations of oligonucleotide, was dose-dependent and exquisitely sensitive to sequence mismatches, and was correlated with the melting temperature and length of oligonucleotide. Activity was independent of RNA target site and cell type but was detectable only when the oligonucleotides were microinjected or delivered with cell-permeabilizing agents. These oligonucleotides may have important applications in therapy and in studies of gene function.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wagner, R W -- Matteucci, M D -- Lewis, J G -- Gutierrez, A J -- Moulds, C -- Froehler, B C -- New York, N.Y. -- Science. 1993 Jun 4;260(5113):1510-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Gilead Sciences, Inc., Foster City, CA 94404.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7684856" target="_blank"〉PubMed〈/a〉
    Keywords: Alkynes/pharmacology ; Animals ; Base Sequence ; Cell Line ; Cercopithecus aethiops ; Humans ; Molecular Sequence Data ; Oligonucleotides, Antisense/pharmacokinetics/*pharmacology ; Pyrimidine Nucleotides/pharmacokinetics/*pharmacology ; RNA/*drug effects ; Rats ; Thionucleotides/pharmacokinetics/*pharmacology
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    Determination of type I receptor specificity by the type II receptors for TGF-beta or activin (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-11-05
    Description: Transforming growth factor-beta (TGF-beta) and activin signal primarily through interaction with type I and type II receptors, which are transmembrane serine-threonine kinases. Tsk 7L is a type I receptor for TGF-beta and requires coexpression of the type II TGF-beta receptor for ligand binding. Tsk 7L also specifically bound activin, when coexpressed with the type IIA activin receptor. Tsk 7L could associate with either type II receptor and the ligand binding specificity of Tsk 7L was conferred by the type II receptor. Tsk 7L can therefore act as type I receptor for both activin and TGF-beta, and possibly other ligands.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ebner, R -- Chen, R H -- Lawler, S -- Zioncheck, T -- Derynck, R -- New York, N.Y. -- Science. 1993 Nov 5;262(5135):900-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Departments of Growth and Development, and Anatomy, University of California at San Francisco 94143-0640.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8235612" target="_blank"〉PubMed〈/a〉
    Keywords: Activin Receptors ; Activins ; Base Sequence ; DNA Primers ; Growth Substances/metabolism ; Humans ; Inhibins/*metabolism ; Molecular Sequence Data ; Precipitin Tests ; Protein-Serine-Threonine Kinases/*metabolism ; Receptors, Growth Factor/*metabolism ; Receptors, Transforming Growth Factor beta/*metabolism ; Recombinant Fusion Proteins/metabolism ; Signal Transduction ; Transfection ; Transforming Growth Factor beta/*metabolism
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    Reconstitution of T cell receptor zeta-mediated calcium mobilization in nonlymphoid cells (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-08-13
    Description: T cell antigen receptor (TCR) activation involves interactions between receptor subunits and nonreceptor protein tyrosine kinases (PTKs). Early steps in signaling through the zeta chain of the TCR were examined in transfected COS-1 cells. Coexpression of the PTK p59fynT, but not p56lck, with zeta or with a homodimeric TCR beta-zeta fusion protein produced tyrosine phosphorylation of both zeta and phospholipase C (PLC)-gamma 1, as well as calcium ion mobilization in response to receptor cross-linking. CD45 coexpression enhanced these effects. No requirement for the PTKZAP-70 was observed. Thus, p59fynT may link zeta directly to the PLC-gamma 1 activation pathway.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hall, C G -- Sancho, J -- Terhorst, C -- AI 15066/AI/NIAID NIH HHS/ -- CA 01486/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1993 Aug 13;261(5123):915-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Immunology, Beth Israel Hospital, Harvard Medical School, Boston, MA 02115.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8346442" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens, CD45/analysis ; Base Sequence ; Calcium/*metabolism ; Cell Line ; Cercopithecus aethiops ; Lymphocyte Specific Protein Tyrosine Kinase p56(lck) ; Membrane Proteins/*metabolism ; Molecular Sequence Data ; Phosphorylation ; Protein-Tyrosine Kinases/*metabolism/physiology ; Proto-Oncogene Proteins/*metabolism ; Proto-Oncogene Proteins c-fyn ; Receptors, Antigen, T-Cell/*metabolism ; Recombinant Fusion Proteins/metabolism ; Signal Transduction ; Transfection ; Type C Phospholipases/metabolism ; Tyrosine/metabolism ; ZAP-70 Protein-Tyrosine Kinase
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    Chemorepulsion of axons in the developing mammalian central nervous system (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-07-02
    Description: During development of the nervous system, distinct populations of nerve cells extend specialized processes, axons and dendrites, over considerable distances to locate their targets. There is strong evidence for two general mechanisms by which these connections are made. The first involves attractive and repulsive interactions, both between cells and between them and their extracellular matrix. The second depends on the release of diffusible chemoattractants by target structures. Evidence is now provided for a mechanism of axon guidance in which diffusible chemorepulsive factors create exclusion zones for developing axons, causing them to turn away from inappropriate territory.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pini, A -- New York, N.Y. -- Science. 1993 Jul 2;261(5117):95-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Medical Research Council Mammalian Development Unit, London, United Kingdom.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8316861" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Axons/*physiology ; Cerebral Cortex/cytology/embryology/physiology ; Contact Inhibition ; Culture Techniques ; Olfactory Bulb/cytology/*embryology/physiology ; Olfactory Pathways/cytology/*embryology/physiology ; Rats ; Telencephalon/cytology/embryology/physiology
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    Controlling signal transduction with synthetic ligands (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-11-12
    Description: Dimerization and oligomerization are general biological control mechanisms contributing to the activation of cell membrane receptors, transcription factors, vesicle fusion proteins, and other classes of intra- and extracellular proteins. Cell permeable, synthetic ligands were devised that can be used to control the intracellular oligomerization of specific proteins. To demonstrate their utility, these ligands were used to induce intracellular oligomerization of cell surface receptors that lacked their transmembrane and extracellular regions but contained intracellular signaling domains. Addition of these ligands to cells in culture resulted in signal transmission and specific target gene activation. Monomeric forms of the ligands blocked the pathway. This method of ligand-regulated activation and termination of signaling pathways has the potential to be applied wherever precise control of a signal transduction pathway is desired.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Spencer, D M -- Wandless, T J -- Schreiber, S L -- Crabtree, G R -- New York, N.Y. -- Science. 1993 Nov 12;262(5136):1019-24.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Stanford University, CA 94305.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7694365" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Carrier Proteins/*metabolism ; Cross-Linking Reagents ; Gene Expression Regulation ; Heat-Shock Proteins/*metabolism ; Ligands ; Membrane Proteins/*metabolism ; Models, Biological ; Molecular Sequence Data ; Polymers ; Receptors, Antigen, T-Cell/*metabolism ; Recombinant Fusion Proteins/metabolism ; *Signal Transduction ; T-Lymphocytes/*metabolism ; Tacrolimus/*analogs & derivatives/chemical synthesis/chemistry/metabolism ; Tacrolimus Binding Proteins ; Transcriptional Activation ; Transfection ; Tumor Cells, Cultured
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    Effect of PU.1 phosphorylation on interaction with NF-EM5 and transcriptional activation (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-03-12
    Description: PU.1 recruits the binding of a second B cell-restricted nuclear factor, NF-EM5, to a DNA site in the immunoglobulin kappa 3' enhancer. DNA binding by NF-EM5 requires a protein-protein interaction with PU.1 and specific DNA contacts. Dephosphorylated PU.1 bound to DNA but did not interact with NF-EM5. Analysis of serine-to-alanine mutations in PU.1 indicated that serine 148 (Ser148) is required for protein-protein interaction. PU.1 produced in bacteria did not interact with NF-EM5. Phosphorylation of bacterially produced PU.1 by purified casein kinase II modified it to a form that interacted with NF-EM5 and that recruited NF-EM5 to bind to DNA. Phosphopeptide analysis of bacterially produced PU.1 suggested that Ser148 is phosphorylated by casein kinase II. This site is also phosphorylated in vivo. Expression of wild-type PU.1 increased expression of a reporter construct containing the PU.1 and NF-EM5 binding sites nearly sixfold, whereas the Ser148 mutant form only weakly activated transcription. These results demonstrate that phosphorylation of PU.1 at Ser148 is necessary for interaction with NF-EM5 and suggest that this phosphorylation can regulate transcriptional activity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pongubala, J M -- Van Beveren, C -- Nagulapalli, S -- Klemsz, M J -- McKercher, S R -- Maki, R A -- Atchison, M L -- AI 30656/AI/NIAID NIH HHS/ -- CA 42909/CA/NCI NIH HHS/ -- GM 42415/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1993 Mar 12;259(5101):1622-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Animal Biology, University of Pennsylvania, School of Veterinary Medicine, Philadelphia 19104.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8456286" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; B-Lymphocytes/immunology ; Base Sequence ; Cell Line ; Cell Nucleus/metabolism ; DNA-Binding Proteins/genetics/isolation & purification/*metabolism ; Enhancer Elements, Genetic ; Immunoglobulin kappa-Chains/genetics ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Oligonucleotide Probes ; Phosphorylation ; Plasmacytoma ; Recombinant Proteins/isolation & purification/metabolism ; Retroviridae Proteins, Oncogenic ; Transcription Factors/*metabolism ; *Transcription, Genetic ; Transfection ; Tumor Cells, Cultured
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    Feedback regulation mechanisms for the control of GTP cyclohydrolase I activity (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-06-04
    Description: Guanosine triphosphate (GTP) cyclohydrolase I, the rate-limiting enzyme in the biosynthesis of tetrahydrobiopterin (BH4), is subject to feedback inhibition by BH4, a cofactor for phenylalanine hydroxylase. Inhibition was found to depend specifically on BH4 and the presence of another protein (p35). The inhibition occurred through BH4-dependent complex formation between p35 protein and GTP cyclohydrolase I. Furthermore, the inhibition was specifically reversed by phenylalanine, and, in conjunction with p35, phenylalanine reduced the cooperativity of GTP cyclohydrolase I. These findings also provide a molecular basis for high plasma BH4 concentrations observed in patients with hyperphenylalaninemia caused by phenylalanine hydroxylase deficiency.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Harada, T -- Kagamiyama, H -- Hatakeyama, K -- New York, N.Y. -- Science. 1993 Jun 4;260(5113):1507-10.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, Osaka Medical College, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8502995" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Biological Factors/physiology ; Biopterin/analogs & derivatives/physiology ; Chromatography, Gel ; Feedback ; GTP Cyclohydrolase/antagonists & inhibitors/*metabolism ; Humans ; In Vitro Techniques ; Liver/metabolism ; Phenylalanine/physiology ; Phenylalanine Hydroxylase/metabolism ; Protein Binding ; Rats ; Recombinant Proteins/metabolism ; Tissue Extracts
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    An essential role for protein phosphatases in hippocampal long-term depression (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-08-20
    Description: The effectiveness of long-term potentiation (LTP) as a mechanism for information storage would be severely limited if processes that decrease synaptic strength did not also exist. In area CA1 of the rat hippocampus, prolonged periods of low-frequency afferent stimulation elicit a long-term depression (LTD) that is specific to the stimulated input. The induction of LTD was blocked by the extracellular application of okadaic acid or calyculin A, two inhibitors of protein phosphatases 1 and 2A. The loading of CA1 cells with microcystin LR, a membrane-impermeable protein phosphatase inhibitor, or calmodulin antagonists also blocked or attenuated LTD. The application of calyculin A after the induction of LTD reversed the synaptic depression, suggesting that phosphatase activity is required for the maintenance of LTD. These findings indicate that the synaptic activation of protein phosphatases plays an important role in the regulation of synaptic transmission.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mulkey, R M -- Herron, C E -- Malenka, R C -- MH00942/MH/NIMH NIH HHS/ -- MH10306/MH/NIMH NIH HHS/ -- MH45334/MH/NIMH NIH HHS/ -- New York, N.Y. -- Science. 1993 Aug 20;261(5124):1051-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Psychiatry, University of California, San Francisco 94143-0984.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8394601" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Calcium/metabolism ; Calmodulin/metabolism ; Electric Stimulation ; Ethers, Cyclic/pharmacology ; Hippocampus/drug effects/enzymology/*physiology ; Microcystins ; Okadaic Acid ; Oxazoles/pharmacology ; Peptides, Cyclic/pharmacology ; Phosphoprotein Phosphatases/antagonists & inhibitors/*metabolism ; Phosphorylation ; Rats ; Rats, Sprague-Dawley ; Receptors, N-Methyl-D-Aspartate/physiology ; Synapses/drug effects/*physiology ; *Synaptic Transmission/drug effects
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    A truncated erythropoietin receptor and cell death (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-01-29
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schwall, R -- New York, N.Y. -- Science. 1993 Jan 29;259(5095):696.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8430322" target="_blank"〉PubMed〈/a〉
    Keywords: Bone Marrow/*physiology ; Cell Death/drug effects/*physiology ; Cell Division/drug effects ; Cell Survival/drug effects ; Erythropoietin/*pharmacology ; Humans ; Receptors, Erythropoietin/*genetics/*physiology ; Transfection
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    Connexin mutations in X-linked Charcot-Marie-Tooth disease (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-12-24
    Description: X-linked Charcot-Marie-Tooth disease (CMTX) is a form of hereditary neuropathy with demyelination. Recently, this disorder was mapped to chromosome Xq13.1. The gene for the gap junction protein connexin32 is located in the same chromosomal segment, which led to its consideration as a candidate gene for CMTX. With the use of Northern (RNA) blot and immunohistochemistry technique, it was found that connexin32 is normally expressed in myelinated peripheral nerve. Direct sequencing of the connexin32 gene showed seven different mutations in affected persons from eight CMTX families. These findings, a demonstration of inherited defects in a gap junction protein, suggest that connexin32 plays an important role in peripheral nerve.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bergoffen, J -- Scherer, S S -- Wang, S -- Scott, M O -- Bone, L J -- Paul, D L -- Chen, K -- Lensch, M W -- Chance, P F -- Fischbeck, K H -- GM37751/GM/NIGMS NIH HHS/ -- NS01565/NS/NINDS NIH HHS/ -- NS08075/NS/NINDS NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1993 Dec 24;262(5142):2039-42.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurology, University of Pennsylvania Medical School, Children's Hospital of Philadelphia 19104.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8266101" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Charcot-Marie-Tooth Disease/*genetics ; Chromosome Mapping ; Connexins/analysis/*genetics ; Female ; Genetic Linkage ; Humans ; Male ; Molecular Sequence Data ; *Mutation ; Nerve Fibers, Myelinated/chemistry ; Nerve Tissue Proteins/analysis ; Peripheral Nerves/chemistry ; Rats ; X Chromosome
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    Rhythmic exocytosis stimulated by GnRH-induced calcium oscillations in rat gonadotropes (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-04-02
    Description: In pituitary gonadotropes, gonadotropin-releasing hormone (GnRH) induces the rhythmic release of Ca2+ from an inositol 1,4,5-trisphosphate (IP3)-sensitive store. Simultaneous measurement of the concentration of cytosolic free Ca2+ ([Ca2+]i) and exocytosis in single identified gonadotropes showed that each elevation of [Ca2+]i induced a burst of exocytosis. These phenomena were largely suppressed by buffering of [Ca2+]i but persisted in the absence of extracellular Ca2+. Activation of voltage-gated Ca2+ channels by brief depolarizations seldom supplied enough Ca2+ for exocytosis, but [Ca2+]i elevations induced by photolysis of caged IP3 did trigger exocytosis, confirming that GnRH-stimulated gonadotropic hormone secretion is closely coupled to intracellular Ca2+ release. Agonist-induced oscillations of [Ca2+]i in secretory cells may be a mechanism to optimize the secretory output while avoiding the toxic effects of sustained elevation of [Ca2+]i.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tse, A -- Tse, F W -- Almers, W -- Hille, B -- New York, N.Y. -- Science. 1993 Apr 2;260(5104):82-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physiology and Biophysics, University of Washington School of Medicine, Seattle 98195.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8385366" target="_blank"〉PubMed〈/a〉
    Keywords: Action Potentials ; Animals ; Calcium/*metabolism ; Calcium Channels/drug effects/physiology ; Cytoplasmic Granules/drug effects/physiology ; Electrophysiology ; Exocytosis/*drug effects ; Gonadotropin-Releasing Hormone/administration & dosage/*pharmacology ; Inositol 1,4,5-Trisphosphate/pharmacology ; Male ; Periodicity ; Photolysis ; Pituitary Gland/drug effects/*physiology/ultrastructure ; Rats ; Rats, Sprague-Dawley
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    Altered growth of human colon cancer cell lines disrupted at activated Ki-ras (1993)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1993-04-02
    Description: Point mutations that activate the Ki-ras proto-oncogene are presented in about 50 percent of human colorectal tumors. To study the functional significance of these mutations, the activated Ki-ras genes in two human colon carcinoma cell lines, DLD-1 and HCT 116, were disrupted by homologous recombination. Compared with parental cells, cells disrupted at the activated Ki-ras gene were morphologically altered, lost the capacity for anchorage-independent growth, grew more slowly both in vitro and in nude mice, and showed reduced expression of c-myc. Thus, the activated Ki-ras gene plays a key role in colorectal tumorigenesis through altered cell differentiation and cell growth.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shirasawa, S -- Furuse, M -- Yokoyama, N -- Sasazuki, T -- New York, N.Y. -- Science. 1993 Apr 2;260(5104):85-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Genetics, Kyushu University, Fukuoka, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8465203" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Cell Differentiation ; Cell Division ; Codon ; Colonic Neoplasms/*genetics/pathology ; Gene Expression Regulation, Neoplastic ; Genes, myc/genetics ; Genes, ras/*genetics ; Humans ; Infant ; Mice ; Mice, Nude ; Molecular Sequence Data ; Mutagenesis, Insertional ; Nucleic Acid Hybridization ; Plasmids ; *Point Mutation ; Polymerase Chain Reaction ; Restriction Mapping ; Transfection ; Tumor Cells, Cultured
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    A single phosphotyrosine residue of Stat91 required for gene activation by interferon-gamma (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-09-24
    Description: Interferon-gamma (IFN-gamma) stimulates transcription of specific genes by inducing tyrosine phosphorylation of a 91-kilodalton cytoplasmic protein (termed STAT for signal transducer and activator of transcription). Stat91 was phosphorylated on a single site (Tyr701), and phosphorylation of this site was required for nuclear translocation, DNA binding, and gene activation. Stat84, a differentially spliced product of the same gene that lacks the 38 carboxyl-terminal amino acids of Stat91, did not activate transcription, although it was phosphorylated and translocated to the nucleus and bound DNA. Thus, Stat91 mediates activation of transcription in response to IFN-gamma.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shuai, K -- Stark, G R -- Kerr, I M -- Darnell, J E Jr -- AI32489-02/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1993 Sep 24;261(5129):1744-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Rockefeller University, Laboratory of Molecular Cell Biology, New York, NY 10021.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7690989" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Cell Line ; Cell Nucleus/metabolism ; DNA-Binding Proteins/chemistry/*metabolism ; *Gene Expression Regulation ; Humans ; Interferon-gamma/*pharmacology ; Molecular Sequence Data ; Peptide Fragments/chemistry/metabolism ; Phosphotyrosine ; *Signal Transduction ; Transcription Factors/chemistry/*metabolism ; Transcriptional Activation ; Transfection ; Tyrosine/analogs & derivatives/chemistry
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    CD40 ligand gene defects responsible for X-linked hyper-IgM syndrome (1993)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1993-02-12
    Description: The ligand for CD40 (CD40L) is a membrane glycoprotein on activated T cells that induces B cell proliferation and immunoglobulin secretion. Abnormalities in the CD40L gene were associated with an X-linked immunodeficiency in humans [hyper-IgM (immunoglobulin M) syndrome]. This disease is characterized by elevated concentrations of serum IgM and decreased amounts of all other isotypes. CD40L complementary DNAs from three of four patients with this syndrome contained distinct point mutations. Recombinant expression of two of the mutant CD40L complementary DNAs resulted in proteins incapable of binding to CD40 and unable to induce proliferation or IgE secretion from normal B cells. Activated T cells from the four affected patients failed to express wild-type CD40L, although their B cells responded normally to wild-type CD40L. Thus, these CD40L defects lead to a T cell abnormality that results in the failure of patient B cells to undergo immunoglobulin class switching.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Allen, R C -- Armitage, R J -- Conley, M E -- Rosenblatt, H -- Jenkins, N A -- Copeland, N G -- Bedell, M A -- Edelhoff, S -- Disteche, C M -- Simoneaux, D K -- A125129/PHS HHS/ -- N01-CO-74101/CO/NCI NIH HHS/ -- New York, N.Y. -- Science. 1993 Feb 12;259(5097):990-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Baylor College of Medicine, Houston, TX 77030.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7679801" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens, CD/*metabolism ; Antigens, CD40 ; Antigens, Differentiation, B-Lymphocyte/*metabolism ; Base Sequence ; CD40 Ligand ; DNA/chemistry/genetics ; Humans ; Immunoglobulin M/*blood ; Immunologic Deficiency Syndromes/*genetics/immunology ; Ligands ; Male ; Membrane Glycoproteins/*genetics ; Mice ; Molecular Sequence Data ; *Point Mutation ; Polymerase Chain Reaction ; T-Lymphocytes/*immunology ; Transfection ; *X Chromosome
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    Involvement of platelet-endothelial cell adhesion molecule-1 in neutrophil recruitment in vivo (1993)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1993-12-03
    Description: During inflammation, neutrophils migrate from the vascular lumen into extravascular sites. In vitro assays have suggested that platelet-endothelial cell adhesion molecule-1 [PECAM-1 (CD31)], a member of the immunoglobulin superfamily, is required for the transmigration of neutrophils across endothelial monolayers. Antibody to human PECAM-1, which cross-reacts with rat PECAM-1, was found to block not only in vivo accumulation of rat neutrophils into the peritoneal cavity and the alveolar compartment of the lung but also neutrophil accumulation in human skin grafts transplanted onto immunodeficient mice. On the basis of these findings in three different models of inflammation, it appears that PECAM-1 is required for neutrophil transmigration in vivo and may thus be a potential therapeutic target.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Vaporciyan, A A -- DeLisser, H M -- Yan, H C -- Mendiguren, I I -- Thom, S R -- Jones, M L -- Ward, P A -- Albelda, S M -- HL-31963/HL/NHLBI NIH HHS/ -- HL-430020-02/HL/NHLBI NIH HHS/ -- HL-46311/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1993 Dec 3;262(5139):1580-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pathology, University of Michigan Medical School, Ann Arbor 48109.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8248808" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antibodies/pharmacology ; Antigens, CD31 ; Antigens, Differentiation, Myelomonocytic/immunology/*physiology ; Cell Adhesion Molecules/immunology/*physiology ; Cell Movement/physiology ; Chemotaxis, Leukocyte/physiology ; Endothelium/immunology ; Humans ; Immune Complex Diseases/immunology ; Membrane Glycoproteins/immunology/*physiology ; Mice ; Mice, SCID ; Neutrophils/*physiology ; Peritoneal Cavity/cytology ; Rats ; Skin Transplantation/immunology ; Transplantation, Heterologous/immunology
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    Transsynaptic expression of a presynaptic glutamate receptor during hippocampal long-term potentiation (1993)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1993-10-15
    Description: Repetitive activation of excitatory synapses in the hippocampus produces a persistent enhancement of synaptic efficiency known as long-term potentiation (LTP). In anesthetized and in freely moving rats, the induction of LTP in the perforant path led to a transient increase in the amount of messenger RNA (mRNA) coding for a presynaptic glutamate receptor (GR33) in dentate granule cells. The amount of GR33 mRNA was increased for at least 5 hours after the induction of LTP but was indistinguishable from control values 1 day after induction. The N-methyl-D-aspartate receptor antagonist 2-aminophosphonovalerate prevented the induction of both LTP and the increase in GR33 mRNA. The amount of GR33 protein was increased in the mossy fiber terminal zone of dentate granule cells 5 hours after the induction of LTP. These results suggest that the induction of LTP in synapses at one stage in a neural network may lead to modification in synaptic function at the next stage in the network.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Smirnova, T -- Laroche, S -- Errington, M L -- Hicks, A A -- Bliss, T V -- Mallet, J -- New York, N.Y. -- Science. 1993 Oct 15;262(5132):433-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratoire de genetique moleculaire de la neurotransmission et des processus neurodegeneratifs, Centre National de la Recherche Scientifique (CNRS), Gif-sur-Yvette, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8105538" target="_blank"〉PubMed〈/a〉
    Keywords: 2-Amino-5-phosphonovalerate/pharmacology ; Animals ; Electric Stimulation ; Evoked Potentials ; Gene Expression ; Hippocampus/*metabolism/physiology ; In Situ Hybridization ; Male ; RNA, Messenger/genetics/metabolism ; Rats ; Rats, Sprague-Dawley ; Receptors, Glutamate/biosynthesis/*genetics ; Receptors, Presynaptic/biosynthesis/*genetics ; Synapses/*metabolism
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    Translocation of TCR alpha chains into the lumen of the endoplasmic reticulum and their degradation (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-03-26
    Description: After synthesis, the alpha chain of the T cell antigen receptor (TCR alpha) can form a complex with other TCR chains and move to the cell surface, or TCR alpha can undergo degradation in the endoplasmic reticulum (ER) if it remains unassembled. The mechanism of translocation and degradation in the ER is unclear. It was found that the putative transmembrane region of TCR alpha (alpha tm) was incompetent on its own to act as a transmembrane region. Molecules that contained alpha tm were translocated into the ER lumen and then underwent either rapid degradation or secretion, depending on the sequence of the cytoplasmic domain. A specific signal for ER degradation within alpha tm does not appear to be present.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shin, J -- Lee, S -- Strominger, J L -- AI20182/AI/NIAID NIH HHS/ -- CA47554/CA/NCI NIH HHS/ -- GM48961/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1993 Mar 26;259(5103):1901-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Tumor Virology, Dana-Farber Cancer Institute, Harvard Medical School, Boston, MA 02115.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8456316" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antigens, CD4/chemistry/genetics/metabolism ; Cytoplasm/metabolism ; DNA/genetics ; Endoplasmic Reticulum/*metabolism ; Glycosylation ; HeLa Cells/metabolism ; Humans ; Immunosorbent Techniques ; Lipid Bilayers/metabolism ; Macromolecular Substances ; Mice ; Molecular Sequence Data ; Mutagenesis ; Protein Structure, Secondary ; Receptors, Antigen, T-Cell/chemistry/genetics/*metabolism ; Recombinant Fusion Proteins/chemistry/metabolism ; Transfection
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    Release of active cytokinin by a beta-glucosidase localized to the maize root meristem (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-11-12
    Description: A beta-glucoside encoded by a cloned Zea mays complementary DNA (Zm-p60.1) cleaved the biologically inactive hormone conjugates cytokinin-O-glucosides and kinetin-N3-glucoside, releasing active cytokinin. Tobacco protoplasts that transiently expressed Zm-p60.1 could use the inactive cytokinin glucosides to initiate cell division. The ability of protoplasts to sustain growth in response to cytokinin glucosides persisted indefinitely after the likely disappearance of the expression vector. In the roots of maize seedlings, Zm-p60.1 was localized to the meristematic cells and may function in vivo to supply the developing maize embryo with active cytokinin.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Brzobohaty, B -- Moore, I -- Kristoffersen, P -- Bako, L -- Campos, N -- Schell, J -- Palme, K -- New York, N.Y. -- Science. 1993 Nov 12;262(5136):1051-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Max-Planck Institut fur Zuchtungsforschung, Koln Federal Republic of Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8235622" target="_blank"〉PubMed〈/a〉
    Keywords: Adenine/analogs & derivatives/metabolism ; Amino Acid Sequence ; Base Sequence ; Cell Division ; Cytokinins/*metabolism ; DNA, Complementary/genetics ; Glucosides/metabolism ; Kinetin ; Molecular Sequence Data ; Plants, Toxic ; Protoplasts/cytology/enzymology ; Tobacco/cytology/enzymology ; Transfection ; Zea mays/enzymology/growth & development/*metabolism ; Zeatin/*metabolism ; beta-Glucosidase/genetics/*metabolism
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    Gene replacement in Toxoplasma gondii with chloramphenicol acetyltransferase as selectable marker (1993)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1993-11-05
    Description: A system for stable transformation of Toxoplasma gondii tachyzoites was developed that exploited the susceptibility of Toxoplasma to chloramphenicol. Introduction of the chloramphenicol acetyltransferase (CAT) gene fused to Toxoplasma flanking sequences followed by chloramphenicol selection resulted in parasites stably expressing CAT. A construct incorporating the tandemly repeated gene, B1, targeted efficiently to its homologous chromosomal locus. Knockout of the single-copy gene, ROP1, was also successful. Stable transformation should permit the identification and analysis of Toxoplasma genes important in the interaction of this opportunistic parasite with its host.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kim, K -- Soldati, D -- Boothroyd, J C -- New York, N.Y. -- Science. 1993 Nov 5;262(5135):911-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology and Immunology, Stanford University School of Medicine 94305.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8235614" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Chloramphenicol/pharmacology ; Chloramphenicol O-Acetyltransferase/*genetics ; Drug Resistance ; *Genes, Protozoan ; Genetic Markers ; Multigene Family ; Plasmids ; Recombination, Genetic ; Toxoplasma/drug effects/*genetics ; Transfection ; *Transformation, Genetic
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    Modulation of cocaine self-administration in the rat through D-3 dopamine receptors (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-06-18
    Description: The reinforcing properties of cocaine are probably mediated by the mesocorticolimbic dopamine pathways in the central nervous system, but not all of the dopamine receptor subtypes involved in cocaine's reinforcing actions have been clearly identified. Recently, the D-3 receptor has been cloned, and its distribution in the brain has been found to be relatively restricted to limbic projections of the midbrain dopamine system. The D-3-selective compounds 7-hydroxy-N,N-di-n-propyl-2-aminotetralin (7-OHDPAT) and quinpirole potently decreased cocaine self-administration in the rat at doses that were not by themselves reinforcing. Moreover, three dopamine receptor agonists had affinities for binding to the D-3 receptor that correlated highly with their relative potencies in decreasing cocaine self-administration. The D-3 receptor may be involved in the reinforcing effects of cocaine and may be a useful target for the development of new pharmacotherapies for cocaine abuse.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Caine, S B -- Koob, G F -- NIDA DA04398/DA/NIDA NIH HHS/ -- NIDA DA05478/DA/NIDA NIH HHS/ -- New York, N.Y. -- Science. 1993 Jun 18;260(5115):1814-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neuropharmacology, Scripps Research Institute, La Jolla, CA 92037.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8099761" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Apomorphine/pharmacology ; Cocaine/*administration & dosage ; Dopamine Agents/*pharmacology ; Dose-Response Relationship, Drug ; Ergolines/pharmacology ; Male ; Quinpirole ; Rats ; Rats, Wistar ; Receptors, Dopamine/*metabolism ; *Receptors, Dopamine D2 ; Receptors, Dopamine D3 ; Reinforcement (Psychology) ; Self Administration ; Tetrahydronaphthalenes/pharmacology
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    Activation of a phosphotyrosine phosphatase by tyrosine phosphorylation (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-03-12
    Description: Regulation of cell proliferation, differentiation, and metabolic homeostasis is associated with the phosphorylation and dephosphorylation of specific tyrosine residues of key regulatory proteins. The phosphotyrosine phosphatase 1D (PTP 1D) contains two amino terminally located Src homology 2 (SH2) domains and is similar to the Drosophila corkscrew gene product, which positively regulates the torso tyrosine kinase signal transduction pathway. PTP activity was found to be regulated by physical interaction with a protein tyrosine kinase. PTP 1D did not dephosphorylate receptor tyrosine kinases, despite the fact that it associated with the epidermal growth factor receptor and chimeric receptors containing the extracellular domain of the epidermal growth factor receptor and the cytoplasmic domain of either the HER2-neu, kit-SCF, or platelet-derived growth factor beta (beta PDGF) receptors. PTP 1D was phosphorylated on tyrosine in cells overexpressing the beta PDGF receptor kinase and this tyrosine phosphorylation correlated with an enhancement of its catalytic activity. Thus, protein tyrosine kinases and phosphatases do not simply oppose each other's action; rather, they may work in concert to maintain a fine balance of effector activation needed for the regulation of cell growth and differentiation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Vogel, W -- Lammers, R -- Huang, J -- Ullrich, A -- New York, N.Y. -- Science. 1993 Mar 12;259(5101):1611-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, Max-Planck-Institut fur Biochemie, Martinsried, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7681217" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Cell Line ; Chimera ; Drosophila/genetics ; Enzyme Activation ; Genes, src ; Humans ; Kidney ; Luminescent Measurements ; Mice ; Molecular Sequence Data ; Oligodeoxyribonucleotides ; Phosphorylation ; Phosphotyrosine ; Plasmids ; Protein Tyrosine Phosphatases/*metabolism ; Proto-Oncogene Proteins/genetics/metabolism ; Proto-Oncogene Proteins c-kit ; Proto-Oncogenes ; Receptor, Epidermal Growth Factor/genetics/metabolism ; Receptor, ErbB-2 ; Receptors, Platelet-Derived Growth Factor/genetics/metabolism ; Sequence Homology, Amino Acid ; Signal Transduction ; Transfection ; Tyrosine/*analogs & derivatives/metabolism
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    Thinking about brain cell assemblies (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-08-20
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Eichenbaum, H -- New York, N.Y. -- Science. 1993 Aug 20;261(5124):993-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for Behavioral Neuroscience, State University of New York, Stony Brook 11794.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8351525" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Brain Mapping ; Cerebral Cortex/physiology ; Hippocampus/*physiology ; *Memory ; Neurons/*physiology ; *Perception ; Rats
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    Modulation of anxiety and neuropeptide Y-Y1 receptors by antisense oligodeoxynucleotides (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-01-22
    Description: The function of neuropeptide Y, one of the most abundant peptide transmitters of the mammalian brain, remains unclear because of a lack of specific receptor antagonists. An antisense oligodeoxynucleotide corresponding to the NH2-terminus of the rat Y1 receptor was constructed and added to cultures of rat cortical neurons. This treatment resulted in a reduced density of Y1 (but not Y2) receptors and diminished the decrease in adenosine 3',5'-monophosphate (cAMP) usually seen after Y1 receptor activation. Repeated injection of the same oligodeoxynucleotide into the lateral cerebral ventricle of rats was followed by a similar reduction of cortical Y1 (but not Y2) receptors. Such antisense-treated animals displayed behavioral signs of anxiety. Thus, specific inhibition of neurotransmitter receptor expression can be accomplished in the living brain and demonstrates that altered central neuropeptide Y transmission produces an anxiety-like state.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wahlestedt, C -- Pich, E M -- Koob, G F -- Yee, F -- Heilig, M -- New York, N.Y. -- Science. 1993 Jan 22;259(5094):528-31.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurology and Neuroscience, Cornell University Medical College, New York, NY 10021.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8380941" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Anxiety ; Base Sequence ; Cells, Cultured ; Cerebral Cortex/*physiology ; Cyclic AMP/metabolism ; Down-Regulation ; Embryo, Mammalian ; Learning ; Male ; Molecular Sequence Data ; Neurons/drug effects/*physiology ; Neuropeptide Y/*physiology ; Oligodeoxyribonucleotides ; Oligonucleotides, Antisense/*pharmacology ; Polymerase Chain Reaction ; Rats ; Rats, Wistar ; Receptors, Neuropeptide Y/*drug effects/*genetics/metabolism
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    Cloning of a type I TGF-beta receptor and its effect on TGF-beta binding to the type II receptor (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-05-28
    Description: Transforming growth factor-beta (TGF-beta) affects cellular proliferation, differentiation, and interaction with the extracellular matrix primarily through interaction with the type I and type II TGF-beta receptors. The type II receptors for TGF-beta and activin contain putative serine-threonine kinase domains. A murine serine-threonine kinase receptor, Tsk 7L, was cloned that shared a conserved extracellular domain with the type II TGF-beta receptor. Overexpression of Tsk 7L alone did not increase cell surface binding of TGF-beta, but coexpression with the type II TGF-beta receptor caused TGF-beta to bind to Tsk 7L, which had the size of the type I TGF-beta receptor. Overexpression of Tsk 7L inhibited binding of TGF-beta to the type II receptor in a dominant negative fashion. Combinatorial interactions and stoichiometric ratios between the type I and II receptors may therefore determine the extent of TGF-beta binding and the resulting biological activities.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ebner, R -- Chen, R H -- Shum, L -- Lawler, S -- Zioncheck, T F -- Lee, A -- Lopez, A R -- Derynck, R -- New York, N.Y. -- Science. 1993 May 28;260(5112):1344-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Growth and Development, University of California, San Francisco 94143-0640.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8388127" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Cell Line ; Cercopithecus aethiops ; Cloning, Molecular ; Humans ; Mice ; Molecular Sequence Data ; Protein-Serine-Threonine Kinases ; Quail ; Receptors, Cell Surface/chemistry/genetics/*metabolism ; Receptors, Transforming Growth Factor beta ; Transfection ; Transforming Growth Factor beta/*metabolism
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    Release of excess amyloid beta protein from a mutant amyloid beta protein precursor (1993)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1993-01-22
    Description: The 4-kilodalton amyloid beta protein (A beta), which forms fibrillar deposits in Alzheimer's disease (AD), is derived from a large protein referred to as the amyloid beta protein precursor (beta APP). Human neuroblastoma (M17) cells transfected with constructs expressing wild-type beta APP or a mutant, beta APP delta NL, recently linked to familial AD were compared. After continuous metabolic labeling for 8 hours, cells expressing beta APP delta NL had five times more of an A beta-bearing, carboxyl terminal, beta APP derivative than cells expressing wild-type beta APP and they released six times more A beta into the medium. Thus this mutant beta APP may cause AD because its processing is altered in a way that releases increased amounts of A beta.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cai, X D -- Golde, T E -- Younkin, S G -- AG06656/AG/NIA NIH HHS/ -- New York, N.Y. -- Science. 1993 Jan 22;259(5094):514-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Neuropathology, Case Western Reserve University, Cleveland, OH 44106.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8424174" target="_blank"〉PubMed〈/a〉
    Keywords: Alzheimer Disease/genetics/metabolism ; Amino Acid Sequence ; Amyloid beta-Peptides/*biosynthesis/genetics ; Amyloid beta-Protein Precursor/*genetics/metabolism ; Base Sequence ; Cloning, Molecular ; Humans ; Molecular Sequence Data ; *Mutagenesis, Site-Directed ; Neuroblastoma ; Oligodeoxyribonucleotides ; Polymerase Chain Reaction/methods ; Transfection ; Tumor Cells, Cultured
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    Selectivity in signal transduction determined by gamma subunits of heterotrimeric G proteins (1993)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1993-02-05
    Description: Various heterotrimeric guanine nucleotide-binding proteins have been identified on the basis of the individual subtypes of their alpha subunits. The beta gamma complexes, composed of beta and gamma subunits, remain tightly associated under physiological conditions and have been assumed to constitute a common pool shared among various guanosine triphosphate (GTP)-binding (G) protein heterotrimers. Particular alpha and beta subunit subtypes participate in the signal transduction processes between somatostatin or muscarinic receptors and the voltage-sensitive L-type calcium channel in rat pituitary GH3 cells. Among gamma subunits the gamma 3 subtype was found to be required for coupling of the somatostatin receptor to voltage-sensitive calcium channels, whereas the gamma 4 subtype was found to be required for coupling of the muscarinic receptor to those channels.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kleuss, C -- Scherubl, H -- Hescheler, J -- Schultz, G -- Wittig, B -- New York, N.Y. -- Science. 1993 Feb 5;259(5096):832-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institut fur Molekularbiologie und Biochemie, Freie Universitat Berlin, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8094261" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Calcium/metabolism ; Calcium Channels/*physiology ; Carbachol/pharmacology ; GTP-Binding Proteins/genetics/*metabolism ; Macromolecular Substances ; Molecular Sequence Data ; Oligodeoxyribonucleotides ; Oligonucleotides, Antisense/pharmacology ; Pituitary Neoplasms ; RNA, Messenger/genetics/isolation & purification/metabolism ; Rats ; Signal Transduction/drug effects/*physiology ; Somatostatin/pharmacology ; Tumor Cells, Cultured
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    Anti-oncogenic and oncogenic potentials of interferon regulatory factors-1 and -2 (1993)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1993-02-12
    Description: Interferon regulatory factor-1 (IRF-1), a transcriptional activator, and IRF-2, its antagonistic repressor, have been identified as regulators of type I interferon and interferon-inducible genes. The IRF-1 gene is itself interferon-inducible and hence may be one of the target genes critical for interferon action. When the IRF-2 gene was overexpressed in NIH 3T3 cells, the cells became transformed and displayed enhanced tumorigenicity in nude mice. This transformed phenotype was reversed by concomitant overexpression of the IRF-1 gene. Thus, restrained cell growth depends on a balance between these two mutually antagonistic transcription factors.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Harada, H -- Kitagawa, M -- Tanaka, N -- Yamamoto, H -- Harada, K -- Ishihara, M -- Taniguchi, T -- New York, N.Y. -- Science. 1993 Feb 12;259(5097):971-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute for Molecular and Cellular Biology, Osaka University, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8438157" target="_blank"〉PubMed〈/a〉
    Keywords: 3T3 Cells/metabolism ; Animals ; Blotting, Northern ; Cell Transformation, Neoplastic/*genetics ; Chromosome Mapping ; Chromosomes, Human, Pair 5 ; DNA/biosynthesis ; DNA-Binding Proteins/*genetics ; *Gene Expression ; Humans ; Immunosorbent Techniques ; Interferon Regulatory Factor-1 ; Interferon Regulatory Factor-2 ; Mice ; Mice, Nude ; Phenotype ; Phosphoproteins/*genetics ; Promoter Regions, Genetic ; RNA, Messenger/genetics ; *Repressor Proteins ; *Transcription Factors ; Transfection
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    Selective inhibition of ras-dependent transformation by a farnesyltransferase inhibitor (1993)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1993-06-25
    Description: To acquire transforming potential, the precursor of the Ras oncoprotein must undergo farnesylation of the cysteine residue located in a carboxyl-terminal tetrapeptide. Inhibitors of the enzyme that catalyzes this modification, farnesyl protein transferase (FPTase), have therefore been suggested as anticancer agents for tumors in which Ras contributes to transformation. The tetrapeptide analog L-731,735 is a potent and selective inhibitor of FPTase in vitro. A prodrug of this compound, L-731,734, inhibited Ras processing in cells transformed with v-ras. L-731,734 decreased the ability of v-ras-transformed cells to form colonies in soft agar but had no effect on the efficiency of colony formation of cells transformed by either the v-raf or v-mos oncogenes. The results demonstrate selective inhibition of ras-dependent cell transformation with a synthetic organic inhibitor of FPTase.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kohl, N E -- Mosser, S D -- deSolms, S J -- Giuliani, E A -- Pompliano, D L -- Graham, S L -- Smith, R L -- Scolnick, E M -- Oliff, A -- Gibbs, J B -- New York, N.Y. -- Science. 1993 Jun 25;260(5116):1934-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cancer Research, Merck Research Laboratories, West Point, PA 19486.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8316833" target="_blank"〉PubMed〈/a〉
    Keywords: *Alkyl and Aryl Transferases ; Animals ; Antineoplastic Agents/chemistry/*pharmacology ; Cell Division/drug effects ; Cell Line ; Cell Transformation, Neoplastic/*drug effects ; Dipeptides/chemistry/*pharmacology ; Drug Design ; Farnesyltranstransferase ; *Genes, ras ; Oncogene Proteins/*metabolism ; Protein Prenylation/*drug effects ; Rats ; Transferases/*antagonists & inhibitors
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    Induction of apoptosis by the low-affinity NGF receptor (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-07-16
    Description: Nerve growth factor (NGF) binding to cellular receptors is required for the survival of some neural cells. In contrast to TrkA, the high-affinity NGF receptor that transduces NGF signals for survival and differentiation, the function of the low-affinity NGF receptor, p75NGFR, remains uncertain. Expression of p75NGFR induced neural cell death constitutively when p75NGFR was unbound; binding by NGF or monoclonal antibody, however, inhibited cell death induced by p75NGFR. Thus, expression of p75NGFR may explain the dependence of some neural cells on NGF for survival. These findings also suggest that p75NGFR has some functional similarities to other members of a superfamily of receptors that include tumor necrosis factor receptors, Fas (Apo-1), and CD40.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rabizadeh, S -- Oh, J -- Zhong, L T -- Yang, J -- Bitler, C M -- Butcher, L L -- Bredesen, D E -- AG10671/AG/NIA NIH HHS/ -- NS10928/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1993 Jul 16;261(5119):345-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurology, University of California, Los Angeles 90024.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8332899" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Apoptosis/drug effects ; Cell Line ; Cell Survival/drug effects ; Culture Media, Serum-Free ; Nerve Growth Factors/*metabolism/pharmacology ; Neurons/*cytology/drug effects/metabolism ; PC12 Cells ; Receptors, Nerve Growth Factor/metabolism/*physiology ; Transfection
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    Peptide translocation by variants of the transporter associated with antigen processing (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-12-24
    Description: Major histocompatibility complex (MHC) class I molecules associate with peptides that are delivered from the cytosol to the lumen of the endoplasmic reticulum by the transporter associated with antigen processing (TAP). Liver microsomes of SHR and Lewis rats, which express different alleles of TAP (cim(b) and cim(a), respectively), accumulate different sets of peptides. Use of MHC congenic rats assigned this difference to the MHC, independent of the class I products expressed. Both the cim(a) and cim(b) TAP complexes translocate peptides with a hydrophobic carboxyl terminus, but translocation of peptides with a carboxyl-terminal His, Lys, or Arg residue is unique to cim(a). Thus, the specificity of the TAP peptide translocator restricts the peptides available for antigen presentation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Heemels, M T -- Schumacher, T N -- Wonigeit, K -- Ploegh, H L -- R01 AI3 3456-01/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1993 Dec 24;262(5142):2059-63.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, Massachusetts Institute of Technology, Cambridge 02139.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8266106" target="_blank"〉PubMed〈/a〉
    Keywords: *ATP-Binding Cassette Transporters ; Alleles ; Amino Acid Sequence ; Animals ; Antigen Presentation/*physiology ; Biological Transport/physiology ; Carrier Proteins/genetics/*physiology ; Histocompatibility Antigens Class I/physiology ; Histocompatibility Antigens Class II/genetics/*physiology ; In Vitro Techniques ; Microsomes, Liver/metabolism ; Molecular Sequence Data ; Oligopeptides/*metabolism ; Rats ; Rats, Inbred BN ; Rats, Inbred Lew ; Rats, Inbred SHR ; Substrate Specificity
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  • 80
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    Sharing of the interleukin-2 (IL-2) receptor gamma chain between receptors for IL-2 and IL-4 (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-12-17
    Description: The gamma chain of the interleukin-2 (IL-2) receptor is an indispensable subunit for IL-2 binding and intracellular signal transduction. A monoclonal antibody to the gamma chain, TUGm2, inhibited IL-2 binding to the functional IL-2 receptors and also inhibited IL-4-induced cell growth and the high-affinity binding of IL-4 to the CTLL-2 mouse T cell line. Another monoclonal antibody, TUGm3, which reacted with the gamma chain cross-linked with IL-2, also immunoprecipitated the gamma chain when cross-linked with IL-4. These results suggest that the IL-2 receptor gamma chain is functionally involved in the IL-4 receptor complex.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kondo, M -- Takeshita, T -- Ishii, N -- Nakamura, M -- Watanabe, S -- Arai, K -- Sugamura, K -- New York, N.Y. -- Science. 1993 Dec 17;262(5141):1874-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology, Tohoku University School of Medicine, Sendai, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8266076" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antibodies, Monoclonal ; Cell Division ; Cell Line ; Interleukin-2/metabolism/pharmacology ; Interleukin-4/metabolism/pharmacology ; Mice ; Rats ; Rats, Wistar ; Receptors, Interleukin-2/chemistry/immunology/*metabolism ; Receptors, Interleukin-4 ; Receptors, Mitogen/chemistry/immunology/*metabolism ; Signal Transduction ; T-Lymphocytes/cytology/immunology
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    Regulation of heat shock factor trimer formation: role of a conserved leucine zipper (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-01-08
    Description: The human and Drosophila heat shock transcription factors (HSFs) are multi-zipper proteins with high-affinity binding to DNA that is regulated by heat shock-induced trimerization. Formation of HSF trimers is dependent on hydrophobic heptad repeats located in the amino-terminal region of the protein. Two subregions at the carboxyl-terminal end of human HSF1 were identified that maintain the monomeric form of the protein under normal conditions. One of these contains a leucine zipper motif that is conserved between vertebrate and insect HSFs. These results suggest that the carboxyl-terminal zipper may suppress formation of trimers by the amino-terminal HSF zipper elements by means of intramolecular coiled-coil interactions that are sensitive to heat shock.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rabindran, S K -- Haroun, R I -- Clos, J -- Wisniewski, J -- Wu, C -- New York, N.Y. -- Science. 1993 Jan 8;259(5092):230-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Biochemistry, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8421783" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Binding Sites ; Cell Line ; DNA/metabolism ; Drosophila/chemistry ; Heat-Shock Proteins/*chemistry/genetics/metabolism ; Hot Temperature ; Humans ; *Leucine Zippers ; Macromolecular Substances ; Molecular Sequence Data ; Mutagenesis ; Structure-Activity Relationship ; Transfection
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    Betacellulin: a mitogen from pancreatic beta cell tumors (1993)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1993-03-12
    Description: Betacellulin, a member of the epidermal growth factor family, has been identified in the conditioned medium of cell lines derived from mouse pancreatic beta cell tumors. Betacellulin is a 32-kilodalton glycoprotein that appears to be processed from a larger transmembrane precursor by proteolytic cleavage. The carboxyl-terminal domain of betacellulin has 50 percent sequence similarity with that of rat transforming growth factor alpha. Betacellulin is a potent mitogen for retinal pigment epithelial cells and vascular smooth muscle cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shing, Y -- Christofori, G -- Hanahan, D -- Ono, Y -- Sasada, R -- Igarashi, K -- Folkman, J -- CA 70118/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1993 Mar 12;259(5101):1604-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Surgery, Children's Hospital, Boston, MA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8456283" target="_blank"〉PubMed〈/a〉
    Keywords: 3T3 Cells ; Amino Acid Sequence ; Animals ; Base Sequence ; Betacellulin ; Cell Division/drug effects ; Cells, Cultured ; DNA Replication/drug effects ; Endothelium, Vascular/cytology/drug effects ; Epidermal Growth Factor/pharmacology ; Growth Substances/*genetics/isolation & purification/pharmacology ; Humans ; *Intercellular Signaling Peptides and Proteins ; Islets of Langerhans/physiopathology ; Kinetics ; Mice ; Molecular Sequence Data ; Muscle, Smooth, Vascular/cytology/drug effects ; Oligodeoxyribonucleotides ; Pancreatic Neoplasms/*physiopathology ; Pigment Epithelium of Eye/cytology/drug effects ; Polymerase Chain Reaction/methods ; Protein Precursors/genetics ; Rats ; Receptor, Epidermal Growth Factor/metabolism ; Recombinant Proteins/pharmacology ; Sequence Homology, Amino Acid ; Thymidine/metabolism ; Transforming Growth Factor alpha/genetics
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    Structural features of polysaccharides that induce intra-abdominal abscesses (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-10-15
    Description: The capsular polysaccharide complex from Bacteroides fragilis promotes the formation of intra-abdominal abscesses--a pathologic host response to infecting microorganisms. This complex consists of two distinct polysaccharides, each with repeating units that have positively charged amino groups and negatively charged carboxyl or phosphate groups. Analysis of these polysaccharides as well as other charged carbohydrates before and after chemical modification revealed that these oppositely charged groups are required for the induction of intra-abdominal abscesses in a rat model.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tzianabos, A O -- Onderdonk, A B -- Rosner, B -- Cisneros, R L -- Kasper, D L -- 1F32 AI 084901 AI/AI/NIAID NIH HHS/ -- 2T32AI07061-11AI/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1993 Oct 15;262(5132):416-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Channing Laboratory, Brigham and Women's Hospital, Boston, MA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8211161" target="_blank"〉PubMed〈/a〉
    Keywords: *Abdomen ; Abscess/*microbiology ; Animals ; Bacterial Capsules/*chemistry/toxicity ; Bacteroides Infections/*microbiology ; Bacteroides fragilis/*pathogenicity ; Carbohydrate Sequence ; Male ; Molecular Sequence Data ; Neisseria meningitidis/pathogenicity ; Polysaccharides, Bacterial/chemistry/toxicity ; Rats ; Rats, Wistar ; Salmonella typhi/pathogenicity ; Streptococcus pneumoniae/pathogenicity ; Structure-Activity Relationship
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  • 84
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    Cyclin-dependent regulation of G1 in mammalian fibroblasts (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-03-26
    Description: Eukaryotic cells become committed to proliferate during the G1 phase of the cell cycle. In budding yeast, commitment occurs when the catalytic subunit of a protein kinase, encoded by the CDC28 gene (the homolog of the fission yeast cdc2+ gene), binds to a positively acting regulatory subunit, a cyclin. Related kinases are also required for progression through the G1 phase in higher eukaryotes. The role of cyclins in controlling G1 progression in mammalian cells was tested by construction of fibroblasts that constitutively overexpress human cyclin E. This was found to shorten the duration of G1, decrease cell size, and diminish the serum requirement for the transition from G1 to S phase. These observations show that cyclin levels can be rate-limiting for G1 progression in mammalian cells and suggest that cyclin synthesis may be the target of physiological signals that control cell proliferation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ohtsubo, M -- Roberts, J M -- New York, N.Y. -- Science. 1993 Mar 26;259(5103):1908-12.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Basic Sciences, Fred Hutchinson Cancer Research Center, Seattle, WA 98104.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8384376" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Division/physiology ; Cell Line ; Cloning, Molecular ; Cyclins/genetics/*physiology ; Fibroblasts/*cytology/metabolism ; Flow Cytometry ; G1 Phase/*physiology ; Gene Expression ; Genetic Vectors ; Humans ; Kanamycin Kinase ; Male ; Phosphotransferases/genetics ; Rats ; Recombinant Fusion Proteins/metabolism ; Retroviridae/genetics ; S Phase/physiology ; Time Factors ; Transfection
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  • 85
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    Treatment and prevention of rat glioblastoma by immunogenic C6 cells expressing antisense insulin-like growth factor I RNA (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-01-01
    Description: Rat C6 glioma cells express insulin-like growth factor I (IGF-I) and form rapidly growing tumors in syngeneic animals. When transfected with an episome-based vector encoding antisense IGF-I complementary DNA, these cells lost tumorigenicity. Subcutaneous injection of IGF-I antisense-transfected C6 cells into rats prevented formation of both subcutaneous tumors and brain tumors induced by nontransfected C6 cells. The antisense-transfected cells also caused regression of established brain glioblastomas when injected at a point distal to the tumor. These antitumor effects result from a glioma-specific immune response involving CD8+ lymphocytes. Antisense blocking of IGF-I expression may reverse a phenotype that allows C6 glioma cells to evade the immune system.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Trojan, J -- Johnson, T R -- Rudin, S D -- Ilan, J -- Tykocinski, M L -- CA-43703/CA/NCI NIH HHS/ -- HD-18271/HD/NICHD NIH HHS/ -- HD-25004/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 1993 Jan 1;259(5091):94-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉INSERM, Paris.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8418502" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens, CD8/*immunology ; Brain Neoplasms/immunology/pathology/*prevention & control/*therapy ; Cytotoxicity, Immunologic ; DNA, Recombinant ; Glioma/immunology/pathology/*prevention & control/*therapy ; Immunohistochemistry ; Insulin-Like Growth Factor I/*genetics ; RNA, Antisense/pharmacology/*therapeutic use ; Rats ; T-Lymphocyte Subsets/*immunology ; *Transfection ; Tumor Cells, Cultured
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  • 86
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    HLA-A11 epitope loss isolates of Epstein-Barr virus from a highly A11+ population (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-04-02
    Description: Cytotoxic T lymphocytes (CTLs) control viral infections by recognizing viral peptides presented by major histocompatibility complex (MHC) class I molecules. Human leukocyte antigen (HLA)-A11-restricted CTLs that recognize peptide residues 416 to 424 of the Epstein-Barr virus (EBV) nuclear antigen-4 frequently dominate EBV-induced responses in A11+ Caucasian donors. This epitope is conserved in type A EBV strains from Caucasians and central African populations, where A11 is relatively infrequent. However, strains from highly A11+ populations in New Guinea carry a lysine-to-threonine mutation at residue 424 that abrogates CTL recognition and binding of the peptide to nascent A11 molecules. The results suggest that evolution of a widespread and genetically stable virus such as EBV is influenced by pressure from MHC-restricted CTL responses.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉de Campos-Lima, P O -- Gavioli, R -- Zhang, Q J -- Wallace, L E -- Dolcetti, R -- Rowe, M -- Rickinson, A B -- Masucci, M G -- 2RO1 CA30264/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1993 Apr 2;260(5104):98-100.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Tumor Biology, Karolinska Institute, Stockholm, Sweden.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7682013" target="_blank"〉PubMed〈/a〉
    Keywords: Africa ; Antigens, Viral/genetics/*immunology ; Cell Line, Transformed ; Cell Nucleus/*immunology ; Cell Transformation, Viral ; DNA-Binding Proteins/genetics/*immunology ; Epitopes/genetics/immunology ; Epstein-Barr Virus Nuclear Antigens ; European Continental Ancestry Group ; Gene Frequency ; HLA-A Antigens/genetics/*immunology ; HLA-A11 Antigen ; Herpesvirus 4, Human/*immunology ; Humans ; New Guinea ; Point Mutation ; T-Lymphocytes, Cytotoxic/*immunology ; Transfection
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  • 87
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    Mineralocorticoid and glucocorticoid receptor activities distinguished by nonreceptor factors at a composite response element (1993)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1993-02-19
    Description: Mineralocorticoid and glucocorticoid hormones elicit distinct physiologic responses, yet the mineralocorticoid receptor (MR) and glucocorticoid receptor (GR) bind to and activate transcription similarly from a consensus simple hormone response element (HRE). The activities of GR and MR at plfG, a 25-base pair composite response element to which both the steroid receptors and transcription factor AP1 can bind, are analyzed here. Under conditions in which GR represses AP1-stimulated transcription from plfG, MR was inactive. With the use of MR-GR chimeras, a segment of the NH2-terminal region of GR (amino acids 105 to 440) was shown to be required for this repression. Thus, the distinct physiologic effects mediated by MR and GR may be determined by differential interactions of nonreceptor factors with specific receptor domains at composite response elements.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pearce, D -- Yamamoto, K R -- New York, N.Y. -- Science. 1993 Feb 19;259(5098):1161-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Biophysics, University of California, San Francisco 94143-0448.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8382376" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Line ; Chloramphenicol O-Acetyltransferase/genetics/metabolism ; Corticosterone/*pharmacology ; DNA/*metabolism ; DNA-Binding Proteins/*metabolism ; HeLa Cells ; Humans ; Hydrocortisone/*pharmacology ; Mineralocorticoids/*metabolism ; Plasmids ; Proto-Oncogene Proteins c-jun/*metabolism ; Receptors, Glucocorticoid/genetics/*metabolism ; Receptors, Mineralocorticoid ; Receptors, Steroid/genetics/*metabolism ; Recombinant Fusion Proteins/metabolism ; Signal Transduction ; *Transcription, Genetic/drug effects ; Transfection ; Zinc Fingers/genetics/physiology
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  • 88
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    Characterization of a presynaptic glutamate receptor (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-10-15
    Description: Glutamate receptors mediate excitatory neurotransmission in the brain and are important in the formation of memory and in some neurodegenerative disorders. A complementary DNA clone that encoded a 33-kilodalton protein (GR33) was obtained by screening a library with an antibody generated against glutamate binding proteins. The sequence of GR33 is identical to that of the recently reported presynaptic protein syntaxin. When GR33 was expressed in Xenopus oocytes, it formed glutamate-activated ion channels that are pharmacologically similar to those of N-methyl-D-aspartate receptors but with different electrophysiological properties. Mutation of the leucine 278 residue in the single putative transmembrane segment of GR33 affects the properties of the channel. Thus, in vivo GR33 may be a presynaptic glutamate receptor.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Smirnova, T -- Stinnakre, J -- Mallet, J -- New York, N.Y. -- Science. 1993 Oct 15;262(5132):430-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratoire de genetique moleculaire de la neurotransmission et des processus neurodegeneratifs, Centre National de la Recherche Scientifique (CNRS), Gif sur Yvette, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8105537" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens, Surface/chemistry ; Brain/embryology ; Brain Chemistry ; Calcium/metabolism ; Cells, Cultured ; Cloning, Molecular ; Glutamates/pharmacology ; Glutamic Acid ; Humans ; Membrane Potentials ; Mutagenesis, Site-Directed ; N-Methylaspartate/pharmacology ; Nerve Tissue Proteins/chemistry ; Neurons/chemistry ; Oocytes ; Rats ; Rats, Wistar ; Receptors, Glutamate/chemistry/genetics/*metabolism ; Receptors, N-Methyl-D-Aspartate/metabolism ; Receptors, Presynaptic/chemistry/genetics/*metabolism ; Syntaxin 1 ; Xenopus
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  • 89
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    Carbon monoxide: a putative neural messenger (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-01-15
    Description: Carbon monoxide, an activator of guanylyl cyclase, is formed by the action of the enzyme heme oxygenase. By in situ hybridization in brain slices, discrete neuronal localization of messenger RNA for the constitutive form of heme oxygenase throughout the brain has been demonstrated. This localization is essentially the same as that for soluble guanylyl cyclase messenger RNA. In primary cultures of olfactory neurons, zinc protoporphyrin-9, a potent selective inhibitor of heme oxygenase, depletes endogenous guanosine 3',5'-monophosphate (cGMP). Thus, carbon monoxide, like nitric oxide, may be a physiologic regulator of cGMP. These findings, together with the neuronal localizations of heme oxygenase, suggest that carbon monoxide may function as a neurotransmitter.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Verma, A -- Hirsch, D J -- Glatt, C E -- Ronnett, G V -- Snyder, S H -- DA00266/DA/NIDA NIH HHS/ -- MH18501/MH/NIMH NIH HHS/ -- NS02131/NS/NINDS NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1993 Jan 15;259(5093):381-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurology, Walter Reed Army Medical Center, Washington, DC 20307.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7678352" target="_blank"〉PubMed〈/a〉
    Keywords: 5-Aminolevulinate Synthetase/analysis/genetics ; Amino Acid Oxidoreductases/analysis/genetics ; Animals ; Animals, Newborn ; Base Sequence ; Brain/*enzymology ; Carbon Monoxide/*metabolism ; Cells, Cultured ; Cyclic GMP/*metabolism ; Guanylate Cyclase/analysis/genetics ; Heme Oxygenase (Decyclizing)/*analysis/genetics ; In Situ Hybridization ; Molecular Sequence Data ; NADPH-Ferrihemoprotein Reductase/analysis/genetics ; Neurons/*enzymology ; Neurotransmitter Agents/*metabolism ; Nitric Oxide Synthase ; Oligodeoxyribonucleotides/chemistry ; RNA, Messenger/analysis ; Rats
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  • 90
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    A nonpeptidyl growth hormone secretagogue (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-06-11
    Description: A nonpeptidyl secretagogue for growth hormone of the structure 3-amino-3-methyl-N-(2,3,4,5-tetrahydro-2-oxo-1-([2'-(1H-tetrazol-5 -yl) (1,1'-biphenyl)-4-yl]methyl)-1H-1-benzazepin-3(R)-yl)-butanamid e (L-692,429) has been identified. L-692,429 synergizes with the natural growth hormone secretagogue growth hormone-releasing hormone and acts through an alternative signal transduction pathway. The mechanism of action of L-692,429 and studies with peptidyl and nonpeptidyl antagonists suggest that this molecule is a mimic of the growth hormone-releasing hexapeptide His-D-Trp-Ala-Trp-D-Phe-Lys-NH2 (GHRP-6). L-692,429 is an example of a nonpeptidyl specific secretagogue for growth hormone.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Smith, R G -- Cheng, K -- Schoen, W R -- Pong, S S -- Hickey, G -- Jacks, T -- Butler, B -- Chan, W W -- Chaung, L Y -- Judith, F -- New York, N.Y. -- Science. 1993 Jun 11;260(5114):1640-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Basic Animal Science Research, Merck Research Laboratories, Rahway, NJ 07065.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8503009" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Benzazepines/*pharmacology ; Cells, Cultured ; Dogs ; Growth Hormone/*drug effects/secretion ; Male ; Membrane Potentials/drug effects ; Molecular Sequence Data ; Oligopeptides/chemistry/pharmacology ; Pituitary Gland, Anterior/drug effects/secretion ; Rats ; Second Messenger Systems/drug effects ; Stereoisomerism ; Structure-Activity Relationship ; Tetrazoles/*pharmacology
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 91
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    A link between cyclin A expression and adhesion-dependent cell cycle progression (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-12-03
    Description: Cell adhesion has an essential role in regulating proliferation during the G1 phase of the cell cycle, and loss of this adhesion requirement is a classic feature of oncogenic transformation. The appearance of cyclin A messenger RNA and protein in late G1 was dependent on cell adhesion in both NRK and NIH 3T3 fibroblasts. In contrast, the expression of Cdc2, Cdk2, cyclin D1, and cyclin E was independent of adhesion in both cell lines. Transfection of NRK cells with a cyclin A complementary DNA resulted in adhesion-independent accumulation of cyclin A protein and cyclin A-associated kinase activity. These transfected cells also entered S phase and complete multiple rounds of cell division in the absence of cell adhesion. Thus, cyclin A is a target of the adhesion-dependent signals that control cell proliferation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Guadagno, T M -- Ohtsubo, M -- Roberts, J M -- Assoian, R K -- GM48224/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1993 Dec 3;262(5139):1572-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Molecular Biophysics, Columbia University, New York, NY 10032.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8248807" target="_blank"〉PubMed〈/a〉
    Keywords: 3T3 Cells ; Animals ; CDC2 Protein Kinase/biosynthesis ; *CDC2-CDC28 Kinases ; Cell Adhesion/*physiology ; Cell Cycle/*physiology ; Cell Line ; Cyclin-Dependent Kinase 2 ; *Cyclin-Dependent Kinases ; Cyclins/*biosynthesis ; Fibroblasts/cytology/metabolism ; Gene Expression Regulation ; Humans ; Mice ; Protein Kinases/biosynthesis ; *Protein-Serine-Threonine Kinases ; Rats ; Transfection
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 92
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    Structure and functional expression of a member of the low voltage-activated calcium channel family (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-05-21
    Description: Oscillatory firing patterns are an intrinsic property of some neurons and have an important function in information processing. In some cells, low voltage-activated calcium channels have been proposed to underlie a depolarizing potential that regulates bursting. The sequence of a rat brain calcium channel alpha 1 subunit (rbE-II) was deduced. Although it is structurally related to high voltage-activated calcium channels, the rbE-II channel transiently activated at negative membrane potentials, required a strong hyperpolarization to deinactivate, and was highly sensitive to block by nickel. In situ hybridization showed that rbE-II messenger RNA is expressed in regions throughout the central nervous system. The electrophysiological properties of the rbE-II current are consistent with a type of low voltage-activated calcium channel that requires membrane hyperpolarization for maximal activity, which suggests that rbE-II may be involved in the modulation of firing patterns.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Soong, T W -- Stea, A -- Hodson, C D -- Dubel, S J -- Vincent, S R -- Snutch, T P -- New York, N.Y. -- Science. 1993 May 21;260(5111):1133-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Biotechnology Laboratory, University of British Columbia, Vancouver, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8388125" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; *Brain Chemistry ; Calcium Channels/*chemistry/genetics/physiology ; Calcium Channels, R-Type ; Cation Transport Proteins ; Cloning, Molecular ; Electric Conductivity ; Hippocampus/chemistry ; In Situ Hybridization ; Membrane Potentials ; Membrane Proteins/*chemistry/genetics/physiology ; Molecular Sequence Data ; Nerve Tissue Proteins/*chemistry/genetics/physiology ; RNA, Messenger/analysis/genetics ; Rats ; Sequence Alignment
    Print ISSN: 0036-8075
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  • 93
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    Common forms of synaptic plasticity in the hippocampus and neocortex in vitro (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-06-04
    Description: Activity-dependent synaptic plasticity in the superficial layers of juvenile cat and adult rat visual neocortex was compared with that in adult rat hippocampal field CA1. Stimulation of neocortical layer IV reliably induced synaptic long-term potentiation (LTP) and long-term depression (LTD) in layer III with precisely the same types of stimulation protocols that were effective in CA1. Neocortical LTP and LTD were specific to the conditioned pathway and, as in the hippocampus, were dependent on activation of N-methyl-D-aspartate receptors. These results provide strong support for the view that common principles may govern experience-dependent synaptic plasticity in CA1 and throughout the superficial layers of the mammalian neocortex.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kirkwood, A -- Dudek, S M -- Gold, J T -- Aizenman, C D -- Bear, M F -- New York, N.Y. -- Science. 1993 Jun 4;260(5113):1518-21.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neuroscience, Brown University, Providence, RI 02912.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8502997" target="_blank"〉PubMed〈/a〉
    Keywords: Action Potentials ; Aging/physiology ; Animals ; Cats ; Cerebral Cortex/*physiology ; Electric Stimulation ; Hippocampus/*physiology ; In Vitro Techniques ; Neural Pathways/physiology ; Neuronal Plasticity/*physiology ; Rats ; Receptors, N-Methyl-D-Aspartate/physiology ; Synapses/*physiology
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  • 94
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    IRS-1: essential for insulin- and IL-4-stimulated mitogenesis in hematopoietic cells (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-09-17
    Description: Although several interleukin-3 (IL-3)-dependent cell lines proliferate in response to IL-4 or insulin, the 32D line does not. Insulin and IL-4 sensitivity was restored to 32D cells by expression of IRS-1, the principal substrate of the insulin receptor. Although 32D cells possessed receptors for both factors, they lacked the IRS-1--related protein, 4PS, which becomes phosphorylated by tyrosine in insulin- or IL-4--responsive lines after stimulation. These results indicate that factors that bind unrelated receptors can use similar mitogenic signaling pathways in hematopoietic cells and that 4PS and IRS-1 are functionally similar proteins that are essential for insulin- and IL-4--induced proliferation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wang, L M -- Myers, M G Jr -- Sun, X J -- Aaronson, S A -- White, M -- Pierce, J H -- DK-43808/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1993 Sep 17;261(5128):1591-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Cellular and Molecular Biology, National Cancer Institute, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8372354" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Division/drug effects ; Cell Line ; Hematopoietic Stem Cells/*cytology/drug effects ; Insulin/*pharmacology ; Insulin Receptor Substrate Proteins ; Interleukin-4/*pharmacology ; Phosphoproteins/*metabolism ; Phosphorylation ; Receptor, Insulin/metabolism ; Receptors, Interleukin-4 ; Receptors, Mitogen/metabolism ; Transfection ; Tyrosine/metabolism
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  • 95
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    Inactivation of the type II receptor reveals two receptor pathways for the diverse TGF-beta activities (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-05-28
    Description: Transforming growth factor-beta (TGF-beta) is a multifunctional protein that regulates cell proliferation and differentiation and extracellular matrix production. Although two receptor types, the type I and type II receptors, have been implicated in TGF-beta-induced signaling, it is unclear how the many activities of TGF-beta are mediated through these receptors. With the use of cells overexpressing truncated type II receptors as dominant negative mutants to selectively block type II receptor signaling, the existence of two receptor pathways was shown. The type II receptors, possibly in conjunction with type I receptors, mediate the induction of growth inhibition and hypophosphorylation of the retinoblastoma gene product pRB. The type I receptors are responsible for effects on extracellular matrix, such as the induction of fibronectin and plasminogen activator inhibitor I, and for increased JunB expression. Selective inactivation of the type II receptors alters the TGF-beta response in a similar manner to the functional inactivation of pRB, suggesting a role for pRB in the type II, but not the type I, receptor pathway.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chen, R H -- Ebner, R -- Derynck, R -- New York, N.Y. -- Science. 1993 May 28;260(5112):1335-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Growth and Development, University of California, San Francisco 94143.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8388126" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Division/drug effects ; Cell Line ; DNA/biosynthesis ; Down-Regulation ; Fibronectins/biosynthesis ; Plasminogen Activator Inhibitor 1/biosynthesis ; Protein-Serine-Threonine Kinases ; Proto-Oncogene Proteins c-jun/genetics ; Receptors, Cell Surface/genetics/*physiology ; *Receptors, Transforming Growth Factor beta ; Retinoblastoma Protein/metabolism ; Signal Transduction ; Transfection ; Transforming Growth Factor beta/*pharmacology/physiology
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  • 96
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    SH2-containing phosphotyrosine phosphatase as a target of protein-tyrosine kinases (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-03-12
    Description: A mouse phosphotyrosine phosphatase containing two Src homology 2 (SH2) domains, Syp, was identified. Syp bound to autophosphorylated epidermal growth factor (EGF) and platelet-derived growth factor (PDGF) receptors through its SH2 domains and was rapidly phosphorylated on tyrosine in PDGF- and EGF-stimulated cells. Furthermore, Syp was constitutively phosphorylated on tyrosine in cells transformed by v-src. This mammalian phosphatase is most closely related, especially in its SH2 domains, to the corkscrew (csw) gene product of Drosophila, which is required for signal transduction downstream of the Torso receptor tyrosine kinase. The Syp gene is widely expressed throughout embryonic mouse development and in adult tissues. Thus, Syp may function in mammalian embryonic development and as a common target of both receptor and nonreceptor tyrosine kinases.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Feng, G S -- Hui, C C -- Pawson, T -- New York, N.Y. -- Science. 1993 Mar 12;259(5101):1607-11.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Molecular and Developmental Biology, Samuel Lunenfeld Research Institute, Mount Sinai Hospital, Toronto, Ontario, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8096088" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Cell Line, Transformed ; Cell Transformation, Neoplastic ; Embryo, Mammalian ; Embryonic and Fetal Development ; Epidermal Growth Factor/pharmacology ; *Genes, src ; Humans ; Intracellular Signaling Peptides and Proteins ; Kinetics ; Mice ; Molecular Sequence Data ; Oligodeoxyribonucleotides ; Phosphorylation ; Platelet-Derived Growth Factor/pharmacology ; Poly A/isolation & purification/metabolism ; Polymerase Chain Reaction ; Protein Tyrosine Phosphatase, Non-Receptor Type 11 ; Protein Tyrosine Phosphatase, Non-Receptor Type 6 ; Protein Tyrosine Phosphatases/genetics/*metabolism ; Protein-Tyrosine Kinases/*metabolism ; RNA, Messenger/isolation & purification/metabolism ; Rats ; Receptor, Epidermal Growth Factor/metabolism ; Receptors, Platelet-Derived Growth Factor/genetics/metabolism ; Sequence Homology, Amino Acid ; Transfection
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  • 97
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    New marker for nerve damage (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-03-12
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stone, R -- New York, N.Y. -- Science. 1993 Mar 12;259(5101):1541.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8456282" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Astrocytes/drug effects/pathology ; Biological Assay ; Biomarkers ; Brain/drug effects/*pathology ; Glial Fibrillary Acidic Protein/*analysis ; Neurons/drug effects/*pathology ; Neurotoxins/*toxicity ; Nitriles/toxicity ; Rats ; United States ; United States Environmental Protection Agency
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  • 98
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    Calcium sparks: elementary events underlying excitation-contraction coupling in heart muscle (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-10-29
    Description: Spontaneous local increases in the concentration of intracellular calcium, called "calcium sparks," were detected in quiescent rat heart cells with a laser scanning confocal microscope and the fluorescent calcium indicator fluo-3. Estimates of calcium flux associated with the sparks suggest that calcium sparks result from spontaneous openings of single sarcoplasmic reticulum (SR) calcium-release channels, a finding supported by ryanodine-dependent changes of spark kinetics. At resting intracellular calcium concentrations, these SR calcium-release channels had a low rate of opening (approximately 0.0001 per second). An increase in the calcium content of the SR, however, was associated with a fourfold increase in opening rate and resulted in some sparks triggering propagating waves of increased intracellular calcium concentration. The calcium spark is the consequence of elementary events underlying excitation-contraction coupling and provides an explanation for both spontaneous and triggered changes in the intracellular calcium concentration in the mammalian heart.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cheng, H -- Lederer, W J -- Cannell, M B -- New York, N.Y. -- Science. 1993 Oct 29;262(5134):740-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physiology, University of Maryland School of Medicine, Baltimore 21201.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8235594" target="_blank"〉PubMed〈/a〉
    Keywords: Aniline Compounds ; Animals ; Calcium/metabolism/*physiology ; Calcium Channels/drug effects/physiology ; Fluorescent Dyes ; In Vitro Techniques ; Ion Channel Gating/physiology ; Microscopy, Fluorescence/methods ; Models, Biological ; Muscle Proteins/drug effects/physiology ; Myocardial Contraction/*physiology ; Myocardium/metabolism ; Rats ; Ryanodine/pharmacology ; Ryanodine Receptor Calcium Release Channel ; Sarcoplasmic Reticulum/metabolism ; Xanthenes
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  • 99
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    Predisposition to neoplastic transformation caused by gene replacement of H-ras1 (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-06-04
    Description: Homologous recombination was used to introduce a nominally transforming mutation into an endogenous H-ras1 gene in Rat1 fibroblasts. Although both the mutant and the remaining normal allele were expressed equally, the heterozygous cells were not neoplastically transformed. Instead, spontaneously transformed cells arose from the heterozygotes at a low frequency, and the majority of these cells had amplified the mutant allele. Thus, the activated H-ras1 allele was not by itself dominant over the normal allele but predisposed cells to transformation by independent events, such as amplification of the mutant allele.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Finney, R E -- Bishop, J M -- CA 44338/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1993 Jun 4;260(5113):1524-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉George Williams Hooper Foundation, University of California, San Francisco 94143.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8502998" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Animals ; Base Sequence ; Cell Division/genetics ; Cell Line ; Cell Line, Transformed ; Cell Transformation, Neoplastic/*genetics ; Genes, ras/*genetics ; Mice ; Mice, Nude ; Molecular Sequence Data ; Neoplasm Transplantation ; Point Mutation ; Rats ; Recombination, Genetic
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 100
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    Promising protein for Parkinson's (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-05-21
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Weiss, R -- New York, N.Y. -- Science. 1993 May 21;260(5111):1072-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8493547" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Blood-Brain Barrier ; Cell Line ; Cell Survival/drug effects ; Dopamine/*biosynthesis ; Humans ; Nerve Growth Factors ; Nerve Tissue Proteins/genetics/isolation & purification/*pharmacology ; Neuroglia/*metabolism ; Neurons/cytology/*drug effects/metabolism ; Parkinson Disease/*drug therapy ; Rats
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