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  • Mice  (97)
  • American Association for the Advancement of Science (AAAS)  (97)
  • American Association for the Advancement of Science
  • American Chemical Society (ACS)
  • National Academy of Sciences
  • 1990-1994  (97)
  • 1980-1984
  • 1991  (97)
Collection
Publisher
  • American Association for the Advancement of Science (AAAS)  (97)
  • American Association for the Advancement of Science
  • American Chemical Society (ACS)
  • National Academy of Sciences
  • Springer  (4)
Years
  • 1990-1994  (97)
  • 1980-1984
Year
  • 1
    Publication Date: 1991-03-08
    Description: The two mouse genes, En-1 and En-2, that are homologs of the Drosophila segmentation gene engrailed, show overlapping spatially restricted patterns of expression in the neural tube during embryogenesis, suggestive of a role in regional specification. Mice homozygous for a targeted mutation that deletes the homeobox were viable and showed no obvious defects in embryonic development. This may be due to functional redundancy of En-2 and the related En-1 gene product during embryogenesis. Consistent with this hypothesis, the mutant mice showed abnormal foliation in the adult cerebellum, where En-2, and not En-1, is normally expressed.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Joyner, A L -- Herrup, K -- Auerbach, B A -- Davis, C A -- Rossant, J -- HD25334/HD/NICHD NIH HHS/ -- NS18381/NS/NINDS NIH HHS/ -- NS20591/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1991 Mar 8;251(4998):1239-43.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉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/1672471" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Blastocyst ; Cell Line ; Cerebellum/*anatomy & histology/embryology/pathology ; Chimera ; *Chromosome Deletion ; Female ; *Genes, Homeobox ; Male ; Mice ; Mice, Inbred BALB C ; Mice, Inbred C57BL ; Nervous System/embryology ; Phenotype
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  • 2
    Publication Date: 1991-09-20
    Description: CD45 is a leukocyte-specific, transmembrane protein tyrosine phosphatase (PTPase) required for T cell responsiveness. How the activity of PTPases is regulated in vivo is unclear. Treatment of murine thymocytes and a variety of murine T cell lines with the calcium ionophore ionomycin decreased CD45 PTPase activity. Ionomycin treatment also led to a decreased phosphorylation of serine residues in CD45. These results indicate that increased intracellular calcium modulates CD45 PTPase activity, demonstrating regulation of CD45 PTPase activity in vivo, and also implicate serine dephosphorylation as a possible mechanism.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ostergaard, H L -- Trowbridge, I S -- CA-17733/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1991 Sep 20;253(5026):1423-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cancer Biology, Salk Institute, San Diego, CA 92186.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1654595" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens, CD/*metabolism ; Antigens, CD45 ; Cell Line ; Histocompatibility Antigens/*metabolism ; Ionomycin/*pharmacology ; Kinetics ; Mice ; Mice, Inbred BALB C ; Phosphoprotein Phosphatases/*metabolism ; Protein Tyrosine Phosphatases ; Spleen/drug effects/enzymology/immunology ; T-Lymphocytes/drug effects/*enzymology/immunology ; Thymus Gland/immunology
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  • 3
    Publication Date: 1991-08-02
    Description: Mammalian 3T3-L1 cells differentiate into adipocytes after continuous exposure to pharmacological doses of insulin or physiological doses of insulin-like growth factor I (IGF-1). Expression of transfected ras oncogenes led to differentiation of these cells into adipocytes in the absence of externally added insulin or IGF-I. Cells transfected with normal ras genes or the tyrosine kinase trk oncogene did not differentiate. Transfection with a dominant inhibitory ras mutant resulted in inhibition of differentiation. Exposure of untransfected 3T3-L1 cells to insulin stimulated formation of the active Ras.GTP complex. These observations indicate that Ras proteins participate in signal transduction pathways initiated by insulin and IGF-I in these cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Benito, M -- Porras, A -- Nebreda, A R -- Santos, E -- New York, N.Y. -- Science. 1991 Aug 2;253(5019):565-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Molecular Microbiology, National Institute of Allergy and Infectious Diseases, National Institute of Health, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1857988" target="_blank"〉PubMed〈/a〉
    Keywords: Adipose Tissue/*cytology ; Animals ; Blotting, Northern ; *Cell Differentiation ; Cell Line ; *Cell Transformation, Neoplastic ; Fibroblasts/cytology ; *Genes, ras ; Mice ; RNA, Messenger/analysis/genetics ; *Transfection
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  • 4
    Publication Date: 1991-05-03
    Description: A transition state analogue was used to produce a mouse antibody that catalyzes transesterification in water. The antibody behaves as a highly efficient catalyst with a covalent intermediate and the characteristic of induced fit. While some features of the catalytic pathway were programmed when the hapten was designed and reflect favorable substrate-antibody interactions, other features are a manifestation of the chemical potential of antibody diversity. The fact that antibodies recapitulate mechanisms and pathways previously thought to be a characteristic of highly evolved enzymes suggests that once an appropriate binding cavity is achieved, reaction pathways commensurate with the intrinsic chemical potential of proteins ensue.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wirsching, P -- Ashley, J A -- Benkovic, S J -- Janda, K D -- Lerner, R A -- GM43858-01/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1991 May 3;252(5006):680-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, Scripps Research Institute, La Jolla, CA 92037.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2024120" target="_blank"〉PubMed〈/a〉
    Keywords: Acylation ; Alcohols/metabolism ; Animals ; Antibodies, Monoclonal/immunology/*metabolism ; Antibody Specificity ; Binding Sites, Antibody ; *Catalysis ; Enzymes/metabolism ; Esterification ; Haptens ; Kinetics ; Mice ; Water
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  • 5
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1991-11-29
    Description: Cell membranes often are patchy, composed of lateral domains. These domains may be formed by barriers within or on either side of the membrane bilayer. Major histocompatibility complex (MHC) class 1 molecules that were either transmembrane- (H-2Db) or glycosylphosphatidylinositol (GPI)-anchored (Qa2) were labeled with antibody-coated gold particles and moved across the cell surface with a laser optical tweezers until they encountered a barrier, the barrier-free path length (BFP). At room temperature, the BFPs of Qa2 and H-2Db were 1.7 +/- 0.2 and 0.6 +/- 0.1 (micrometers +/- SEM), respectively. Barriers persisted at 34 degrees C, although the BFP for both MHC molecules was fivefold greater at 34 degrees C than at 23 degrees C. This indicates that barriers to lateral movement are primarily on the cytoplasmic half of the membrane and are dynamic.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Edidin, M -- Kuo, S C -- Sheetz, M P -- AL14584/PHS HHS/ -- GM 36277/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1991 Nov 29;254(5036):1379-82.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, Johns Hopkins University, Baltimore, MD 21218.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1835798" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antibodies, Monoclonal ; Cell Line ; Glycolipids/physiology ; Glycosylphosphatidylinositols ; Gold ; H-2 Antigens/*physiology ; Histocompatibility Antigens Class I/*physiology ; *Lipid Bilayers ; Membrane Glycoproteins/*physiology ; Mice ; Phosphatidylinositols/physiology ; Thermodynamics ; Transfection
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  • 6
    Publication Date: 1991-03-08
    Description: Engagement of the antigen-specific receptor (TCR) of CD4+ T lymphocytes without a second (costimulatory) signal prevents the subsequent production of interleukin-2 (IL-2) by these cells. Because IL-2 is a key immunoregulatory lymphokine and is also produced by a subset of CD8+ T cells that are able to kill target cells, the effect of engaging the TCR of one such clone in the absence of costimulatory signals was examined. The capacity for TCR-dependent IL-2 production was lost, indicating comparable costimulator-dependent signaling requirements for IL-2 production in CD4+ and CD8+ T cells. However, TCR-mediated cytotoxicity was not impaired, implying that costimulation is required for only certain TCR-dependent effector functions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Otten, G R -- Germain, R N -- New York, N.Y. -- Science. 1991 Mar 8;251(4998):1228-31.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Lymphocyte Biology Section, 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/1900952" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antibodies, Monoclonal/immunology ; Antigen-Presenting Cells/immunology ; Antigens, CD8 ; Antigens, Differentiation, T-Lymphocyte/*immunology ; Female ; Interleukin-2/biosynthesis/*physiology ; Kinetics ; Lymphocyte Activation ; Mice ; Mice, Inbred Strains ; Ovalbumin/immunology ; Rats ; Receptors, Antigen, T-Cell/*immunology ; Spleen/immunology/radiation effects ; T-Lymphocytes/*immunology
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  • 7
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1991-08-16
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kenyon, K -- Contente, S -- Trackman, P C -- Tang, J -- Kagan, H M -- Friedman, R M -- P01 HL13262/HL/NHLBI NIH HHS/ -- R01 CA37351-04A1/CA/NCI NIH HHS/ -- R37 AR18880/AR/NIAMS NIH HHS/ -- New York, N.Y. -- Science. 1991 Aug 16;253(5021):802.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pathology, Uniformed Services University of the Health Sciences, Bethesda, MD 20814.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1678898" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Blotting, Northern ; Cell Line ; *Cell Transformation, Neoplastic ; Gene Expression ; *Genes, Tumor Suppressor ; In Vitro Techniques ; Mice ; Protein-Lysine 6-Oxidase/*physiology ; RNA, Messenger/genetics
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  • 8
    Publication Date: 1991-04-26
    Description: DNA sequences associated with the mouse pink-eyed unstable mutation were identified in the absence of closely linked molecular markers and without prior knowledge of the encoded gene product. This was accomplished by "genome scanning," a technique in which high-resolution Southern blots of genomic DNAs were hybridized to a dispersed and moderately repetitive DNA sequence. In this assay, pink-eyed unstable DNA was distinguished from the DNA of wild-type and revertant mice by enhanced hybridization to one of several hundred resolved fragments. The fragment showing enhanced hybridization in pink-eyed unstable DNA was cloned and found to lie within a DNA duplication that is located close to, or within, the pink-eyed dilution locus. The duplication associated with the mouse pink-eyed unstable mutation may mediate the high reversion frequency characteristic of this mutation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Brilliant, M H -- Gondo, Y -- Eicher, E M -- CA06927/CA/NCI NIH HHS/ -- GM43840/GM/NIGMS NIH HHS/ -- RR05529/RR/NCRR NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1991 Apr 26;252(5005):566-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Cancer Research, Fox Chase Cancer Center, Philadelphia, PA 19111.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1673574" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Animals ; Blotting, Southern/methods ; DNA/genetics/isolation & purification ; Eye Color/*genetics ; *Genes ; Homozygote ; Mice ; Mice, Inbred C57BL ; Mice, Mutant Strains ; *Mutation ; Restriction Mapping ; Tyrosine 3-Monooxygenase/genetics
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  • 9
    Publication Date: 1991-12-20
    Description: Pancreatic islet cells are the targets of an autoimmune response in type I diabetes. In the nonobese diabetic (NOD) mouse model of autoimmune diabetes, expression of major histocompatibility complex (MHC) class I proteins was inversely correlated with diabetes; in this mouse a mutation in the MHC class II-linked gene for the putative MHC class I peptide transporter was also present. Mice deficient in MHC class I expression because they do not produce beta 2-microglobulin also developed late onset autoimmune diabetes. In cells from humans with type I diabetes expression of MHC class I was decreased; subsets of prediabetics categorized as most likely to become hyperglycemic also had low MHC class I. T cell responses to self antigens are faulty in diabetics. In sets of genetically identical twins that are discordant for diabetes, the defect appeared to reside with the antigen presenting cell. Thus, a lack of surface MHC class I protein is associated with autoimmune diabetes; the concomitant defect in antigen presentation may impair the development of self tolerance, which could result in autoimmune disease.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Faustman, D -- Li, X P -- Lin, H Y -- Fu, Y E -- Eisenbarth, G -- Avruch, J -- Guo, J -- New York, N.Y. -- Science. 1991 Dec 20;254(5039):1756-61.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine, Harvard Medical School, Massachusetts General Hospital, Charlestown 02129.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1763324" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Autoimmune Diseases/*genetics ; Cytotoxicity, Immunologic ; Diabetes Mellitus, Type 1/genetics/*immunology ; Diseases in Twins ; Flow Cytometry ; Gene Expression ; *Genes, MHC Class I ; Humans ; *Lymphocyte Activation ; Lymphocytes/*immunology ; Mice ; Mice, Inbred BALB C ; Mice, Inbred C57BL ; Mice, Inbred NOD ; Prediabetic State/genetics/immunology ; Spleen/immunology ; T-Lymphocytes/immunology
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  • 10
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1991-05-10
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marx, J -- New York, N.Y. -- Science. 1991 May 10;252(5007):779-80.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1674172" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Gene Expression Regulation, Enzymologic ; Hormones/*metabolism ; Mice ; Neurotransmitter Agents/metabolism ; Pro-Opiomelanocortin/metabolism ; Proprotein Convertase 2 ; Proprotein Convertases ; Protein Precursors/metabolism ; *Protein-Tyrosine Kinases ; Proto-Oncogene Proteins/metabolism ; Proto-Oncogene Proteins c-fes ; Serine Endopeptidases/*physiology
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  • 11
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1991-07-12
    Description: Mutations that cause pituitary dwarfism in the mouse reside in the gene encoding the transcription factor growth hormone factor 1 (GHF1 or pit1). These dwarf mice (dw and dwJ) are deficient in growth hormone (GH) and prolactin (PRL) synthesis and exhibit pituitary hypoplasia, suggesting a stem cell defect. With antisense oligonucleotide technology, a cell culture model of this genetic defect was developed. Specific inhibition of GHF1 synthesis by complementary oligonucleotides led to a marked decrease in GH and PRL expression and to a marked decrease in proliferation of somatotrophic cell lines. These results provide direct evidence that the homeodomain protein GHF1 is required not only for the establishment and maintenance of the differentiated phenotype but for cell proliferation as well.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Castrillo, J L -- Theill, L E -- Karin, M -- DK38527/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1991 Jul 12;253(5016):197-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, School of Medicine, University of California, San Diego, La Jolla 92093.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1677216" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antisense Elements (Genetics) ; Base Sequence ; *Cell Division ; Cells, Cultured ; DNA/biosynthesis ; DNA-Binding Proteins/*physiology ; Dwarfism/genetics ; Gene Expression Regulation ; *Genes, Homeobox ; Growth Hormone/genetics ; In Vitro Techniques ; Mice ; Molecular Sequence Data ; Pituitary Gland/*cytology/physiology ; Prolactin/genetics ; Transcription Factor Pit-1 ; Transcription Factors/*physiology
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  • 12
    Publication Date: 1991-02-01
    Description: Neurotransmitter receptors are generally clustered in the postsynaptic membrane. The mechanism of clustering was analyzed with fibroblast cell lines that were stably transfected with the four subunits for fetal (alpha, beta, gamma, delta) or adult (alpha, beta, epsilon, delta) type mouse muscle nicotinic acetylcholine receptors (AChRs). Immunofluorescent staining indicated that AChRs were dispersed on the surface of these cells. When transiently transfected with an expression construct encoding a 43-kilodalton protein that is normally concentrated under the postsynaptic membrane, AChRs expressed in these cells became aggregated in large cell-surface clusters, colocalized with the 43-kilodalton protein. This suggests that 43-kilodalton protein can induce AChR clustering and that cluster induction involves direct contact between AChR and 43-kilodalton protein.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Phillips, W D -- Kopta, C -- Blount, P -- Gardner, P D -- Steinbach, J H -- Merlie, J P -- R01 NS022356/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1991 Feb 1;251(4993):568-70.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, Washington University School of Medicine, St. Louis, MO 63110.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1703661" target="_blank"〉PubMed〈/a〉
    Keywords: Acetylcholine/pharmacology ; Animals ; Cell Membrane/physiology ; Fetus ; Fibroblasts/cytology/physiology ; Fluorescent Antibody Technique ; Ion Channels/drug effects/physiology ; Macromolecular Substances ; Mice ; Molecular Weight ; Muscles/physiology ; Receptors, Nicotinic/analysis/genetics/*physiology ; Recombinant Proteins/analysis/metabolism ; Transfection
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  • 13
    Publication Date: 1991-05-03
    Description: The circumsporozoite (CS) protein has been the target for development of malaria sporozoite vaccines for a decade. However, immunization with subunit vaccines based on the CS protein has never given the complete protection found after immunization with irradiated sporozoites. BALB/c mice immunized with irradiated Plasmodium yoelii sporozoites produced antibodies and cytotoxic T cells against a 140-kilodalton protein, sporozoite surface protein 2 (SSP2). Mice immunized with P815 cells that had been transfected with either SSP2 or CS genes were partially protected, and those immunized with a mixture of SSP2 and CS transfectants were completely protected against malaria. These studies emphasize the importance of vaccine delivery systems in achieving protection and define a multi-antigen sporozoite vaccine.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Khusmith, S -- Charoenvit, Y -- Kumar, S -- Sedegah, M -- Beaudoin, R L -- Hoffman, S L -- New York, N.Y. -- Science. 1991 May 3;252(5006):715-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Malaria Program, Naval Medical Research Institute, Bethesda, MD 20889.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1827210" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antibodies, Monoclonal/immunology ; Antibodies, Protozoan/immunology ; Antigens, Protozoan/genetics/*immunology ; Immunization ; Malaria/*prevention & control ; Mice ; Mice, Inbred BALB C ; Molecular Weight ; Plasmodium yoelii/*immunology ; Protozoan Proteins/genetics/*immunology ; *Protozoan Vaccines ; T-Lymphocytes, Cytotoxic/immunology ; T-Lymphocytes, Helper-Inducer/immunology ; T-Lymphocytes, Regulatory/immunology ; Transfection ; *Vaccination
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  • 14
    Publication Date: 1991-03-29
    Description: Cloned integrin alpha 2 subunit complementary DNA was expressed on human rhabdomyosarcoma (RD) cells to give a functional VLA-2 (alpha 2 beta 1) adhesion receptor. The VLA-2-positive RDA2 cells not only showed increased adhesion to collagen and laminin in vitro, but also formed substantially more metastatic tumor colonies in nude mice after either intravenous or subcutaneous injection. These results show that a specific adhesion receptor (VLA-2) can markedly enhance both experimental and spontaneous metastasis. In contrast to the metastasis results, there was no difference in either the in vitro growth rate or apparent in vivo tumorigenicity of RD and RDA2 cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chan, B M -- Matsuura, N -- Takada, Y -- Zetter, B R -- Hemler, M E -- CA 37393/CA/NCI NIH HHS/ -- GM 38903/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1991 Mar 29;251(5001):1600-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉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/2011740" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Cell Adhesion ; Cell Line ; Collagen ; Fibronectins ; Humans ; Kinetics ; Laminin ; Lung Neoplasms/pathology/secondary ; Mice ; Mice, Nude ; Neoplasm Metastasis ; Neoplasm Transplantation ; Receptors, Very Late Antigen/genetics/*physiology ; Rhabdomyosarcoma/*pathology ; Transplantation, Heterologous
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  • 15
    Publication Date: 1991-07-05
    Description: Molecular cloning of the t(10;14)(q24;q11) recurrent breakpoint of T cell acute lymphoblastic leukemia has demonstrated a transcript for the candidate gene TCL3. Characterization of this gene from chromosome segment 10q24 revealed it to be a new homeobox, HOX11. The HOX11 homeodomain is most similar to that of the murine gene Hlx and possesses a markedly glycine-rich variable region and an acidic carboxyl terminus. HOX11, while expressed in liver, was not detected in normal thymus or T cells. This lineage-restricted homeobox gene is deregulated upon translocation into the T cell receptor locus where it may act as an oncogene.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hatano, M -- Roberts, C W -- Minden, M -- Crist, W M -- Korsmeyer, S J -- 1 PO1 CA49712/CA/NCI NIH HHS/ -- CA 21765/CA/NCI NIH HHS/ -- CA 30969/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1991 Jul 5;253(5015):79-82.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Washington University School of Medicine, St. Louis, MO 63110.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1676542" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Blotting, Northern ; Chromosomes, Human, Pair 10 ; Chromosomes, Human, Pair 14 ; Cloning, Molecular ; *Gene Expression Regulation, Neoplastic ; *Genes, Homeobox ; Humans ; Leukemia-Lymphoma, Adult T-Cell/*genetics ; Mice ; Molecular Sequence Data ; Receptors, Antigen, T-Cell/genetics ; Restriction Mapping ; Sequence Homology, Nucleic Acid ; *Translocation, Genetic
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  • 16
    Publication Date: 1991-06-07
    Description: Thy-1+ dendritic epidermal T cells (dECs) express invariant gamma delta antigen receptors and are found in intimate contact with keratinocytes in murine epidermis--thus raising the possibility that keratinocytes express a ligand for the antigen receptor of these T cells. Thy-1+ dECs were stimulated to produce lymphokines by interaction with keratinocytes in vitro. This stimulation was mediated through the dEC antigen receptor and did not appear to be restricted by the major histocompatibility complex. Thus, dECs can recognize self antigens and may participate in immune surveillance for cellular damage rather than for foreign antigens.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Havran, W L -- Chien, Y H -- Allison, J P -- AI26942/AI/NIAID NIH HHS/ -- CA40041/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1991 Jun 7;252(5011):1430-2.〈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/1828619" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Autoantigens/*immunology ; Cell Line ; Dendrites/immunology ; Epidermis ; *Immunity, Cellular ; In Vitro Techniques ; Interleukin-2/secretion ; Keratinocytes/physiology ; Mice ; Mice, Inbred BALB C ; Receptors, Antigen, T-Cell/*physiology ; Receptors, Antigen, T-Cell, gamma-delta ; T-Lymphocytes/*immunology
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  • 17
    Publication Date: 1991-01-04
    Description: An expression cloning strategy was devised to isolate the keratinocyte growth factor (KGF) receptor complementary DNA. NIH/3T3 fibroblasts, which secrete this epithelial cell-specific mitogen, were transfected with a keratinocyte expression complementary DNA library. Among several transformed foci identified, one demonstrated the acquisition of specific high-affinity KGF binding sites. The pattern of binding competition by related fibroblast growth factors (FGFs) indicated that this receptor had high affinity for acidic FGF as well as KGF. The rescued 4.2-kilobase complementary DNA was shown to encode a predicted membrane-spanning tyrosine kinase related to but distinct from the basic FGF receptor. This expression cloning approach may be generally applicable to the isolation of genes that constitute limiting steps in mitogenic signaling pathways.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Miki, T -- Fleming, T P -- Bottaro, D P -- Rubin, J S -- Ron, D -- Aaronson, S A -- New York, N.Y. -- Science. 1991 Jan 4;251(4989):72-5.〈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/1846048" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Binding, Competitive ; Cell Line ; *Cloning, Molecular ; DNA/*genetics ; Fibroblast Growth Factor 10 ; Fibroblast Growth Factor 7 ; Fibroblast Growth Factors/metabolism ; Fibroblasts/metabolism ; *Gene Expression ; Growth Substances/metabolism ; Mice ; Molecular Sequence Data ; Nucleic Acid Hybridization ; Plasmids ; Receptor, Fibroblast Growth Factor, Type 2 ; Receptors, Cell Surface/*genetics/metabolism ; *Receptors, Fibroblast Growth Factor ; Recombinant Proteins/metabolism ; Transfection ; Transformation, Genetic
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  • 18
    Publication Date: 1991-06-21
    Description: Basic fibroblast growth factor (bFGF) binds to heparan sulfate proteoglycans at the cell surface and to receptors with tyrosine kinase activity. Prevention of binding between cell surface heparan sulfate and bFGF (i) substantially reduces binding of fibroblast growth factor to its cell-surface receptors, (ii) blocks the ability of bFGF to support the growth of Swiss 3T3 fibroblasts, and (iii) induces terminal differentiation of MM14 skeletal muscle cells, which is normally repressed by fibroblast growth factor. These results indicate that cell surface heparan sulfate is directly involved in bFGF cell signaling.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rapraeger, A C -- Krufka, A -- Olwin, B B -- 5T32H007118/PHS HHS/ -- AR39467/AR/NIAMS NIH HHS/ -- HD21881/HD/NICHD NIH HHS/ -- R01 AR039467/AR/NIAMS NIH HHS/ -- R01 HD021881/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 1991 Jun 21;252(5013):1705-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pathology, University of Wisconsin, Madison 53706.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1646484" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Differentiation ; Cell Division ; Cell Line ; Chlorates/pharmacology ; Fibroblast Growth Factor 2/*metabolism ; Fibroblasts/*cytology ; Heparitin Sulfate/*physiology ; In Vitro Techniques ; Mice ; Muscles/*cytology ; Polysaccharide-Lyases/pharmacology ; Protein Binding ; Receptors, Cell Surface/metabolism ; Structure-Activity Relationship
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  • 19
    Publication Date: 1991-02-08
    Description: Mutations in the cystic fibrosis transmembrane conductance regulator (CFTR) cause cystic fibrosis. In order to evaluate its function, CFTR was expressed in HeLa, Chinese hamster ovary (CHO), and NIH 3T3 fibroblast cells, and anion permeability was assessed with a fluorescence microscopic assay and the whole-cell patch-clamp technique. Adenosine 3',5'-monophosphate (cAMP) increased anion permeability and chloride currents in cells expressing CFTR, but not in cells expressing a mutant CFTR (delta F508) or in nontransfected cells. The simplest interpretation of these observations is that CFTR is itself a cAMP-activated chloride channel. The alternative interpretation, that CFTR directly or indirectly regulates chloride channels, requires that these cells have endogenous cryptic, chloride channels that are stimulated by cAMP only in the presence of CFTR.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Anderson, M P -- Rich, D P -- Gregory, R J -- Smith, A E -- Welsh, M J -- New York, N.Y. -- Science. 1991 Feb 8;251(4994):679-82.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Internal Medicine, University of Iowa College of Medicine, Iowa City 52242.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1704151" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Line ; Chloride Channels ; Chlorides/*metabolism ; Cricetinae ; Cyclic AMP/*physiology ; Cystic Fibrosis Transmembrane Conductance Regulator ; Humans ; Membrane Proteins/*metabolism/*physiology ; Mice ; Mutation ; Recombinant Proteins ; Structure-Activity Relationship
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  • 20
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1991-12-06
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hoffman, M -- New York, N.Y. -- Science. 1991 Dec 6;254(5037):1455-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1962203" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Line ; Genetic Therapy/*methods ; Growth Hormone/administration & dosage ; Mice ; Muscles/*cytology/secretion ; Recombinant Proteins/administration & dosage
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  • 21
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1991-11-22
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hoffman, M -- New York, N.Y. -- Science. 1991 Nov 22;254(5035):1111-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1720260" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Collagen/physiology ; Epidermis/*physiology ; Epidermolysis Bullosa/*physiopathology ; Humans ; Keratins/*physiology ; Mice ; Mice, Transgenic
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  • 22
    Publication Date: 1991-12-20
    Description: The goal of islet transplantation in human diabetes is to maintain the islet grafts in the recipients without the use of immunosuppression. One approach is to encapsulate the donor islets in permselective membranes. Hollow fibers fabricated from an acrylic copolymer were used to encapsulate small numbers of rat islets that were immobilized in an alginate hydrogel for transplantation in diabetic mice. The fibers were biocompatible, prevented rejection, and maintained normoglycemia when transplanted intraperitoneally; hyperglycemia returned when the fibers were removed at 60 days. Normoglycemia was also maintained by subcutaneous implants that had an appropriately constructed outer surface on the fibers.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lacy, P E -- Hegre, O D -- Gerasimidi-Vazeou, A -- Gentile, F T -- Dionne, K E -- DK01226/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1991 Dec 20;254(5039):1782-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pathology, Washington University School of Medicine, St. Louis, MO 63110.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1763328" target="_blank"〉PubMed〈/a〉
    Keywords: *Acrylic Resins ; Animals ; Animals, Newborn ; Blood Glucose/*metabolism ; Diabetes Mellitus, Experimental/blood/*surgery ; In Vitro Techniques ; Insulin/secretion ; Islets of Langerhans/*secretion ; Islets of Langerhans Transplantation/*physiology ; Male ; Membranes, Artificial ; Mice ; Mice, Inbred C57BL ; *Polyvinyl Chloride ; Rats ; Rats, Inbred WF ; Time Factors ; Transplantation, Heterologous
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  • 23
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1991-10-25
    Description: The protein tyrosine kinase activity of the cellular Src protein is negatively regulated by phosphorylation at tyrosine residue 527 (Tyr527). It has not been established whether this regulatory modification of Src is mediated by autophosphorylation or by another cellular protein kinase. The phosphorylation of a modified form of c-Src that lacks kinase activity was examined in mouse cells that do not express endogenous Src (because of the targeted disruption of both src alleles). Phosphorylation of the inactive form of Src on Tyr527 occurred to a similar extent in cells lacking endogenous Src as it did in cells expressing Src. Therefore, Tyr527 phosphorylation, and thus negative control of Src kinase activity, is mediated by another cellular protein tyrosine kinase.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Thomas, J E -- Soriano, P -- Brugge, J S -- New York, N.Y. -- Science. 1991 Oct 25;254(5031):568-71.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Microbiology, University of Pennsylvania, School of Medicine, Philadelphia 19104.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1719633" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Cells, Cultured ; Cyanogen Bromide ; Embryo, Mammalian ; Mice ; Peptide Mapping ; Phosphopeptides/isolation & purification ; Phosphorylation ; Protein-Tyrosine Kinases ; Proto-Oncogene Proteins pp60(c-src)/*metabolism ; *Tyrosine
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  • 24
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1991-10-25
    Description: Extensive data on genetic divergence among 24 inbred strains of mice provide an opportunity to examine the concordance of gene trees and species trees, especially whether structured subsamples of loci give congruent estimates of phylogenetic relationships. Phylogenetic analyses of 144 separate loci reproduce almost exactly the known genealogical relationships among these 24 strains. Partitioning these loci into structured subsets representing loci coding for proteins, the immune system and endogenous viruses give incongruent phylogenetic results. The gene tree based on protein loci provides an accurate picture of the genealogical relationships among strains; however, gene trees based upon immune and viral data show significant deviations from known genealogical affinities.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Atchley, W R -- Fitch, W M -- GM-45344/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1991 Oct 25;254(5031):554-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Genetics, North Carolina State University, Raleigh 27695.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1948030" target="_blank"〉PubMed〈/a〉
    Keywords: Algorithms ; Alleles ; Analysis of Variance ; Animals ; Genes, Immunoglobulin ; Genotype ; Mice ; Mice, Inbred Strains/*genetics ; *Phylogeny ; Probability ; Proteins/genetics
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  • 25
    Publication Date: 1991-02-15
    Description: Severe combined immunodeficient (SCID) mice reconstituted with human peripheral blood leukocytes (hu-PBL-SCID mice) have inducible human immune function and may be useful as a small animal model for acquired immunodeficiency syndrome (AIDS) research. Hu-PBL-SCID mice infected with human immunodeficiency virus-1 (HIV-1) contained virus that was recoverable by culture from the peritoneal cavity, spleen, peripheral blood, and lymph nodes for up to 16 weeks after infection; viral sequences were also detected by in situ hybridization and by amplification with the polymerase chain reaction (PCR). Mice could be infected with multiple strains of HIV-1, including LAV-1/Bru, IIIB, MN, SF2, and SF13. HIV-1 infection affected the concentration of human immunoglobulin and the number of CD4+ T cells in the mice. These results support the use of the hu-PBL-SCID mouse for studies of the pathogenesis and treatment of AIDS.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mosier, D E -- Gulizia, R J -- Baird, S M -- Wilson, D B -- Spector, D H -- Spector, S A -- AI-27703/AI/NIAID NIH HHS/ -- AI-29182/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1991 Feb 15;251(4995):791-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Immunology, Medical Biology Institute, La Jolla, CA 92037.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1990441" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Blood Transfusion ; Chimera/*immunology ; *Disease Models, Animal ; *HIV Infections/immunology ; *HIV-1/isolation & purification ; Humans ; Immunologic Deficiency Syndromes/genetics/*immunology ; Lymphocyte Transfusion ; Mice ; Mice, Mutant Strains/*immunology ; Spleen/microbiology
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  • 26
    Publication Date: 1991-11-08
    Description: Humoral immunity is important for protection against viral infection and neutralization of extracellular virus, but clearance of virus from infected tissues is thought to be mediated solely by cellular immunity. However, in a SCID mouse model of persistent alphavirus encephalomyelitis, adoptive transfer of hyperimmune serum resulted in clearance of infectious virus and viral RNA from the nervous system, whereas adoptive transfer of sensitized T lymphocytes had no effect on viral replication. Three monoclonal antibodies to two different epitopes on the E2 envelope glycoprotein mediated viral clearance. Treatment of alphavirus-infected primary cultured rat neurons with these monoclonal antibodies to E2 resulted in decreased viral protein synthesis, followed by gradual termination of mature infectious virion production. Thus, antibody can mediate clearance of alphavirus infection from neurons by restricting viral gene expression.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Levine, B -- Hardwick, J M -- Trapp, B D -- Crawford, T O -- Bollinger, R C -- Griffin, D E -- NS29234/NS/NINDS NIH HHS/ -- T32-NS-07000/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1991 Nov 8;254(5033):856-60.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine, 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/1658936" target="_blank"〉PubMed〈/a〉
    Keywords: Alphavirus/immunology/isolation & purification/*physiology ; Animals ; Antibodies, Monoclonal/*therapeutic use ; Central Nervous System/immunology/*microbiology ; Encephalomyelitis/*immunology/microbiology/therapy ; *Immunotherapy, Adoptive ; Mice ; Mice, Inbred Strains ; Mice, SCID ; Neurons/immunology/*microbiology ; RNA, Viral/isolation & purification ; T-Lymphocytes/*immunology ; Togaviridae Infections/*immunology/therapy ; Virus Replication
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  • 27
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1991-01-18
    Description: The CCAAT-enhancer binding protein (C/EBP) has now been found to promote the terminal differentiation of adipocytes. During the normal course of adipogenesis, C/EBP expression is restricted to a terminal phase wherein proliferative growth is arrested, and specialized cell phenotype is first manifested. A conditional form of C/EBP was developed, making it feasible to test its capacity to regulate the differentiation of cultured adipocytes. Premature expression of C/EBP in adipoblasts caused a direct cessation of mitotic growth. Moreover, when abetted by the effects of three adipogenic hormones, C/EBP promoted terminal cell differentiation. Since C/EBP is expressed in a variety of tissues, it may have a fundamental role in regulating the balance between cell growth and differentiation in higher animals.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Umek, R M -- Friedman, A D -- McKnight, S L -- New York, N.Y. -- Science. 1991 Jan 18;251(4991):288-92.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Research Laboratories, Department of Embryology, Carnegic Institution of Washington, Baltimore, MD 21210.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1987644" target="_blank"〉PubMed〈/a〉
    Keywords: Adipose Tissue/*cytology ; Animals ; CCAAT-Enhancer-Binding Proteins ; *Cell Differentiation ; Cell Division ; DNA-Binding Proteins/*physiology ; Gene Expression Regulation ; L Cells (Cell Line) ; Mice ; Nuclear Proteins/*physiology ; Receptors, Steroid/physiology ; Regulatory Sequences, Nucleic Acid ; Structure-Activity Relationship
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  • 28
    Publication Date: 1991-05-31
    Description: The crystal structure of a murine adenosine deaminase complexed with 6-hydroxyl-1,6-dihydropurine ribonucleoside, a nearly ideal transition-state analog, has been determined and refined at 2.4 angstrom resolution. The structure is folded as an eight-stranded parallel alpha/beta barrel with a deep pocket at the beta-barrel COOH-terminal end wherein the inhibitor and a zinc are bound and completely sequestered. The presence of the zinc cofactor and the precise structure of the bound analog were not previously known. The 6R isomer of the analog is very tightly held in place by the coordination of the 6-hydroxyl to the zinc and the formation of nine hydrogen bonds. On the basis of the structure of the complex a stereoselective addition-elimination or SN2 mechanism of the enzyme is proposed with the zinc atom and the Glu and Asp residues playing key roles. A molecular explanation of a hereditary disease caused by several point mutations of an enzyme is also presented.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wilson, D K -- Rudolph, F B -- Quiocho, F A -- CA14030/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1991 May 31;252(5010):1278-84.〈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/1925539" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Deaminase/*chemistry/deficiency/metabolism ; Amino Acid Sequence ; Animals ; Binding Sites ; Catalysis ; Crystallization ; Immunologic Deficiency Syndromes/*enzymology/genetics ; Mice ; Models, Molecular ; Molecular Structure ; Mutation ; Protein Conformation ; Purine Nucleosides/chemistry/*metabolism ; Ribonucleosides/chemistry/*metabolism ; Zinc/metabolism
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  • 29
    Publication Date: 1991-10-18
    Description: The neurotransmitter serotonin (5HT) activates a variety of second messenger signaling systems and through them indirectly regulates the function of ion channels. Serotonin also activates ion channels directly, suggesting that it may also mediate rapid, excitatory responses. A complementary DNA clone containing the coding sequence of one of these rapidly responding channels, a 5HT3 subtype of the serotonin receptor, has been isolated by screening a neuroblastoma expression library for functional expression of serotonin-gated currents in Xenopus oocytes. The predicted protein product has many of the features shared by other members of the ligand-gated ion channel family. The pharmacological and electrophysiological characteristics of the cloned receptor are largely consistent with the properties of native 5HT3 receptors. Messenger RNA encoding this receptor is found in the brain, spinal cord, and heart. This receptor defines a new class of excitatory ligand-gated channels.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Maricq, A V -- Peterson, A S -- Brake, A J -- Myers, R M -- Julius, D -- GM44298/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1991 Oct 18;254(5030):432-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, University of California, San Francisco 94143-0450.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1718042" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Binding, Competitive ; Cell Line ; Ion Channels/*chemistry/drug effects/physiology ; Mice ; Molecular Sequence Data ; Oocytes/metabolism ; Poly A ; RNA, Messenger ; Radioligand Assay ; Receptors, Serotonin/*chemistry/drug effects/physiology ; Xenopus
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  • 30
    Publication Date: 1991-04-26
    Description: The trk proto-oncogene encodes a 140-kilodalton, membrane-spanning protein tyrosine kinase (p140prototrk) that is expressed only in neural tissues. Nerve growth factor (NGF) stimulates phosphorylation of p140prototrk in neural cell lines and in embryonic dorsal root ganglia. Affinity cross-linking and equilibrium binding experiments with 125I-labeled NGF indicate that p140prototrk binds NGF specifically in cultured cells with a dissociation constant of 10(-9) molar. The identification of p140prototrk as an NGF receptor indicates that this protein participates in the primary signal transduction mechanism of NGF.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kaplan, D R -- Hempstead, B L -- Martin-Zanca, D -- Chao, M V -- Parada, L F -- N01-CO-74101/CO/NCI NIH HHS/ -- New York, N.Y. -- Science. 1991 Apr 26;252(5005):554-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Eukaryotic Signal Transduction Group, National Cancer Institute-Frederick Cancer Research and Development Center, MD 21702.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1850549" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Line ; Cell Membrane/physiology ; Cross-Linking Reagents ; Embryo, Mammalian ; Ganglia, Spinal/*metabolism ; Humans ; Kinetics ; Mice ; Nerve Growth Factors/metabolism/*physiology ; Neuroblastoma ; Protein-Tyrosine Kinases/*metabolism ; Proto-Oncogene Proteins/*metabolism ; *Proto-Oncogenes ; Receptor, trkA ; Receptors, Cell Surface/metabolism/*physiology ; Receptors, Nerve Growth Factor ; *Signal Transduction
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  • 31
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1991-01-11
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉New York, N.Y. -- Science. 1991 Jan 11;251(4990):142-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1987635" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Carcinogenicity Tests ; Cell Division ; Mathematics ; Mice ; Mitosis
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  • 32
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1991-01-18
    Description: The murine acquired immunodeficiency syndrome (MAIDS) is associated with proliferation of target cells that have been infected by a defective retrovirus. To control the growth of this primary neoplasia, virus-inoculated mice were treated with anti-neoplastic drugs. Paradoxically, cyclophosphamide, which is also immunosuppressive, was very effective in preventing the appearance and progression of the disease, in restoring a normal T cell function, and in depleting the number of infected target cells. This result suggests that the proliferating infected target cells were responsible for the immunodeficiency.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Simard, C -- Jolicoeur, P -- New York, N.Y. -- Science. 1991 Jan 18;251(4991):305-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Molecular Biology, Clinical Research Institute of Montreal, Quebec, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1987646" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antineoplastic Agents/*therapeutic use ; Blotting, Northern ; Blotting, Southern ; Cell Division ; Cyclophosphamide/therapeutic use ; Lymphocyte Activation ; Mice ; Mice, Inbred BALB C ; Murine Acquired Immunodeficiency Syndrome/*drug therapy/pathology ; RNA, Viral/analysis ; Spleen/pathology ; Virus Replication
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  • 33
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1991-06-21
    Description: Destruction of target cells by cytotoxic T lymphocytes requires the presence of HLA (human lymphocyte antigen) class I antigens on the target cells for adhesion as well as for triggering of the antigen-specific T cell receptor. Rejection of xenogeneic human pancreatic islets and liver was circumvented by masking, before transplantation, donor antigens with F(ab')2 antibody fragments to HLA class I or tissue-specific epitopes. This strategy eliminated the need for recipient immunosuppression and allowed islet xenograft survival beyond 200 days, as demonstrated functionally by C peptide secretion as well as by histology. These in vivo observations are consistent with the importance of donor HLA class I in eliciting graft rejection and have potential applicability to the successful transplantation of other HLA class I-bearing donor tissues.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Faustman, D -- Coe, C -- New York, N.Y. -- Science. 1991 Jun 21;252(5013):1700-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Diabetes Unit, Massachusetts General Hospital, Harvard Medical School, Boston 02129.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1710828" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antibodies, Monoclonal/immunology ; Antigen-Antibody Complex ; Antigens, CD/immunology ; Antigens, CD29 ; C-Peptide/blood ; *Graft Rejection ; Histocompatibility Antigens Class I/*immunology ; Humans ; Immunoglobulin Fab Fragments/immunology ; Islets of Langerhans/*immunology ; Islets of Langerhans Transplantation/*immunology ; Mice ; Mice, Inbred BALB C ; T-Lymphocytes/*immunology ; Transplantation, Heterologous
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  • 34
    Publication Date: 1991-11-01
    Description: The cerebellum has many properties that make it a useful model for investigating neural development. Purkinje cells, the major output neurons of the cerebellar cortex, have drawn special attention because of the availability of biochemical markers and mutants that affect their development. The spatial expression of L7, a protein specific for Purkinje cells, and L7 beta Gal, a gene expressed in transgenic mice that was constructed from the L7 promoter and the marker beta-galactosidase, delineated bands of Purkinje cells that increased in number during early postnatal development. Expression of the transgene in adult reeler mutant mice, which show inverted cortical lamination, and in primary culture showed that the initial expression of L7 is intrinsic to Purkinje cells and does not depend on extracellular signals. This may reflect an underlying developmental map in cerebellum.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Smeyne, R J -- Oberdick, J -- Schilling, K -- Berrebi, A S -- Mugnaini, E -- Morgan, J I -- NRSA 08-08601/NR/NINR NIH HHS/ -- NS-09904/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1991 Nov 1;254(5032):719-21.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurosciences, Roche Institute of Molecular Biology, Roche Research Center, Nutley, NJ 07110.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1948052" target="_blank"〉PubMed〈/a〉
    Keywords: Aging ; Animals ; Cerebellum/cytology/embryology/*growth & development ; Embryonic and Fetal Development ; Mice ; Mice, Neurologic Mutants ; Mice, Transgenic ; Purkinje Cells/cytology/*physiology ; Recombinant Proteins/metabolism ; beta-Galactosidase/*genetics/metabolism
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  • 35
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1991-05-10
    Description: The zinc finger DNA-binding motif occurs in many proteins that regulate eukaryotic gene expression. The crystal structure of a complex containing the three zinc fingers from Zif268 (a mouse immediate early protein) and a consensus DNA-binding site has been determined at 2.1 angstroms resolution and refined to a crystallographic R factor of 18.2 percent. In this complex, the zinc fingers bind in the major groove of B-DNA and wrap part way around the double helix. Each finger has a similar relation to the DNA and makes its primary contacts in a three-base pair subsite. Residues from the amino-terminal portion of an alpha helix contact the bases, and most of the contracts are made with the guanine-rich strand of the DNA. This structure provides a framework for understanding how zinc fingers recognize DNA and suggests that this motif may provide a useful basis for the design of novel DNA-binding proteins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pavletich, N P -- Pabo, C O -- GM-31471/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1991 May 10;252(5007):809-17.〈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/2028256" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Crystallography ; DNA/*metabolism ; DNA-Binding Proteins/*chemistry/isolation & purification/physiology ; Early Growth Response Protein 1 ; *Immediate-Early Proteins ; Mice ; Models, Molecular ; Molecular Sequence Data ; Molecular Structure ; Transcription Factors/*chemistry/isolation & purification/physiology ; Zinc Fingers/*physiology
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  • 36
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1991-09-06
    Description: Alloimmune mice (mice that have been exposed to cells from another murine strain) were shown to make antibodies against gp120 and p24 of human immunodeficiency virus (HIV), and mice of the autoimmune strains MRL-lpr/lpr and MRL-(+)/+ made antibodies against gp120. This is surprising because the mice were not exposed to HIV. Furthermore, anti-anti-MHC antibodies (molecules that have shapes similar to those of major histocompatibility complex molecules) were detected in both alloimmune sera and MRL mice. These results are discussed in the context of a possible role for allogeneic stimuli in the pathogenesis of acquired immunodeficiency syndrome, as suggested by an idiotypic network model.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kion, T A -- Hoffmann, G W -- New York, N.Y. -- Science. 1991 Sep 6;253(5024):1138-40.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology, University of British Columbia, Vancouver, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1909456" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antibodies, Monoclonal ; *Antibody Formation ; Autoimmune Diseases/genetics/*immunology/microbiology ; Enzyme-Linked Immunosorbent Assay ; Gene Products, gag/*immunology ; HIV Antibodies/*biosynthesis ; HIV Antigens/*immunology ; HIV Core Protein p24 ; HIV Envelope Protein gp120/*immunology ; Histocompatibility Antigens Class II/*immunology ; Isoantibodies/*biosynthesis ; *Major Histocompatibility Complex ; Mice ; Mice, Inbred BALB C ; Mice, Inbred CBA ; Mice, Mutant Strains ; T-Lymphocytes/immunology ; Viral Core Proteins/*immunology
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  • 37
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1991-04-19
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stamatoyannopoulos, G -- New York, N.Y. -- Science. 1991 Apr 19;252(5004):383.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine, University of Washington, Seattle 98195.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2017679" target="_blank"〉PubMed〈/a〉
    Keywords: Anemia, Sickle Cell/genetics ; Animals ; Fetus/metabolism ; *Gene Expression Regulation ; Globins/*genetics ; Humans ; Mice ; Mice, Transgenic ; Regulatory Sequences, Nucleic Acid ; Thalassemia/genetics
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  • 38
    Publication Date: 1991-11-15
    Description: Binding of ligand or antibody to certain cell-surface proteins that are anchored to the membrane by glycophosphatidylinositol (GPI) can cause activation of leukocytes. However, it is not known how these molecules, which lack intracellular domains, can transduce signals. The GPI-linked human molecules CD59, CD55, CD48, CD24, and CD14 as well as the mouse molecules Thy-1 and Ly-6 were found to associate with protein tyrosine kinases, key regulators of cell activation and signal transduction. A protein tyrosine kinase associated with the GPI-linked proteins CD59, CD55, and CD48 in human T cells, and with Thy-1 in mouse T cells was identified as p56lck, a protein tyrosine kinase related to Src. This interaction of GPI-linked molecules with protein tyrosine kinases suggests a potential mechanism of signal transduction in cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stefanova, I -- Horejsi, V -- Ansotegui, I J -- Knapp, W -- Stockinger, H -- New York, N.Y. -- Science. 1991 Nov 15;254(5034):1016-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Immunology-Vienna International Research Cooperation Center, University of Vienna, Austria.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1719635" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens, CD/*physiology ; Antigens, Differentiation/physiology ; Cell Adhesion Molecules/physiology ; Glycolipids/physiology ; Glycosylphosphatidylinositols ; Humans ; Membrane Glycoproteins/physiology ; Membrane Proteins/*physiology ; Mice ; Phosphatidylinositols/physiology ; Phosphorylation ; Phosphotyrosine ; Protein-Tyrosine Kinases/*physiology ; Receptor Aggregation ; Receptors, Cell Surface/*physiology ; Signal Transduction ; Tyrosine/analogs & derivatives/metabolism
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  • 39
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1991-10-04
    Description: The CD19-CR2 complex of B lymphocytes contains proteins that participate in two host-defense systems, the immune and complement systems. The ligand for the subunit of the immune system, CD19, is not known, but the complement receptor subunit, CR2 (CD21), binds activation fragments of the C3 component of the complement system and may mediate immunopotentiating effects of complement. A recombinant, soluble CR2 was prepared by fusing the C3-binding region of the receptor to immunoglobulin G1 (IgG1). The (CR2)2-IgG1 chimera competed with cellular CR2 for C3 binding and suppressed the antibody response to a T cell-dependent antigen when administered to mice at the time of immunization. This inhibitory effect of (CR2)2-IgG1 demonstrates the B cell-activating function of the CD19-CR2 complex and suggests a new method for humoral immunosuppression.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hebell, T -- Ahearn, J M -- Fearon, D T -- AI-22833/AI/NIAID NIH HHS/ -- AI-28191/AI/NIAID NIH HHS/ -- GM-43803/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1991 Oct 4;254(5028):102-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine, 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/1718035" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; *Antibody Formation ; Antigens, CD/*physiology ; Antigens, CD19 ; Antigens, Differentiation, B-Lymphocyte/chemistry/*physiology ; B-Lymphocytes/*physiology ; Base Sequence ; Binding, Competitive ; Cloning, Molecular ; Immunosuppression ; In Vitro Techniques ; Mice ; Mice, Inbred BALB C ; Mice, Inbred C3H ; Molecular Sequence Data ; Receptors, Complement/chemistry/*physiology ; Receptors, Complement 3d ; Recombinant Fusion Proteins ; Signal Transduction ; Solubility
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  • 40
    Publication Date: 1991-12-20
    Description: Dimerization among transcription factors has become a recurrent theme in the regulation of eukaryotic gene expression. Hepatocyte nuclear factor-1 alpha (HNF-1 alpha) is a homeodomain-containing protein that functions as a dimer. A dimerization cofactor of HNF-1 alpha (DCoH) was identified that displayed a restricted tissue distribution and did not bind to DNA, but, rather, selectively stabilized HNF-1 alpha dimers. The formation of a stable tetrameric DCoH-HNF-1 alpha complex, which required the dimerization domain of HNF-1 alpha, did not change the DNA binding characteristics of HNF-1 alpha, but enhanced its transcriptional activity. However, DCoH did not confer transcriptional activation to the GAL4 DNA binding domain. These results indicate that DCoH regulates formation of transcriptionally active tetrameric complexes and may contribute to the developmental specificity of the complex.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mendel, D B -- Khavari, P A -- Conley, P B -- Graves, M K -- Hansen, L P -- Admon, A -- Crabtree, G R -- CA 09302/CA/NCI NIH HHS/ -- HD 07201/HD/NICHD NIH HHS/ -- HL 33942/HL/NHLBI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1991 Dec 20;254(5039):1762-7.〈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/1763325" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Cell Nucleus/physiology ; Chromosome Deletion ; DNA-Binding Proteins/*metabolism ; Gene Library ; Hepatocyte Nuclear Factor 1 ; Hepatocyte Nuclear Factor 1-alpha ; Hepatocyte Nuclear Factor 1-beta ; Humans ; *Hydro-Lyases ; Liver/physiology ; Macromolecular Substances ; Mice ; Molecular Sequence Data ; *Nuclear Proteins ; Protein Biosynthesis ; RNA, Messenger/genetics ; Rabbits ; Rats ; Reticulocytes/metabolism ; Transcription Factors/genetics/*metabolism ; Transcription, Genetic
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  • 41
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1991-10-25
    Description: The production and functional activity of two important white blood cells, the granulocytes and macrophages, are regulated mainly by a group of glycoprotein colony-stimulating factors. The colony-stimulating factors have been mass-produced with recombinant technology and are now proving of value in preventing or suppressing infections in a variety of individuals with subnormal or defective formation of blood cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Metcalf, D -- New York, N.Y. -- Science. 1991 Oct 25;254(5031):529-33.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Walter and Eliza Hall Institute of Medical Research, Post Office Royal Melbourne Hospital, Victoria, Australia.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1948028" target="_blank"〉PubMed〈/a〉
    Keywords: Acquired Immunodeficiency Syndrome/therapy ; Anemia, Aplastic/therapy ; Animals ; Colony-Stimulating Factors/genetics/*physiology/therapeutic use ; Granulocytes/cytology/*physiology ; Hematopoiesis ; Hematopoietic Stem Cells/cytology/*physiology ; Humans ; Macrophages/cytology/*physiology ; Mice ; Neoplasms/therapy ; Neutropenia/therapy ; Recombinant Proteins/therapeutic use
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  • 42
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1991-10-25
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hillis, D M -- Bull, J J -- New York, N.Y. -- Science. 1991 Oct 25;254(5031):528.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Zoology, University of Texas, Austin 78712.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1948027" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Genes ; *Genome ; Mice ; Mice, Inbred Strains/*genetics ; *Phylogeny ; Polymorphism, Genetic
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  • 43
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1991-10-04
    Description: The 17-amino acid peptide from chicken ovalbumin, Ova(323-339), was labeled at the amino terminus with fluorescein [FOva(323-339)] and near the carboxyl terminus with Texas Red [AcOva(323-338)KTR]. Fluorescence spectroscopy was carried out on resolved electrophoretic bands on nonreducing polyacrylamide gels derived from incubation mixtures containing major histocompatibility complex (MHC) class II molecules IAd and the FOva(323-339)- and AcOva(323-338)KTR-labeled peptides. Energy transfer between fluorescein and Texas Red was observed in the "floppy" alpha beta heterodimer band, but not in the "compact" alpha beta heterodimer band. Energy transfer was detected between the truncated peptides FOva(323-328)CONH2 and AcOva(331-338)KTR in both the compact alpha beta and floppy alpha beta gel bands. The energy-transfer data suggest that the two binding sites of floppy alpha beta arise from splitting apart a putative large, single binding site region in compact alpha beta.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tampe, R -- Clark, B R -- McConnell, H M -- 2R37 AI 13587-16/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1991 Oct 4;254(5028):87-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Stauffer Laboratory for Physical Chemistry, Stanford University, CA 94305.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1656526" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Binding Sites ; Energy Transfer ; Histocompatibility Antigens Class II/chemistry/*metabolism ; In Vitro Techniques ; Mice ; Molecular Sequence Data ; Ovalbumin/chemistry ; Peptides/chemistry/*metabolism ; Spectrometry, Fluorescence ; Structure-Activity Relationship
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  • 44
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1991-11-01
    Description: Interleukin-4 (IL-4) promotes the growth and differentiation of many hematopoietic cells in vitro; in particular, it directs the immunoglobulin (Ig) class switch to IgG1 and IgE. Mice homozygous for a mutation that inactivates the IL-4 gene were generated to test the requirement for IL-4 in vivo. In the mutant mice T and B cell development was normal, but the serum levels of IgG1 and IgE were strongly reduced. The IgG1 dominance in a T cell-dependent immune response was lost, and IgE was not detectable upon nematode infection. Thus, some but not all of the in vitro properties of IL-4 are critical for the physiology of the immune system in vivo.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kuhn, R -- Rajewsky, K -- Muller, W -- New York, N.Y. -- Science. 1991 Nov 1;254(5032):707-10.〈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/1948049" target="_blank"〉PubMed〈/a〉
    Keywords: Aging ; Alleles ; Animals ; B-Lymphocytes/immunology ; Blotting, Southern ; Chromosome Deletion ; Concanavalin A ; DNA/genetics/isolation & purification ; Female ; Interleukin-4/deficiency/*genetics ; Lymph Nodes/growth & development/immunology ; Lymphocyte Activation ; Male ; Mice ; Mice, Inbred C57BL ; Mice, Mutant Strains ; Restriction Mapping ; Spleen/growth & development/immunology ; T-Lymphocytes/immunology ; Thymus Gland/growth & development/immunology
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  • 45
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1991-08-09
    Description: The neurological mutant mouse strain E1 is a model for complex partial seizures in humans. The inheritance of epileptic seizures with seven conventional chromosomal markers and over 60 endogenous proviral markers was studied by means of back-crosses of E1 with two seizure-resistant strains, DBA/2J and ABP/LeJ. The major gene responsible for this epileptic phenotype (El-1) was localized to a region distal with respect to the centromere on chromosome 9. At least one other gene, El-2, linked to proviral markers on chromosome 2, also influences the seizure phenotype. In addition, a potential modifier of seizures was detected in the DBA/2J background. The location of El-1 on distal chromosome 9 may allow identification of an epilepsy candidate gene in humans on the basis of conserved synteny with human chromosome 3.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rise, M L -- Frankel, W N -- Coffin, J M -- Seyfried, T N -- NS 23355/NS/NINDS NIH HHS/ -- R35CA44385/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1991 Aug 9;253(5020):669-73.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, Boston College, Chestnut Hill 02167.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1871601" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Chromosome Mapping ; Crosses, Genetic ; Epilepsy/*genetics ; Female ; Genetic Predisposition to Disease ; Male ; Mice ; Mice, Inbred Strains ; Mice, Neurologic Mutants/*genetics ; Recombination, Genetic ; Seizures/genetics ; Software
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  • 46
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1991-03-08
    Description: T lymphocytes undergo selection events not only in the thymus, but also after they leave the thymus and reside in the periphery. Peripheral selection was found to be dependent on T cell receptor (TCR)-ligand interactions but to differ from thymic selection with regard to specificity and mechanism. Unlike thymic selection, peripheral selection required binding of antigen to the TCR, and it induced expansion of T cell clones. Tolerance to self antigens that are restricted to the periphery occurred through the elimination of self-reactive T cells and by the clonal anergy, which was associated with down-regulation of the alpha beta TCR and CD8.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rocha, B -- von Boehmer, H -- New York, N.Y. -- Science. 1991 Mar 8;251(4998):1225-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Unite INSERM U-25 CNRS UA-122, Hopital Necker, Paris, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1900951" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens, CD4/immunology ; Antigens, CD8 ; Antigens, Differentiation, T-Lymphocyte/immunology ; Cells, Cultured ; Down-Regulation ; Female ; Histocompatibility Antigens Class I/immunology ; Immunotherapy, Adoptive ; Male ; Mice ; Mice, Nude ; Receptors, Antigen, T-Cell/*physiology ; T-Lymphocytes/*immunology ; Thymectomy ; Thymus Gland/*immunology
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  • 47
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1991-10-04
    Description: Transcription factor E3 (mTFE3) is a murine transcription activator that binds to the intronic enhancer of the immunoglobulin heavy chain gene. A naturally occurring splice product of mTFE3 messenger RNA (mRNA) lacked 105 nucleotides that encode an activation domain; both absolute and relative amounts of long and truncated mRNAs varied in different tissues. Cells were cotransfected with complementary DNAs that encoded the two mRNA forms in amounts that corresponded to the amounts of each mRNA found in different cells. Small changes in substoichiometric amounts of the truncated form of mRNA effected trans-dominant negative modulation of mTFE3 activity. These findings identify a function for differential splicing in the regulation of transcription factor activity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Roman, C -- Cohn, L -- Calame, K -- R01CA38571/CA/NCI NIH HHS/ -- R01GM28361/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1991 Oct 4;254(5028):94-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Chemistry, University of California, Los Angeles 90024.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1840705" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Basic Helix-Loop-Helix Leucine Zipper Transcription Factors ; DNA-Binding Proteins/*genetics ; *Gene Expression Regulation ; Mice ; Molecular Sequence Data ; RNA Splicing ; RNA, Messenger/genetics ; Regulatory Sequences, Nucleic Acid ; Structure-Activity Relationship ; Transcription Factors/*genetics ; *Transcription, Genetic
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  • 48
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1991-07-12
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rosner, M H -- Vigano, M A -- Rigby, P W -- Arnheiter, H -- Staudt, L M -- New York, N.Y. -- Science. 1991 Jul 12;253(5016):144-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Metabolism Branch, 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/1853199" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; DNA Replication ; DNA-Binding Proteins/*physiology ; Embryo, Mammalian/*physiology ; Gene Expression Regulation ; Mice ; Octamer Transcription Factor-3 ; Stem Cells/physiology ; Teratoma/genetics/pathology ; Transcription Factors/*physiology
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  • 49
    Publication Date: 1991-07-12
    Description: The role of major histocompatibility complex (MHC) class I expression in natural killer (NK) cell target recognition is controversial. Normal T cell blasts from MHC class I-deficient mutant mice were found to serve as target cells for NK cells in vitro, which suggests that MHC class I molecules are directly involved in NK cell recognition. Spleen cells from the mutant mice were deficient in their ability to lyse MHC class I-deficient target cells or NK-susceptible tumor targets, and mutant mice could not reject allogeneic bone marrow. Thus, class I molecules may participate in the positive selection or tolerance induction of NK cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Liao, N S -- Bix, M -- Zijlstra, M -- Jaenisch, R -- Raulet, D -- R01 AI30171/AI/NIAID NIH HHS/ -- R35 CA44339/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1991 Jul 12;253(5016):199-202.〈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/1853205" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cytotoxicity, Immunologic ; Histocompatibility Antigens Class I/*immunology ; *Immunity, Cellular ; *Immunity, Innate ; Killer Cells, Natural/*immunology ; Major Histocompatibility Complex ; Mice ; Mice, Inbred Strains ; T-Lymphocyte Subsets/immunology ; T-Lymphocytes, Cytotoxic/immunology ; beta 2-Microglobulin/physiology
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  • 50
    Publication Date: 1991-05-10
    Description: A mutated form of the platelet-derived growth factor (PDGF) beta receptor lacking most of its cytoplasmic domain was tested for its ability to block wild-type PDGF receptor function. PDGF induced the formation of complexes consisting of wild-type and truncated receptors. Such complexes were defective in autophosphorylation. When truncated receptors were expressed in excess compared to wild-type receptors, stimulation by PDGF of receptor autophosphorylation, association of phosphatidylinositol-3 kinase with the receptor, and calcium mobilization were blocked. Thus, a truncated receptor can inactivate wild-type receptor function by forming ligand-dependent receptor complexes (probably heterodimers) that are incapable of mediating the early steps of signal transduction.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ueno, H -- Colbert, H -- Escobedo, J A -- Williams, L T -- P01 HL-43821/HL/NHLBI NIH HHS/ -- R01 HL-32898/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1991 May 10;252(5007):844-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine, University of California, San Francisco 94143.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1851331" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cells, Cultured ; Centrifugation, Density Gradient ; Cricetinae ; In Vitro Techniques ; Ligands ; Mice ; Mice, Inbred BALB C ; Phosphorylation ; Platelet-Derived Growth Factor ; Receptors, Cell Surface/*antagonists & inhibitors/physiology ; Receptors, Platelet-Derived Growth Factor ; Signal Transduction/*physiology
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  • 51
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1991-03-08
    Description: Increasing the content of the actin-binding protein gelsolin in cultured mouse fibroblasts by up to 125 percent by gene transfection proportionally enhanced the rate at which the cells migrated through porous filters toward a gradient of serum and closed a wound made on a confluent monolayer of cells in a tissue culture dish. These results provide direct evidence that gelsolin, which promotes both actin assembly and disassembly in vitro, is an important element in fibroblast locomotion and demonstrate that the manipulation of intracellular machinery can increase cell motility.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cunningham, C C -- Stossel, T P -- Kwiatkowski, D J -- AI28465/AI/NIAID NIH HHS/ -- HL07680/HL/NHLBI NIH HHS/ -- HL19429/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1991 Mar 8;251(4998):1233-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Hematology-Oncology Unit, Massachusetts General Hospital, Boston 02129.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1848726" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Calcium-Binding Proteins/genetics/*physiology ; Cell Line ; *Chemotaxis ; Fibroblasts/physiology ; Gelsolin ; Gene Expression ; Humans ; Kinetics ; Mice ; Microfilament Proteins/genetics/*physiology ; RNA Splicing ; RNA, Messenger/genetics ; Transfection
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  • 52
    Publication Date: 1991-09-20
    Description: The maturation of T cells in the thymus is dependent on the expression of major histocompatibility complex (MHC) molecules. By disruption of the MHC class II Ab beta gene in embryonic stem cells, mice were generated that lack cell surface expression of class II molecules. These MHC class II-deficient mice were depleted of mature CD4+ T cells and were deficient in cell-mediated immune responses. These results provide genetic evidence that class II molecules are required for the maturation and function of mature CD4+ T cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Grusby, M J -- Johnson, R S -- Papaioannou, V E -- Glimcher, L H -- AI21569/AI/NIAID NIH HHS/ -- HD27295/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 1991 Sep 20;253(5026):1417-20.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cancer Biology, Harvard School of Public Health, Boston, MA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1910207" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens, CD4/*immunology ; Crosses, Genetic ; Embryo, Mammalian ; Enzyme-Linked Immunosorbent Assay ; Female ; *Genes, MHC Class II ; Immunity, Cellular/genetics ; Immunoglobulin G/analysis/classification ; Immunoglobulin M/analysis ; Immunologic Deficiency Syndromes/*genetics ; *Lymphocyte Depletion ; Male ; Mice ; Mice, Inbred C57BL ; Mice, Transgenic ; Stem Cells/immunology ; T-Lymphocyte Subsets/*immunology
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  • 53
    Publication Date: 1991-08-30
    Description: Human T cell leukemia virus type-I (HTLV-I) is the etiologic agent of adult T cell leukemia and has also been suggested to be involved in other diseases such as chronic arthritis or myelopathy. To elucidate pathological roles of the virus in disease, transgenic mice were produced that carry the HTLV-I genome. At 2 to 3 months of age, many of the mice developed chronic arthritis resembling rheumatoid arthritis. Synovial and periarticular inflammation with articular erosion caused by invasion of granulation tissues were marked. These observations suggest a possibility that HTLV-I is one of the etiologic agents of chronic arthritis in humans.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Iwakura, Y -- Tosu, M -- Yoshida, E -- Takiguchi, M -- Sato, K -- Kitajima, I -- Nishioka, K -- Yamamoto, K -- Takeda, T -- Hatanaka, M -- New York, N.Y. -- Science. 1991 Aug 30;253(5023):1026-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Medical Science, University of Tokyo, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1887217" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Arthritis, Rheumatoid/*genetics/pathology/physiopathology ; Genes, Viral ; Human T-lymphotropic virus 1/*genetics ; Inflammation ; Joints/pathology ; Mice ; Mice, Inbred Strains ; Mice, Transgenic ; RNA, Messenger/genetics ; Repetitive Sequences, Nucleic Acid ; Viral Envelope Proteins/genetics
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  • 54
    Publication Date: 1991-10-11
    Description: Wilms tumor has been associated with genomic alterations at both the 11p13 and 11p15 regions. To differentiate between the involvement of these two loci, a chromosome 11 was constructed that had one or the other region deleted, and this chromosome was introduced into the tumorigenic Wilms tumor cell line G401. When assayed for tumor-forming activity in nude mice, the 11p13-deleted, but not the 11p15.5-p14.1-deleted chromosome, retained its ability to suppress tumor formation. These results provide in vivo functional evidence for the existence of a second genetic locus (WT2) involved in suppressing the tumorigenic phenotype of Wilms tumor.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dowdy, S F -- Fasching, C L -- Araujo, D -- Lai, K M -- Livanos, E -- Weissman, B E -- Stanbridge, E J -- CA19104/CA/NCI NIH HHS/ -- CA44470/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1991 Oct 11;254(5029):293-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology and Molecular Genetics, University of California, Irvine 92717.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1656527" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Line ; Chromosome Mapping ; *Chromosomes, Human, Pair 11 ; Genes, Tumor Suppressor/*genetics ; *Genes, Wilms Tumor/genetics ; Humans ; Karyotyping ; Kidney Neoplasms/*genetics ; Mice ; Mice, Nude ; Wilms Tumor/*genetics
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  • 55
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1991-05-10
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Williams, A F -- New York, N.Y. -- Science. 1991 May 10;252(5007):764.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1851327" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens, CD45 ; Antigens, Differentiation ; Cell Membrane/*enzymology ; Histocompatibility Antigens ; Mice ; *Phosphoprotein Phosphatases ; Protein Tyrosine Phosphatases ; Rats
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  • 56
    Publication Date: 1991-12-20
    Description: Transient activation of the interleukin-2 (IL-2) gene after antigen recognition by T lymphocytes is crucial for subsequent T cell proliferation and differentiation. Several IL-2 gene regulatory elements and binding factors necessary for activation of the IL-2 gene have been defined. However, little is known about negative regulation of IL-2 expression, which is likely to be important in the rapid shut-off of IL-2 transcription. A nucleotide sequence element (NRE-A) that negatively regulates IL-2 expression has been identified within the IL-2 gene. T cell nuclear extracts contained an NRE-A binding activity. A complementary DNA was isolated that encodes a zinc finger-containing protein that suppressed IL-2 gene expression. The observation of negative regulation of the immunoglobulin heavy chain gene enhancer by an element similar to NRE-A suggests that related proteins may regulate multiple immune response genes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Williams, T M -- Moolten, D -- Burlein, J -- Romano, J -- Bhaerman, R -- Godillot, A -- Mellon, M -- Rauscher, F J 3rd -- Kant, J A -- AI23879/AI/NIAID NIH HHS/ -- CA23413/CA/NCI NIH HHS/ -- CA54428/CA/NCI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1991 Dec 20;254(5039):1791-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pathology, School of Medicine, University of New Mexico, Albuquerque 87131.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1840704" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Cell Line ; DNA Probes ; *Enhancer Elements, Genetic ; *Gene Expression Regulation ; *Genes, Immunoglobulin ; Humans ; Immunoglobulin Heavy Chains/*genetics ; Interleukin-2/*genetics ; Mice ; Molecular Sequence Data ; Oligodeoxyribonucleotides ; Regulatory Sequences, Nucleic Acid ; Restriction Mapping ; T-Lymphocytes/*immunology ; *Transcription, Genetic ; Zinc Fingers/*genetics/physiology
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  • 57
    Publication Date: 1991-06-28
    Description: CD45 is a member of a family of membrane proteins that possess phosphotyrosine phosphatase activity, and is the source of much of the tyrosine phosphatase activity in lymphocytes. In view of its enzymatic activity and high copy number, it seems likely that CD45 functions in transmembrane signal transduction by lymphocyte receptors that are coupled to activation of tyrosine kinases. The B cell antigen receptor was found to transduce a Ca(2+)-mobilizing signal only if cells expressed CD45. Also, both membrane immunoglobulin M (mIgM) and CD45 were lost from the surface of cells treated with antibody to CD45, suggesting a physical interaction between these proteins. Finally, CD45 dephosphorylated a complex of mIg-associated proteins that appears to function in signal transduction by the antigen receptor. These data indicate that CD45 occurs as a component of a complex of proteins associated with the antigen receptor, and that CD45 may regulate signal transduction by modulating the phosphorylation state of the antigen receptor subunits.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Justement, L B -- Campbell, K S -- Chien, N C -- Cambier, J C -- AI20519/AI/NIAID NIH HHS/ -- AI21768/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1991 Jun 28;252(5014):1839-42.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pediatrics, National Jewish Center for Immunology and Respiratory Medicine, Denver, CO.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1648262" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens, CD45 ; Antigens, Differentiation/genetics/*physiology ; B-Lymphocytes/*immunology ; Calcium/physiology ; Cell Line ; Cell Membrane/physiology ; Cells, Cultured ; Clone Cells ; Histocompatibility Antigens/genetics/*physiology ; Immunoglobulin M/physiology ; Membrane Glycoproteins/*physiology ; Mice ; Phosphoprotein Phosphatases/metabolism ; Phosphorylation ; Plasmacytoma ; Protein Tyrosine Phosphatases ; RNA, Messenger/genetics ; Receptors, Antigen, B-Cell/*physiology ; *Signal Transduction ; Spleen/immunology ; Transfection
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  • 58
    Publication Date: 1991-06-28
    Description: Trypanosoma brucei, the protozoan parasite responsible for African sleeping sickness, evades the host immune response through the process of antigenic variation. The variant antigen, known as the variant surface glycoprotein (VSG), is anchored to the cell surface by a glycosyl phosphatidylinositol (GPI) structure that contains myristate (n-tetradecanoate) as its only fatty acid component. The utilization of heteroatom-containing analogs of myristate was studied both in a cell-free system and in vivo. Results indicated that the specificity of fatty acid incorporation depends on chain length rather than on hydrophobicity. One analog, 10-(propoxy)decanoic acid, was highly toxic to trypanosomes in culture although it is nontoxic to mammalian cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Doering, T L -- Raper, J -- Buxbaum, L U -- Adams, S P -- Gordon, J I -- Hart, G W -- Englund, P T -- 5T32GM07309/GM/NIGMS NIH HHS/ -- AI21334/AI/NIAID NIH HHS/ -- AI27179/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1991 Jun 28;252(5014):1851-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Chemistry, Johns Hopkins Medical School, Baltimore, MD 21210.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1829548" target="_blank"〉PubMed〈/a〉
    Keywords: Acyl Coenzyme A/metabolism ; Animals ; Cell-Free System ; Glycolipids/metabolism ; Glycosylphosphatidylinositols ; Kinetics ; Mice ; Myristic Acid ; Myristic Acids/*metabolism/*pharmacology ; Phosphatidylinositols/metabolism ; Structure-Activity Relationship ; Trypanosoma brucei brucei/*drug effects/metabolism/ultrastructure
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  • 59
    Publication Date: 1991-05-31
    Description: Many candidate antigens of malaria vaccines have limited immunological recognition. One exception is Pfs25, a cysteine-rich, 25-kilodalton sexual stage surface protein of Plasmodium falciparum. Pfs25 is a target of monoclonal antibodies that block transmission of malaria from vertebrate host to mosquito vector. The surface of mammalian cells infected with a recombinant vaccinia virus that expressed Pfs25 specifically bound transmission-blocking monoclonal antibodies. Furthermore, major histocompatibility complex-disparate congenic mouse strains immunized with recombinant Pfs25 elicited transmission-blocking antibodies, demonstrating that the capacity to develop transmission-blocking antibodies is not genetically restricted in mice. Live recombinant viruses may provide an inexpensive, easily administered alternative to subunit vaccines prepared from purified recombinant proteins to block transmission of malaria in developing countries.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kaslow, D C -- Isaacs, S N -- Quakyi, I A -- Gwadz, R W -- Moss, B -- Keister, D B -- New York, N.Y. -- Science. 1991 May 31;252(5010):1310-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Malaria Section, 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/1925544" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antibodies, Monoclonal/analysis/immunology ; Antibodies, Protozoan/*immunology ; Antigens, Protozoan ; Immunization ; Malaria, Falciparum/*prevention & control ; Mice ; Plasmodium falciparum/*immunology ; Protozoan Proteins/genetics/*immunology ; Recombinant Proteins/immunology ; Transfection ; Vaccinia virus/genetics/*immunology
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  • 60
    Publication Date: 1991-01-11
    Description: Antigen is thought to cross-link membrane-bound immunoglobulins (Igs) of B cells, causing proliferation and differentiation or the inhibition of growth. Protein tyrosine kinases are probably involved in signal transduction for cell proliferation and differentiation. The Src-like protein tyrosine kinase Lyn is expressed preferentially in B cells. The Lyn protein and its kinase activity could be coimmunoprecipitated with IgM from detergent lysates. Cross-linking of membrane-bound IgM induced a rapid increase in tyrosine phosphorylation of at least ten distinct proteins of B cells. Thus, Lyn is physically associated with membrane-bound IgM, and is suggested to participate in antigen-mediated signal transduction.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yamanashi, Y -- Kakiuchi, T -- Mizuguchi, J -- Yamamoto, T -- Toyoshima, K -- New York, N.Y. -- Science. 1991 Jan 11;251(4990):192-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Oncology, University of Tokyo, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1702903" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; B-Lymphocytes/immunology ; Cell Line ; Detergents ; Electrophoresis, Polyacrylamide Gel ; Immunoblotting ; Immunoglobulin M/metabolism ; Immunosorbent Techniques ; Mice ; Molecular Weight ; Phosphoproteins/metabolism ; Phosphorylation ; Phosphotyrosine ; Protein-Tyrosine Kinases/genetics/*metabolism ; Receptors, Antigen, B-Cell/*metabolism ; Signal Transduction ; Tyrosine/analogs & derivatives/metabolism ; *src-Family Kinases
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  • 61
    Publication Date: 1991-05-31
    Description: In the presence of antigen presenting cells, a murine T helper (Th) cell specific for murine hemoglobin (Hb) responded to its immunogenic peptide by both cytokine (interleukin-4) secretion and proliferation. An altered Hb peptide with a single amino acid substitution induced only cytokine secretion and did not induce proliferation. Interleukin-1 costimulated and restored the Th proliferative response to normal levels. The altered peptide also supported cognate T cell-B cell interactions indicative of T cell helper function. Thus, this result suggests that the T cell receptor has the capacity of differential signaling.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Evavold, B D -- Allen, P M -- AI24157/AI/NIAID NIH HHS/ -- ESO7066/ES/NIEHS NIH HHS/ -- New York, N.Y. -- Science. 1991 May 31;252(5010):1308-10.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pathology, Washington University School of Medicine, St. Louis, MO 63110.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1833816" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Cell Division ; Clone Cells ; Hemoglobins/chemistry/*immunology ; Interleukin-4/*biosynthesis ; Lymphocyte Activation/*immunology ; Mice ; Molecular Sequence Data ; Peptide Fragments/chemistry/*immunology ; Receptors, Antigen, T-Cell/immunology/*metabolism ; Signal Transduction ; T-Lymphocytes, Helper-Inducer/cytology/*immunology
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  • 62
    Publication Date: 1991-02-08
    Description: The mos proto-oncogene product, pp39mos, is a protein kinase and has been equated with cytostatic factor (CSF), an activity in unfertilized eggs that is thought to be responsible for the arrest of meiosis at metaphase II. The biochemical properties and potential substrates of pp39mos were examined in unfertilized eggs and in transformed cells in order to study how the protein functions both as CSF and in transformation. The pp39mos protein associated with polymers under conditions that favor tubulin oligomerization and was present in an approximately 500-kilodalton "core" complex under conditions that favor depolymerization. beta-Tubulin was preferentially coprecipitated in pp39mos immunoprecipitates and was the major phosphorylated product in a pp39mos-dependent immune complex kinase assay. Immunofluorescence analysis of NIH 3T3 cells transformed with Xenopus c-mos showed that pp39mos colocalizes with tubulin in the spindle during metaphase and in the midbody and asters during telophase. Disruption of microtubules with nocodazole affected tubulin and pp39mos organization in the same way. It therefore appears that pp39mos is a tubulin-associated protein kinase and may thus participate in the modification of microtubules and contribute to the formation of the spindle. This activity expressed during interphase in somatic cells may be responsible for the transforming activity of pp39mos.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zhou, R P -- Oskarsson, M -- Paules, R S -- Schulz, N -- Cleveland, D -- Vande Woude, G F -- N01-CO-74101/CO/NCI NIH HHS/ -- New York, N.Y. -- Science. 1991 Feb 8;251(4994):671-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉ABL-Basic Research Program, NCI-Frederick Cancer Research and Development Center, MD 21702.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1825142" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antibodies, Monoclonal ; Cell Line ; Cell Transformation, Neoplastic/metabolism ; Macromolecular Substances ; Mice ; Mice, Inbred BALB C ; Molecular Sequence Data ; Phosphoproteins/metabolism ; Precipitin Tests ; Protein Binding ; Protein-Tyrosine Kinases/*metabolism ; Proto-Oncogene Proteins/*metabolism ; Proto-Oncogene Proteins c-mos ; Tubulin/*metabolism
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 63
    Publication Date: 1991-03-15
    Description: Deficiency of adenosine deaminase (ADA) results in severe combined immunodeficiency (SCID), a candidate genetic disorder for somatic cell gene therapy. Peripheral blood lymphocytes from patients affected by ADA- SCID were transduced with a retroviral vector for human ADA and injected into immunodeficient mice. Long-term survival of vector-transduced human cells was demonstrated in recipient animals. Expression of vector-derived ADA restored immune functions, as indicated by the presence in reconstituted animals of human immunoglobulin and antigen-specific T cells. Retroviral vector gene transfer, therefore, is necessary and sufficient for development of specific immune functions in vivo and has therapeutic potential to correct this lethal immunodeficiency.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ferrari, G -- Rossini, S -- Giavazzi, R -- Maggioni, D -- Nobili, N -- Soldati, M -- Ungers, G -- Mavilio, F -- Gilboa, E -- Bordignon, C -- New York, N.Y. -- Science. 1991 Mar 15;251(4999):1363-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Hematology, Istituto Scientifico H.S. Raffaele, Milano, Italy.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1848369" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Deaminase/*deficiency/genetics ; Animals ; Base Sequence ; Genetic Therapy ; Genetic Vectors ; Humans ; Immunologic Deficiency Syndromes/*genetics/therapy ; Kanamycin Kinase ; Lymphocyte Transfusion ; Lymphocytes/physiology ; Mice ; Mice, Mutant Strains ; Oligonucleotides/chemistry ; Phosphotransferases/genetics ; Polymerase Chain Reaction ; Retroviridae/genetics
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  • 64
    Publication Date: 1991-05-10
    Description: Malignant gliomas are the most common malignant brain tumors and are almost always fatal. A thymidine kinase-negative mutant of herpes simplex virus-1 (dlsptk) that is attenuated for neurovirulence was tested as a possible treatment for gliomas. In cell culture, dlsptk killed two long-term human glioma lines and three short-term human glioma cell populations. In nude mice with implanted subcutaneous and subrenal U87 human gliomas, intraneoplastic inoculation of dlsptk caused growth inhibition. In nude mice with intracranial U87 gliomas, intraneoplastic inoculation of dlsptk prolonged survival. Genetically engineered viruses such as dlsptk merit further evaluation as novel antineoplastic agents.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Martuza, R L -- Malick, A -- Markert, J M -- Ruffner, K L -- Coen, D M -- NS24279/NS/NINDS NIH HHS/ -- R01-AI26126/AI/NIAID NIH HHS/ -- SO7RRO5381/RR/NCRR NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1991 May 10;252(5007):854-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Molecular Neurogenetics Laboratory, Harvard Medical School, Massachusetts General Hospital-East, Charlestown 02129.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1851332" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antiviral Agents/pharmacology ; Brain Neoplasms/*therapy ; Cells, Cultured ; Dose-Response Relationship, Drug ; Foscarnet ; Glioma/*therapy ; Mice ; Mice, Nude ; Mutagenesis ; Phosphonoacetic Acid/analogs & derivatives/pharmacology ; Simplexvirus/genetics/*immunology ; Thymidine Kinase/genetics ; Vidarabine/pharmacology ; Viral Vaccines/*therapeutic use
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  • 65
    Publication Date: 1991-03-08
    Description: Self-tolerance to a transgene-encoded protein, hen egg lysozyme, was examined in the T and B cell repertoires of a series of lines of transgenic mice that expressed different serum concentrations of soluble lysozyme. T cells were tolerant in all lines in which lysozyme was expressed irrespective of the antigen concentration, whereas B cell tolerance did not occur when the serum lysozyme concentration was less than 1.5 nanograms per milliliter (0.1 nM). Induction of elevated transgene expression could restore B cell tolerance. These findings support the hypothesis that autoimmune disease may in some instances arise through a bypass of T cell tolerance.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Adelstein, S -- Pritchard-Briscoe, H -- Anderson, T A -- Crosbie, J -- Gammon, G -- Loblay, R H -- Basten, A -- Goodnow, C C -- New York, N.Y. -- Science. 1991 Mar 8;251(4998):1223-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cell Biology and Metabolism 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/1900950" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; B-Lymphocytes/*immunology ; Chickens ; Egg White ; Enzyme-Linked Immunosorbent Assay ; Female ; Fluorescein-5-isothiocyanate ; Fluoresceins ; Fluorescent Dyes ; *Immune Tolerance ; Mice ; Mice, Inbred C57BL ; Mice, Transgenic ; Muramidase/blood/*genetics/immunology ; T-Lymphocytes/*immunology ; Thiocyanates
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  • 66
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1991-12-13
    Description: In mammals, retinol is the precursor for retinoids, which affect various aspects of morphogenesis and development. However, B lymphocytes, although retinol-dependent, do not use retinoic acid as mediator. Retinol is metabolized by B lymphocytes and other cell lines to optically active 14-hydroxy-4,14-retro-retinol; it is this compound that mediates the growth control. Thus another second messenger molecule, in addition to retinoic acid and retinal, is derived from retinol.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Buck, J -- Derguini, F -- Levi, E -- Nakanishi, K -- Hammerling, U -- AI38351/AI/NIAID NIH HHS/ -- CA49933/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1991 Dec 13;254(5038):1654-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Immunology, Memorial Sloan-Kettering Cancer Center, New York, New York 10021.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1749937" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; B-Lymphocytes/physiology ; Cell Line ; Growth Substances ; Humans ; Magnetic Resonance Spectroscopy ; Mice ; Retinoids/*chemistry ; Second Messenger Systems ; Signal Transduction ; Spectrophotometry, Ultraviolet ; Vitamin A/*analogs & derivatives/chemistry/physiology
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  • 67
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1991-03-08
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hamilton, D P -- New York, N.Y. -- Science. 1991 Mar 8;251(4998):1168-72.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1900949" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biomedical Research ; Federal Government ; Genes, Immunoglobulin ; *Government Regulation ; Immunoglobulin Heavy Chains/genetics ; Immunoglobulin mu-Chains/genetics ; Mice ; Mice, Transgenic ; *National Institutes of Health (U.S.) ; Publishing ; *Scientific Misconduct ; United States
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  • 68
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1991-01-11
    Description: Molecular mechanisms that mediate signal transduction by growth inhibitory cytokines are poorly understood. Type I (alpha and beta) interferons (IFNs) are potent growth inhibitory cytokines whose biological activities depend on induced changes in gene expression. IFN-alpha induced the transient activation of phospholipase A2 in 3T3 fibroblasts and rapid hydrolysis of [3H]arachidonic acid (AA) from prelabeled phospholipid pools. The phospholipase inhibitor, bromophenacyl bromide (BPB), specifically blocked IFN-induced binding of nuclear factors to a conserved, IFN-regulated enhancer element, the interferon-stimulated response element (ISRE). BPB also caused a dose-dependent inhibition of IFN-alpha-induced ISRE-dependent transcription in transient transfection assays. Specific inhibition of AA oxygenation by eicosatetraynoic acid prevented IFN-alpha induction of factor binding to the ISRE. Treatment of intact cells with inhibitors of fatty acid cyclooxygenase or lipoxygenase enzymes resulted in amplification of IFN-alpha-induced ISRE binding and gene expression. Thus, IFN-alpha receptor-coupled AA hydrolysis may function in activation of latent transcription factors by IFN-alpha and provides a system for studying the role of AA metabolism in transduction of growth inhibitory signals.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hannigan, G E -- Williams, B R -- New York, N.Y. -- Science. 1991 Jan 11;251(4990):204-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Research Institute, Hospital for Sick Children, Toronto, Ontario, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1898993" target="_blank"〉PubMed〈/a〉
    Keywords: 5,8,11,14-Eicosatetraynoic Acid/pharmacology ; Acetophenones/pharmacology ; Animals ; Arachidonic Acid ; Arachidonic Acids/*metabolism ; Base Sequence ; Cell Line ; Cyclooxygenase Inhibitors ; Enhancer Elements, Genetic ; Enzyme Activation ; Indomethacin/pharmacology ; Interferon Type I/*physiology ; Lipoxygenase Inhibitors ; Lysophosphatidylcholines/metabolism ; Masoprocol/pharmacology ; Mice ; Mice, Inbred BALB C ; Molecular Sequence Data ; Phospholipases A/antagonists & inhibitors/*metabolism ; Phospholipases A2 ; Platelet-Derived Growth Factor/pharmacology ; Second Messenger Systems ; *Signal Transduction ; Transcription Factors/metabolism ; Transcription, Genetic ; Transfection
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  • 69
    Publication Date: 1991-02-15
    Description: Transfer of a normal Chinese hamster X chromosome (carried in a mouse A9 donor cell line) to a nickel-transformed Chinese hamster cell line with an Xq chromosome deletion resulted in senescense of these previously immortal cells. At early passages of the A9/CX donor cells, the hamster X chromosome was highly active, inducing senescence in 100% of the colonies obtained after its transfer into the nickel-transformed cells. However, senescence was reduced to 50% when Chinese hamster X chromosomes were transferred from later passage A9 cells. Full senescing activity of the intact hamster X chromosome was restored by treatment of the donor mouse cells with 5-azacytidine, which induced demethylation of DNA. These results suggest that a senescence gene or genes, which may be located on the Chinese hamster X chromosome, can be regulated by DNA methylation, and that escape from senescence and possibly loss of tumor suppressor gene activity can occur by epigenetic mechanisms.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Klein, C B -- Conway, K -- Wang, X W -- Bhamra, R K -- Lin, X H -- Cohen, M D -- Annab, L -- Barrett, J C -- Costa, M -- ES 04715/ES/NIEHS NIH HHS/ -- ES 04895/ES/NIEHS NIH HHS/ -- ES 05512/ES/NIEHS NIH HHS/ -- New York, N.Y. -- Science. 1991 Feb 15;251(4995):796-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Environmental Medicine, New York University Medical Center, NY 10016.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1990442" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Fusion ; Cell Line, Transformed ; Cell Survival/*genetics ; Cell Transformation, Neoplastic/chemically induced/*genetics ; Chromosome Deletion ; Cricetinae ; Cricetulus ; Hypoxanthine Phosphoribosyltransferase/genetics ; Mice ; Nickel/*pharmacology ; X Chromosome/*drug effects
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  • 70
    Publication Date: 1991-07-26
    Description: The crystal structure of the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase complexed with a 20-amino acid substrate analog inhibitor has been solved and partially refined at 2.7 A resolution to an R factor of 0.212. The magnesium adenosine triphosphate (MgATP) binding site was located by difference Fourier synthesis. The enzyme structure is bilobal with a deep cleft between the lobes. The cleft is filled by MgATP and a portion of the inhibitor peptide. The smaller lobe, consisting mostly of amino-terminal sequence, is associated with nucleotide binding, and its largely antiparallel beta sheet architecture constitutes an unusual nucleotide binding motif. The larger lobe is dominated by helical structure with a single beta sheet at the domain interface. This lobe is primarily involved in peptide binding and catalysis. Residues 40 through 280 constitute a conserved catalytic core that is shared by more than 100 protein kinases. Most of the invariant amino acids in this conserved catalytic core are clustered at the sites of nucleotide binding and catalysis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Knighton, D R -- Zheng, J H -- Ten Eyck, L F -- Ashford, V A -- Xuong, N H -- Taylor, S S -- Sowadski, J M -- RR01644/RR/NCRR NIH HHS/ -- T32CA09523/CA/NCI NIH HHS/ -- T32DK07233/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1991 Jul 26;253(5018):407-14.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, University of California, San Diego, La Jolla 92093-0654.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1862342" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphate/metabolism ; Animals ; Binding Sites ; Computer Simulation ; Fourier Analysis ; Macromolecular Substances ; Mice ; Models, Molecular ; Protein Kinases/*chemistry/metabolism ; Recombinant Proteins/chemistry/metabolism ; X-Ray Diffraction
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  • 71
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1991-07-05
    Description: Mutations in the evolutionarily conserved codons of the p53 tumor suppressor gene are common in diverse types of human cancer. The p53 mutational spectrum differs among cancers of the colon, lung, esophagus, breast, liver, brain, reticuloendothelial tissues, and hemopoietic tissues. Analysis of these mutations can provide clues to the etiology of these diverse tumors and to the function of specific regions of p53. Transitions predominate in colon, brain, and lymphoid malignancies, whereas G:C to T:A transversions are the most frequent substitutions observed in cancers of the lung and liver. Mutations at A:T base pairs are seen more frequently in esophageal carcinomas than in other solid tumors. Most transitions in colorectal carcinomas, brain tumors, leukemias, and lymphomas are at CpG dinucleotide mutational hot spots. G to T transversions in lung, breast, and esophageal carcinomas are dispersed among numerous codons. In liver tumors in persons from geographic areas in which both aflatoxin B1 and hepatitis B virus are cancer risk factors, most mutations are at one nucleotide pair of codon 249. These differences may reflect the etiological contributions of both exogenous and endogenous factors to human carcinogenesis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hollstein, M -- Sidransky, D -- Vogelstein, B -- Harris, C C -- CA 09071/CA/NCI NIH HHS/ -- CA 43460/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1991 Jul 5;253(5015):49-53.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Human Carcinogenesis, 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/1905840" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Chickens ; DNA Mutational Analysis ; *Genes, p53 ; Haplorhini ; Humans ; Mice ; Molecular Sequence Data ; *Mutation ; Neoplasms/*genetics ; Rats ; Sequence Homology, Nucleic Acid ; Trout ; Xenopus
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  • 72
    Publication Date: 1991-03-18
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lin, C S -- Nicolelis, M A -- Schneider, J S -- Chapin, J K Jr -- New York, N.Y. -- Science. 1991 Mar 8;251(4998):1162.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1706534" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Axonal Transport ; Cerebral Cortex/*anatomy & histology ; Diencephalon/*anatomy & histology ; Horseradish Peroxidase ; Mice ; Neurons/cytology ; Rats ; Thalamus/*anatomy & histology ; gamma-Aminobutyric Acid/*physiology
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  • 73
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1991-04-26
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Barinaga, M -- New York, N.Y. -- Science. 1991 Apr 26;252(5005):505-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1850547" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Brain/physiology ; Mice ; Nerve Growth Factors/*physiology ; Neurons/physiology ; Protein-Tyrosine Kinases/genetics ; Proto-Oncogene Proteins/*genetics ; *Proto-Oncogenes ; Receptor, trkA ; Receptors, Cell Surface/*physiology ; Receptors, Nerve Growth Factor
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  • 74
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1991-07-12
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hotchin, J -- Hotchin, L B -- New York, N.Y. -- Science. 1991 Jul 12;253(5016):210.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1712986" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens, Viral/immunology ; Epitopes ; Immunity ; Mice ; Vaccines, Synthetic/adverse effects/*immunology ; Viral Vaccines/adverse effects/*immunology ; Virus Diseases/immunology/prevention & control
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  • 75
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1991-12-13
    Description: Long-term depression (LTD) in the intact cerebellum is a decrease in the efficacy of the parallel fiber-Purkinje neuron synapse induced by coactivation of climbing fiber and parallel fiber inputs. In cultured Purkinje neurons, a similar depression can be induced by iontophoretic glutamate pulses and Purkinje neuron depolarization. This form of LTD is expressed as a depression of alpha-amino-3-hydroxy-5-methyl-4- isoxazole-propionic acid (AMPA)-mediated current, and its induction is dependent on activation of metabotropic quisqualate receptors. The effect of inhibitors of protein kinase C (PKC) on LTD induction was studied. Inhibitors of PKC blocked LTD induction, while phorbol-12,13-diacetate (PDA), a PKC activator, mimicked LTD. These results suggest that PKC activation is necessary for the induction of cerebellar LTD.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Linden, D J -- Connor, J A -- New York, N.Y. -- Science. 1991 Dec 13;254(5038):1656-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurosciences, Roche Institute of Molecular Biology, Roche Research Center, Nutley, NJ 07110.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1721243" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Calcium/physiology ; Cells, Cultured ; Cerebellum/*physiology ; Enzyme Activation/drug effects ; Ibotenic Acid/analogs & derivatives/pharmacology ; In Vitro Techniques ; *Indoles ; Mice ; *Naphthalenes ; Phorbol Esters/pharmacology ; Polycyclic Compounds/pharmacology ; Protein Kinase C/antagonists & inhibitors/pharmacology/*physiology ; Purkinje Cells/*physiology ; Quisqualic Acid/pharmacology ; Receptors, AMPA ; Receptors, Neurotransmitter/physiology ; Synaptic Membranes/*physiology ; alpha-Amino-3-hydroxy-5-methyl-4-isoxazolepropionic Acid
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  • 76
    Publication Date: 1991-10-25
    Description: After antigenic stimulation of T lymphocytes, genes essential for proliferation and immune function, such as the interleukin-2 (IL-2) gene, are transcriptionally activated. In both transient transfections and T lymphocyte-specific in vitro transcription, the homeodomain-containing protein Oct-1 participated in the inducible regulation of transcription of the IL-2 gene. Oct-1 functioned in this context with a 40-kilodalton protein called Oct-1-associated protein (OAP40). In addition to interacting specifically with DNA, OAP40 reduced the rate of dissociation of Oct-1 from its cognate DNA-binding site, suggesting that a direct interaction exists between Oct-1 and OAP40.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ullman, K S -- Flanagan, W M -- Edwards, C A -- Crabtree, G R -- AI07290/AI/NIAID NIH HHS/ -- CA39612/CA/NCI NIH HHS/ -- HL33942/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1991 Oct 25;254(5031):558-62.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology and Immunology, Stanford University, CA 94305.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1683003" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antibodies, Monoclonal ; Base Sequence ; DNA-Binding Proteins/biosynthesis/*genetics/*physiology ; Enhancer Elements, Genetic ; *Gene Expression Regulation ; Genes, Homeobox ; Host Cell Factor C1 ; Interleukin-2/*genetics ; Mice ; Mice, Inbred BALB C/immunology ; Molecular Sequence Data ; Octamer Transcription Factor-1 ; Oligodeoxyribonucleotides ; Peptides/chemical synthesis/immunology ; Rats ; T-Lymphocytes/immunology/*physiology ; Transcription Factors/*genetics/physiology ; *Transcription, Genetic ; Transfection
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  • 77
    Publication Date: 1991-04-19
    Description: The development of an immunodeficiency syndrome of mice caused by a replication-defective murine leukemia virus (MuLV) is paradoxically associated with a rapid activation and proliferation of CD4+ T cells that are dependent on the presence of B cells. The responses of normal spleen cells to B cell lines that express the defective virus indicated that these lines express a cell surface determinant that shares "superantigenic" properties with some microbial antigens and Mls-like self antigens. This antigen elicited a potent proliferative response that was dependent on the presence of CD4+ T cells and was associated with selective expansion of cells bearing V beta 5. This response was markedly inhibited by a monoclonal antibody specific for the MuLV gag-encoded p30 antigen.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hugin, A W -- Vacchio, M S -- Morse, H C 3rd -- N01-AI-72622/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1991 Apr 19;252(5004):424-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Immunopathology, National Institute of Allergy and Infectious Diseases, NIH, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1850169" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens, Viral/genetics/*immunology ; B-Lymphocytes/immunology ; Gene Products, gag/genetics ; HIV-1/immunology ; Histocompatibility Antigens Class II/immunology ; Leukemia Virus, Murine/genetics/*immunology ; Lymphocyte Activation ; Mice ; Mice, Inbred CBA ; Murine Acquired Immunodeficiency Syndrome/immunology/*microbiology ; Mutation ; Receptors, Antigen, T-Cell/genetics/immunology ; T-Lymphocytes/immunology ; T-Lymphocytes, Helper-Inducer/immunology ; Virus Replication/genetics
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  • 78
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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 1991-12-06
    Description: The ability to stably deliver recombinant proteins to the systemic circulation would facilitate the treatment of a variety of acquired and inherited diseases. To explore the feasibility of the use of genetically engineered myoblasts as a recombinant protein delivery system, stable transfectants of the murine C2C12 myoblast cell line were produced that synthesize and secrete high levels of human growth hormone (hGH) in vitro. Mice injected with hGH-transfected myoblasts had significant levels of hGH in both muscle and serum that were stable for at least 3 weeks after injection. Histological examination of muscles injected with beta-galactosidase-expressing C2C12 myoblasts demonstrated that many of the injected cells had fused to form multinucleated myotubes. Thus, genetically engineered myoblasts can be used for the stable delivery of recombinant proteins into the circulation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Barr, E -- Leiden, J M -- 1 P01 DK42718-01/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1991 Dec 6;254(5037):1507-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, University of Michigan Medical Center, Ann Arbor 48109.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1962212" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Line ; Genetic Therapy/*methods ; Growth Hormone/*administration & dosage/blood ; Mice ; Muscles/*cytology/physiology ; Recombinant Proteins/*administration & dosage ; *Transfection
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  • 79
    Publication Date: 1991-06-07
    Description: As well as being activated or rendered unresponsive, mature T lymphocytes can be deleted, depending on the signals received by the cell. Deletion by programmed cell death (apoptosis) is triggered if a T cell that has received a signal through its T cell receptor complex also receives a signal through the alpha 3 domain of its class I major histocompatibility complex (MHC) molecule. Such a signal can be delivered by a CD8 molecule, which recognizes the alpha 3 domain, or by an antibody to this domain. Precursors of both cytotoxic T lymphocytes (CTL's) and T helper cells are sensitive to this signal but become resistant at some point before completing differentiation into functioning CTL's or T helper cells. Because CTL's carry CD8, they can induce cell death in T cells that recognize them. This pathway may be important in both removal of autoreactive T cells and immunoregulation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sambhara, S R -- Miller, R G -- New York, N.Y. -- Science. 1991 Jun 7;252(5011):1424-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Ontario Cancer Institute, University of Toronto, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1828618" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens, CD8 ; Antigens, Differentiation, T-Lymphocyte/physiology ; Cell Survival/physiology ; Cells, Cultured ; Histocompatibility Antigens Class I/*physiology ; In Vitro Techniques ; Interleukin-2/analysis ; Lymphocyte Culture Test, Mixed ; Mice ; Receptors, Antigen, T-Cell/*physiology ; Signal Transduction ; T-Lymphocytes/*physiology ; T-Lymphocytes, Cytotoxic/physiology
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  • 80
    Publication Date: 1991-09-06
    Description: In the mammalian central nervous system, receptors for excitatory amino acid neurotransmitters such as the alpha-amino-3-hydroxy-5-methyl-4- isoxazolepropionic acid (AMPA)-kainate receptor mediate a large fraction of excitatory transmission. Currents induced by activation of the AMPA-kainate receptor were potentiated by agents that specifically stimulate adenosine 3',5'-monophosphate (cAMP)-dependent protein kinase A (PKA) activity or were supported by intracellular application of the catalytic subunit of PKA by itself or in combination with cAMP. Furthermore, depression of these currents by a competitive inhibitor of PKA indicates that AMPA-kainate receptors are regulated by endogenous PKA. Endogenous protein phosphatases also regulate these receptors because an inhibitor of cellular phosphates enhanced kainate currents. Modulation of PKA and phosphatases may regulate the function of these receptors and thus contribute to synaptic plasticity in hippocampal neurons.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wang, L Y -- Salter, M W -- MacDonald, J F -- New York, N.Y. -- Science. 1991 Sep 6;253(5024):1132-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physiology, University of Toronto, Ontario, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1653455" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cells, Cultured ; Cyclic AMP/pharmacology/physiology ; Ethers, Cyclic/*pharmacology ; Fetus ; Hippocampus/*physiology ; Homeostasis ; Kainic Acid/*metabolism ; Kinetics ; Macromolecular Substances ; Membrane Potentials/drug effects ; Mice ; N-Methylaspartate/pharmacology ; Neurons/drug effects/*physiology ; Okadaic Acid ; Phosphoprotein Phosphatases/*metabolism ; Protein Kinase Inhibitors ; Protein Kinases/*metabolism ; Receptors, Kainic Acid ; Receptors, Neurotransmitter/drug effects/*physiology
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  • 81
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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 1991-01-11
    Description: The c-fos serum response element (SRE) is a primary nuclear target for intracellular signal transduction pathways triggered by growth factors. It is the target for both protein kinase C (PKC)-dependent and -independent signals. Function of the SRE requires binding of a cellular protein, termed serum response factor (SRF). A second protein, p62TCF, recognizes the SRE-SRF complex to form a ternary complex. A mutated SRE that bound SRF but failed to form the ternary complex selectively lost response to PKC activators, but retained response to PKC-independent signals. Thus, two different signaling pathways act through discrete nuclear targets at the SRE. At least one of these pathways functions by recruitment of a pathway-specific accessory factor (p62TCF). These results offer a molecular mechanism to account for the biological specificity of signals that appear to act through common DNA sequence elements.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Graham, R -- Gilman, M -- AI27270/AI/NIAID NIH HHS/ -- CA45642/CA/NCI NIH HHS/ -- CA46370/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1991 Jan 11;251(4990):189-92.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cold Spring Harbor Laboratory, NY 11724.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1898992" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Binding Sites ; Blood ; Cell Line ; DNA/metabolism ; *Enhancer Elements, Genetic ; Mice ; Mice, Inbred BALB C ; Molecular Sequence Data ; Mutagenesis ; Nuclear Proteins/*metabolism ; Promoter Regions, Genetic/genetics ; Protein Kinase C/metabolism ; Proto-Oncogene Proteins/*genetics ; Proto-Oncogene Proteins c-fos ; Second Messenger Systems ; Serum Response Factor ; *Signal Transduction ; Tetradecanoylphorbol Acetate/pharmacology ; Transfection
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  • 82
    Publication Date: 1991-12-20
    Description: The binding of multivalent immunoglobulin G complexes to Fc receptors (Fc gamma Rs) on macrophages activates multiple immune functions. A murine macrophage cell line, but not a fibroblast cell line, that was transfected with human Fc gamma RIIA mediated phagocytosis and an intracellular Ca2+ concentration ([Ca2+]i) flux upon cross-linking of human Fc gamma RIIA. Transfected macrophages that expressed a truncated receptor lacking 17 carboxy-terminal amino acids phagocytosed small antibody complexes. However, only wild-type transfectants phagocytosed labeled erythrocytes and fluxed [Ca2+]i. Thus, the cytoplasmic domain of human Fc gamma RIIA contains distinct functional regions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Odin, J A -- Edberg, J C -- Painter, C J -- Kimberly, R P -- Unkeless, J C -- AI 24322/AI/NIAID NIH HHS/ -- AI 24671/AI/NIAID NIH HHS/ -- AR 33062/AR/NIAMS NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1991 Dec 20;254(5039):1785-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, Mount Sinai Medical Center, New York, NY 10029.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1837175" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antibodies, Monoclonal ; Antigens, Differentiation/genetics/*physiology ; CHO Cells ; Calcium/*metabolism ; Cell Line ; Cloning, Molecular ; Cricetinae ; Homeostasis ; Humans ; Immunoglobulin G/metabolism ; Kinetics ; Macrophages ; Mice ; *Phagocytosis ; Receptors, Fc/genetics/*physiology ; Receptors, IgG ; Recombinant Proteins/metabolism ; *Transfection
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  • 83
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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 1991-01-11
    Description: Recombinant virus vaccines that express a limited number of epitopes are currently being developed to prevent disease by changing the relative balance between viral spread and the immune response. Some circumstances, however, were found in infections with a noncytopathic virus in which vaccination caused disease; sensitive parameters included the genetic background of the host, the time or dose of infection, and the constituents of the vaccine. Thus, immunopathologic damage by T cells may be an unwanted consequence of vaccination with the new types of peptide or recombinant vaccines that are being investigated for the human immunodeficiency viruses and other pathogens.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Oehen, S -- Hengartner, H -- Zinkernagel, R M -- New York, N.Y. -- Science. 1991 Jan 11;251(4990):195-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory for Experimental Pathology, University of Zurich, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1824801" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Glycoproteins/immunology ; H-2 Antigens/immunology ; Immunization ; Lymphocytic Choriomeningitis/*immunology/prevention & control ; Lymphocytic choriomeningitis virus/*immunology/isolation & purification ; Meninges/immunology/microbiology ; Mice ; Mice, Inbred BALB C ; Mice, Inbred DBA ; Nucleoproteins/immunology ; Spleen/microbiology ; T-Lymphocytes/*immunology ; T-Lymphocytes, Cytotoxic/immunology ; T-Lymphocytes, Regulatory/immunology ; Vaccines, Synthetic/*adverse effects ; Vaccinia virus/immunology ; Viral Vaccines/*adverse effects ; Virus Diseases/*prevention & control
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  • 84
    Publication Date: 1991-04-19
    Description: A model for human lymphocyte ontogeny has been developed in a normal mouse. Human bone marrow, depleted of mature T and B lymphocytes, and bone marrow from mice with severe combined immunodeficiency were transplanted into lethally irradiated BALB/c mice. Human B and T cells were first detected 2 to 4 months after transplantation and persisted for at least 6 months. Most human thymocytes (30 to 50 percent of total thymocytes) were CD3+CD4+CD8+. Human immunoglobulin was detected in some chimeras, and a human antibody response to dinitrophenol could be generated after primary and secondary immunization.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lubin, I -- Faktorowich, Y -- Lapidot, T -- Gan, Y -- Eshhar, Z -- Gazit, E -- Levite, M -- Reisner, Y -- New York, N.Y. -- Science. 1991 Apr 19;252(5004):427-31.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biophysics, Weizmann Institute of Science, Rehovot, Israel.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1826797" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antibodies/analysis ; Antibodies, Monoclonal/immunology ; Antigens, CD3 ; Antigens, Differentiation, T-Lymphocyte/immunology ; B-Lymphocytes/*cytology/immunology ; *Bone Marrow Cells ; *Bone Marrow Transplantation ; Cell Differentiation ; Chimera ; Hematopoietic Stem Cells/cytology ; Hemocyanin/immunology ; Humans ; Immunization ; Immunoglobulins/analysis ; Immunologic Deficiency Syndromes ; Immunophenotyping ; Mice ; Mice, Inbred BALB C ; Receptors, Antigen, T-Cell/immunology ; T-Lymphocytes/*cytology/immunology ; *Transplantation, Heterologous
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  • 85
    Publication Date: 1991-12-06
    Description: A recombinant gene encoding human growth hormone (hGH) was stably introduced into cultured myoblasts with a retroviral vector. After injection of genetically engineered myoblasts into mouse muscle, hGH could be detected in serum for 3 months. The fate of injected myoblasts was assessed by coinfecting the cells with two retroviral vectors, one encoding hGH and the other encoding beta-galactosidase from Escherichia coli. These results provide evidence that myoblasts, which can fuse into preexisting multinucleated myofibers that are vascularized and innervated, may be advantageous as vehicles for systemic delivery of recombinant proteins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dhawan, J -- Pan, L C -- Pavlath, G K -- Travis, M A -- Lanctot, A M -- Blau, H M -- AG-09521/AG/NIA NIH HHS/ -- HD-18179/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 1991 Dec 6;254(5037):1509-12.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, Stanford University School of Medicine, CA 94305.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1962213" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Differentiation ; Clone Cells ; Gene Expression ; Genetic Therapy/*methods ; Growth Hormone/*administration & dosage ; Humans ; Mice ; Muscles/*cytology ; Recombinant Proteins/*administration & dosage ; *Transfection
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  • 86
    Publication Date: 1991-10-11
    Description: The v-akt oncogene codes for a 105-kilodalton fusion phosphoprotein containing Gag sequences at its amino terminus. Sequence analysis of v-akt and biochemical characterization of its product revealed that it codes for a protein kinase C-related serine-threonine kinase whose cellular homolog is expressed in most tissues, with the highest amount found in thymus. Although Akt is a serine-threonine kinase, part of its regulatory region is similar to the Src homology-2 domain, a structural motif characteristic of cytoplasmic tyrosine kinases that functions in protein-protein interactions. This suggests that Akt may form a functional link between tyrosine and serine-threonine phosphorylation pathways.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bellacosa, A -- Testa, J R -- Staal, S P -- Tsichlis, P N -- CA-06927/CA/NCI NIH HHS/ -- CA-38047/CA/NCI NIH HHS/ -- RR-05539/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 1991 Oct 11;254(5029):274-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medical Oncology, Fox Chase Cancer Center, Philadelphia, PA 19111.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1833819" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Mice ; Mink ; Mink Cell Focus-Inducing Viruses/genetics ; Molecular Sequence Data ; Oncogene Protein v-akt ; Oncogenes/*genetics ; Protein Kinases/*genetics ; Protein-Serine-Threonine Kinases ; Protein-Tyrosine Kinases/*genetics ; Retroviridae Proteins, Oncogenic/*genetics ; Sequence Homology, Nucleic Acid
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  • 87
    Publication Date: 1991-07-19
    Description: Alzheimer's disease is characterized by widespread deposition of amyloid in the central nervous system. The 4-kilodalton amyloid beta protein is derived from a larger amyloid precursor protein and forms amyloid deposits in the brain by an unknown pathological mechanism. Except for aged nonhuman primates, there is no animal model for Alzheimer's disease. Transgenic mice expressing amyloid beta protein in the brain could provide such a model. To investigate this possibility, the 4-kilodalton human amyloid beta protein was expressed under the control of the promoter of the human amyloid precursor protein in two lines of transgenic mice. Amyloid beta protein accumulated in the dendrites of some but not all hippocampal neurons in 1-year-old transgenic mice. Aggregates of the amyloid beta protein formed amyloid-like fibrils that are similar in appearance to those in the brains of patients with Alzheimer's disease.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wirak, D O -- Bayney, R -- Ramabhadran, T V -- Fracasso, R P -- Hart, J T -- Hauer, P E -- Hsiau, P -- Pekar, S K -- Scangos, G A -- Trapp, B D -- New York, N.Y. -- Science. 1991 Jul 19;253(5017):323-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Molecular Therapeutics Inc., Miles Research Center, West Haven, CT 06516.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1857970" target="_blank"〉PubMed〈/a〉
    Keywords: Alzheimer Disease/*genetics/pathology ; Amyloid beta-Peptides/analysis/*genetics ; Animals ; Base Sequence ; Brain/*metabolism/pathology ; DNA/genetics ; Hippocampus/ultrastructure ; Humans ; Mice ; Mice, Transgenic ; Microscopy, Electron ; Molecular Sequence Data ; Neurofibrils/ultrastructure ; Oligonucleotide Probes ; Restriction Mapping
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  • 88
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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 1991-05-03
    Description: Major histocompatibility complex (MHC) class II genes are coordinately regulated and show tissue-specific expression. With the use of in vivo footprinting, common promoter sites in these genes were found to be occupied only in cells that expressed the genes, in spite of the presence of the promoter binding proteins. In vivo analysis of mutant cell lines that exhibited coordinate loss of class II MHC expression, including several from individuals with bare lymphocyte syndrome, revealed two in vivo phenotypes. One suggests a defect in gene activation, whereas the other suggests a defect in promoter accessibility.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kara, C J -- Glimcher, L H -- AI21163/AI/NIAID NIH HHS/ -- GM36864/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1991 May 3;252(5006):709-12.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cancer Biology, Harvard School of Public Health, Boston, MA 02115.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1902592" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; B-Lymphocytes/*immunology ; Base Sequence ; Cell Line ; DNA/genetics ; *Gene Expression ; Genes, MHC Class II/*genetics ; Humans ; Mice ; Mice, Inbred BALB C ; Molecular Sequence Data ; *Mutation ; Polymerase Chain Reaction ; *Promoter Regions, Genetic ; Regulatory Sequences, Nucleic Acid ; Syndrome
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  • 89
    Publication Date: 1991-08-23
    Description: The alpha beta and gamma delta T cell receptors for antigen (TCR) delineate distinct T cell populations. TCR alpha beta-bearing thymocytes must be positively selected by binding of the TCR to major histocompatibility complex (MHC) molecules on thymic epithelium. To examine the requirement for positive selection of TCR gamma delta T cells, mice bearing a class I MHC-specific gamma delta transgene (Tg) were crossed to mice with disrupted beta 2 microglobulin (beta 2M) genes. The Tg+beta 2M- (class I MHC-) offspring had Tg+ thymocytes that did not proliferate to antigen or Tg-specific monoclonal antibody and few peripheral Tg+ cells. This is evidence for positive selection within the gamma delta T cell subset.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wells, F B -- Gahm, S J -- Hedrick, S M -- Bluestone, J A -- Dent, A -- Matis, L A -- AI 26847-03/AI/NIAID NIH HHS/ -- AI00602/AI/NIAID NIH HHS/ -- N01-C0-74102/PHS HHS/ -- New York, N.Y. -- Science. 1991 Aug 23;253(5022):903-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Biological Carcinogenesis and Development Program, Program Resources, Inc./DynCorp, NCI-Frederick Cancer Research and Development Center, MD 21701-0201.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1831565" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Division ; Epithelium/immunology ; Flow Cytometry ; H-2 Antigens/immunology ; Histocompatibility Antigens Class I/immunology ; Lymph Nodes/cytology ; Mice ; Mice, Inbred BALB C ; Mice, Nude ; Mice, Transgenic ; Receptors, Antigen, T-Cell/immunology/*metabolism ; Spleen/cytology ; T-Lymphocytes/cytology/*immunology ; T-Lymphocytes, Helper-Inducer/cytology/immunology ; T-Lymphocytes, Regulatory/cytology/immunology ; Thymus Gland/immunology ; beta 2-Microglobulin/genetics
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  • 90
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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 1991-08-02
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kenyon, C -- Wang, B -- New York, N.Y. -- Science. 1991 Aug 2;253(5019):516-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Biophysics, University of California, San Francisco 94143.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1677487" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Caenorhabditis/genetics ; Drosophila/genetics ; *Genes, Homeobox ; Mice ; Molecular Sequence Data ; Sequence Homology, Nucleic Acid ; Species Specificity
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  • 91
    Publication Date: 1991-08-02
    Description: Transgenic mice carrying the bel region of human foamy retrovirus (HFV) under transcriptional control of its own long terminal repeat expressed the transgene in their central nervous systems and in smooth and striated muscle tissues. The animals developed a progressive degenerative disease of the central nervous system and of the striated muscle. Because expression of the transgene was closely correlated with the appearance of structural damage and inflammatory reactions were scanty, the disease is likely to be caused directly by the HFV proteins. These unexpected findings call for a reevaluation of the pathogenic potential of HFV in humans.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bothe, K -- Aguzzi, A -- Lassmann, H -- Rethwilm, A -- Horak, I -- New York, N.Y. -- Science. 1991 Aug 2;253(5019):555-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Virology and Immunobiology, University of Wurzburg, Federal Republic of Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1650034" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Brain/*pathology ; Cerebellum/pathology ; DNA, Viral/administration & dosage/genetics ; Genes, Viral ; Hippocampus/pathology ; Humans ; Mice ; Mice, Transgenic ; Muscles/*pathology ; Neurons/*pathology ; Restriction Mapping ; Retroviridae Infections/*genetics/pathology ; Spumavirus/*genetics
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    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 92
    Publication Date: 1991-09-13
    Description: Viruses frequently persist in neurons, suggesting that these cells can evade immune surveillance. In a mouse model, 5 x 10(6) cytotoxic T lymphocytes (CTLs), specific for lymphocytic choriomeningitis virus (LCMV), did not lyse infected neurons or cause immunopathologic injury. In contrast, intracerebral injection of less than 10(3) CTL caused disease and death when viral antigens were expressed on leptomeningeal and choroid plexus cells of the nervous system. The neuronal cell line OBL21 expresses little or no major histocompatibility (MHC) class I surface glycoproteins and when infected with LCMV, resisted lysis by virus-specific CTLs. Expression of MHC heavy chain messenger RNA was limited, but beta 2-microglobulin messenger RNA and protein was made normally. OBL21 cells were made sensitive to CTL lysis by transfection with a fusion gene encoding another MHC class I molecule. Hence, neuronal cells probably evade immune surveillance by failing to express MHC class I molecules.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Joly, E -- Mucke, L -- Oldstone, M B -- New York, N.Y. -- Science. 1991 Sep 13;253(5025):1283-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neuropharmacology, Scripps Clinic and Research Foundation, La Jolla, CA 92037.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1891717" target="_blank"〉PubMed〈/a〉
    Keywords: Acute Disease ; Animals ; Brain/immunology/*microbiology ; Cell Line ; Chronic Disease ; Gene Expression ; *Genes, MHC Class I ; Histocompatibility Antigens Class I/analysis ; Lymphocytic Choriomeningitis/*immunology ; Lymphocytic choriomeningitis virus/immunology/*pathogenicity ; Mice ; Mice, Inbred Strains ; Neurons/immunology/*microbiology ; T-Lymphocytes, Cytotoxic/*immunology
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    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 93
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1991-07-19
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marx, J -- New York, N.Y. -- Science. 1991 Jul 19;253(5017):266-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1907022" target="_blank"〉PubMed〈/a〉
    Keywords: Alzheimer Disease/*genetics/pathology ; Amyloid beta-Peptides/*genetics ; Amyloid beta-Protein Precursor ; Animals ; Brain/metabolism/pathology ; Disease Models, Animal ; Humans ; Mice ; *Mice, Transgenic ; Protein Precursors/*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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  • 94
    Publication Date: 1991-10-04
    Description: A DNA construct containing the bacterial beta-galactosidase gene (lacZ) was used to study somatic DNA recombination in the transgenic mouse brain. Recombination-positive areas of the adult brain were stained blue with X-gal, a substrate of beta-galactosidase. Blue-colored cells appeared soon after birth, and continued to emerge in postnatal tissue. Staining was prominent in sensory as opposed to motor regions of the brain, and was present in more than 70 discrete areas of the nervous system. The possibility of DNA rearrangement is discussed with respect to the development of the central nervous system.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Matsuoka, M -- Nagawa, F -- Okazaki, K -- Kingsbury, L -- Yoshida, K -- Muller, U -- Larue, D T -- Winer, J A -- Sakano, H -- AI18790/AI/NIAID NIH HHS/ -- NS16832/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1991 Oct 4;254(5028):81-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Immunology, University of California, Berkeley 94720.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1925563" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Blotting, Southern ; Brain/*physiology ; Brain Mapping ; *Gene Rearrangement ; Mice ; Mice, Transgenic/genetics ; Molecular Sequence Data ; Neurons, Afferent/physiology ; Promoter Regions, Genetic ; *Recombination, Genetic ; beta-Galactosidase/genetics
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 95
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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 1991-05-10
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cherfas, J -- New York, N.Y. -- Science. 1991 May 10;252(5007):782.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2028253" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Female ; Gene Expression Regulation/genetics ; Genes, Switch/*physiology ; Male ; Mice ; Mice, Transgenic ; *Sex Determination Analysis ; Sex Differentiation/physiology ; Testis/embryology ; *Y Chromosome
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 96
    Publication Date: 1991-08-16
    Description: The expression of the V(D)J [variable (diversity) joining elements] recombination activating genes, RAG-1 and RAG-2, has been examined during T cell development in the thymus. In situ hybridization to intact thymus and RNA blot analysis of isolated thymic subpopulations separated on the basis of T cell receptor (TCR) expression demonstrated that both TCR- and TCR+ cortical thymocytes express RAG-1 and RAG-2 messenger RNA's. Within the TCR+ population, RAG expression was observed in immature CD4+CD8+ (double positive) cells, but not in the more mature CD4+CD8- or CD4-CD8+ (single positive) subpopulations. Thus, although cortical thymocytes that bear TCR on their surface continue to express RAG-1 and RAG-2, it appears that the expression of both genes is normally terminated during subsequent thymic maturation. Since thymocyte maturation in vivo is thought to be regulated through the interaction of the TCR complex with self major histocompatibility complex (MHC) antigens, these data suggest that signals transduced by the TCR complex might result in the termination of RAG expression. Consistent with this hypothesis, thymocyte TCR cross-linking in vitro led to rapid termination of RAG-1 and RAG-2 expression, whereas cross-linking of other T cell surface antigens such as CD4, CD8, or HLA class I had no effect.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Turka, L A -- Schatz, D G -- Oettinger, M A -- Chun, J J -- Gorka, C -- Lee, K -- McCormack, W T -- Thompson, C B -- DK-01899/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1991 Aug 16;253(5021):778-81.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Internal Medicine, University of Michigan, Ann Arbor 48109.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1831564" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens, CD/physiology ; Antigens, CD3 ; Antigens, Differentiation, T-Lymphocyte/physiology ; Cell Differentiation ; Cell Survival ; DNA Nucleotidyltransferases/*genetics ; *DNA-Binding Proteins ; Gene Expression ; *Gene Rearrangement, T-Lymphocyte ; *Homeodomain Proteins ; Humans ; Mice ; Nuclear Proteins ; Nucleic Acid Hybridization ; Proteins/*genetics ; RNA, Messenger/genetics ; Receptor Aggregation ; Receptors, Antigen, T-Cell/*physiology ; Receptors, Interleukin-2/genetics ; T-Lymphocyte Subsets/enzymology/*physiology ; Thymus Gland/cytology/*enzymology ; VDJ Recombinases
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 97
    Publication Date: 1991-11-01
    Description: The generation of antigen-specific antitumor immunity is the ultimate goal in cancer immunotherapy. When cells from a spontaneously arising murine renal cell tumor were engineered to secrete large doses of interleukin-4 (IL-4) locally, they were rejected in a predominantly T cell-independent manner. However, animals that rejected the IL-4-transfected tumors developed T cell-dependent systemic immunity to the parental tumor. This systemic immunity was tumor-specific and primarily mediated by CD8+ T cells. Established parental tumors could be cured by the systemic immune response generated by injection of the genetically engineered tumors. These results provide a rationale for the use of lymphokine gene-transfected tumor cells as a modality for cancer therapy.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Golumbek, P T -- Lazenby, A J -- Levitsky, H I -- Jaffee, L M -- Karasuyama, H -- Baker, M -- Pardoll, D M -- New York, N.Y. -- Science. 1991 Nov 1;254(5032):713-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine, Johns Hopkins University, Baltimore, MD 21205.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1948050" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Carcinoma, Renal Cell/genetics/immunology/pathology/*therapy ; Cell Division ; Cell Line ; *Immunotherapy ; Interleukin-4/*genetics/secretion ; Kidney Neoplasms/genetics/immunology/pathology/*therapy ; Lymphocyte Depletion ; Mice ; Mice, Inbred BALB C ; Mice, SCID ; Neoplasm Transplantation ; *Protein Engineering ; T-Lymphocyte Subsets/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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