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  • Cell Line  (65)
  • 42.75
  • Chemical Engineering
  • Chemistry
  • American Association for the Advancement of Science (AAAS)  (68)
  • 1990-1994  (68)
  • 1950-1954
  • 1991  (68)
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  • 1990-1994  (68)
  • 1950-1954
Year
  • 1
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    Subtle cerebellar phenotype in mice homozygous for a targeted deletion of the En-2 homeobox (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    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
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 2
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    Clathrate hydrate formation in amorphous cometary ice analogs in vacuo (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-10-25
    Description: The presence of clathrate hydrates in cometary ice has been suggested to account for anomalous gas release at large radial distances from the sun as well as the retention of volatiles in comets to elevated temperatures. However, how clathrate hydrates can form in low-pressure environments, such as in cold interstellar molecular clouds, in the outer reaches of the early solar nebula, or in cometary ices, has been poorly understood. Experiments performed with the use of a modified electron microscope demonstrate that during the warming of vapor-deposited amorphous ices in vacuo, clathrate hydrates can form by rearrangements in the solid state. Phase separations and microporous textures that are the result of these rearrangements may account for a variety of anomalous cometary phenomena.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Blake, D -- Allamandola, L -- Sandford, S -- Hudgins, D -- Freund, F -- New York, N.Y. -- Science. 1991 Oct 25;254:548-51.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Planetary Biology Branch, Ames Research Center, Moffett Field, CA 94035, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11538372" target="_blank"〉PubMed〈/a〉
    Keywords: Chemical Phenomena ; Chemistry ; Crystallography ; Earth (Planet) ; Hydrocarbons/chemistry ; Ice/*analysis ; *Meteoroids ; Microscopy, Electron ; *Solar System
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 3
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    Negative regulation of CD45 protein tyrosine phosphatase activity by ionomycin in T cells (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    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
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 4
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    Differentiation of 3T3-L1 fibroblasts to adipocytes induced by transfection of ras oncogenes (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    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
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 5
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    Lateral movements of membrane glycoproteins restricted by dynamic cytoplasmic barriers (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    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
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 6
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    Lysyl oxidase and rrg messenger RNA (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    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
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 7
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    In vitro and in vivo consequences of VLA-2 expression on rhabdomyosarcoma cells (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    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
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 8
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    Interaction of the IL-2 receptor with the src-family kinase p56lck: identification of novel intermolecular association (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-06-14
    Description: In the interleukin-2 (IL-2) system, intracellular signal transduction is triggered by the beta chain of the IL-2 receptor (IL-2R beta); however, the responsible signaling mechanism remains unidentified. Evidence for the formation of a stable complex of IL-2R beta and the lymphocyte-specific protein tyrosine kinase p56lck is presented. Specific association sites were identified in the tyrosine kinase catalytic domain of p56lck and in the cytoplasmic domain of IL-2R beta. As a result of interaction, IL-2R beta became phosphorylated in vitro by p56lck. Treatment of T lymphocytes with IL-2 promotes p56lck kinase activity. These data suggest the participation of p56lck as a critical signaling molecule downstream of IL-2R via a novel interaction.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hatakeyama, M -- Kono, T -- Kobayashi, N -- Kawahara, A -- Levin, S D -- Perlmutter, R M -- Taniguchi, T -- New York, N.Y. -- Science. 1991 Jun 14;252(5012):1523-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute for Molecular and Cellular Biology, Osaka University, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2047859" target="_blank"〉PubMed〈/a〉
    Keywords: Adult ; Animals ; Antigens, CD/immunology ; Base Sequence ; Binding Sites ; Cell Division/drug effects ; Cell Line ; Humans ; Interleukin-2/pharmacology ; Killer Cells, Natural/cytology/drug effects/immunology ; Lymphocyte Activation ; Lymphocyte Specific Protein Tyrosine Kinase p56(lck) ; Lymphocytes/drug effects/*immunology ; Macromolecular Substances ; Molecular Sequence Data ; Molecular Weight ; Oligonucleotide Probes ; Protein-Tyrosine Kinases/genetics/isolation & purification/*metabolism ; Receptors, Interleukin-2/genetics/isolation & purification/*physiology ; *Signal Transduction ; 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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  • 9
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    Recognition of self antigens by skin-derived T cells with invariant gamma delta antigen receptors (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    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
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 10
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    Regulation of adhesion of ICAM-1 by the cytoplasmic domain of LFA-1 integrin beta subunit (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-03-29
    Description: Interactions between cytotoxic lymphocytes and their targets require the T cell antigen receptor (TCR) and the integrin lymphocyte function-associated molecule-1 (LFA-1, CD11a/CD18). LFA-1 is not constitutively avid for its counter-receptors, intercellular adhesion molecules (ICAMs)-1 and -2. Cross-linking of the TCR transiently converts LFA-1 to a high avidity state and thus provides a mechanism for regulating cellular adhesion and de-adhesion in an antigen-specific manner. Truncation of the cytoplasmic domain of the beta, but not the alpha, subunit of LFA-1 eliminated binding to ICAM-1 and sensitivity to phorbol esters. Thus, LFA-1 binding to ICAM-1 was found to be regulated by the cytoplasmic domain of the beta subunit of LFA-1.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hibbs, M L -- Xu, H -- Stacker, S A -- Springer, T A -- CA31798/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1991 Mar 29;251(5001):1611-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for Blood Research, Harvard Medical School, Boston, MA 02115.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1672776" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; *Cell Adhesion ; Cell Adhesion Molecules/*physiology ; Cell Line ; Flow Cytometry ; Intercellular Adhesion Molecule-1 ; Lymphocyte Function-Associated Antigen-1/genetics/*physiology ; Macromolecular Substances ; Molecular Sequence Data ; Receptors, Antigen, T-Cell/*physiology ; Tetradecanoylphorbol Acetate/pharmacology ; Transfection
    Print ISSN: 0036-8075
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  • 11
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    A heparin-binding growth factor secreted by macrophage-like cells that is related to EGF (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-02-22
    Description: Macrophage-like U-937 cells secrete a 22-kilodalton heparin-binding growth factor that is mitogenic for BALB-3T3 fibroblasts and smooth muscle cells, but not endothelial cells. The amino acid sequence predicted from complementary DNA clones indicates that the mitogen is a new member of the epidermal growth factor (EGF) family. This heparin-binding EGF-like growth factor (HB-EGF) binds to EGF receptors on A-431 epidermoid carcinoma cells and smooth muscle cells, but is a far more potent mitogen for smooth muscle cells than is EGF. HB-EGF is also expressed in cultured human macrophages and may be involved in macrophage-mediated cellular proliferation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Higashiyama, S -- Abraham, J A -- Miller, J -- Fiddes, J C -- Klagsbrun, M -- CA37392/CA/NCI NIH HHS/ -- CA45548/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1991 Feb 22;251(4996):936-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Surgical Research, Children's Hospital, Boston, MA 02115.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1840698" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Cell Division/drug effects ; Cell Line ; Chromatography, Affinity ; Chromatography, High Pressure Liquid ; DNA Replication/drug effects ; Epidermal Growth Factor/genetics/isolation & ; purification/*metabolism/pharmacology ; Growth Substances/*metabolism ; Heparin/*metabolism ; Humans ; Kinetics ; Macrophages/*metabolism ; Molecular Sequence Data ; Protein Binding ; Receptor, Epidermal Growth Factor/metabolism ; Sequence Homology, Nucleic Acid
    Print ISSN: 0036-8075
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  • 12
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    Expression cDNA cloning of the KGF receptor by creation of a transforming autocrine loop (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    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
    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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  • 13
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    Targets for dioxin: genes for plasminogen activator inhibitor-2 and interleukin-1 beta (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-10-18
    Description: Dioxin (2,3,7,8-tetrachlorodibenzo-p-dioxin, TCDD), a widespread environmental contaminant, may elicit its effects by altering gene expression in susceptible cells. Five TCDD-responsive complementary DNA clones were isolated from a human keratinocyte cell line. One of these clones encodes plasminogen activator inhibitor-2, a factor that influences growth and differentiation by regulating proteolysis of the extracellular matrix. Another encodes the cytokine interleukin-1 beta. Thus, TCDD alters the expression of growth regulatory genes and has effects similar to those of other tumor-promoting agents that affect both inflammation and differentiation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sutter, T R -- Guzman, K -- Dold, K M -- Greenlee, W F -- New York, N.Y. -- Science. 1991 Oct 18;254(5030):415-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Chemical Industry Institute of Toxicology, Research Triangle Park, NC 27709.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1925598" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Blood Physiological Phenomena ; Blotting, Northern ; Calcium/pharmacology ; Cell Line ; Cloning, Molecular ; Cycloheximide/pharmacology ; Gene Expression Regulation/drug effects ; Humans ; Interleukin-1/*genetics ; *Plasminogen Inactivators ; RNA, Messenger/drug effects ; Tetrachlorodibenzodioxin/*pharmacology ; Transcription, Genetic/drug effects
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  • 14
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    Requirement of heparan sulfate for bFGF-mediated fibroblast growth and myoblast differentiation (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    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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  • 15
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    Generation of cAMP-activated chloride currents by expression of CFTR (1991)
    American Association for the Advancement of Science (AAAS)
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    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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  • 16
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    Cloning of a factor required for activity of the Ah (dioxin) receptor (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-05-17
    Description: The aryl hydrocarbon (Ah) receptor binds various environmental pollutants, such as polycyclic aromatic hydrocarbons, heterocyclic amines, and polychlorinated aromatic compounds (dioxins, dibenzofurans, and biphenyls), and mediates the carcinogenic effects of these agents. The complementary DNA and part of the gene for an 87-kilodalton human protein that is necessary for Ah receptor function have been cloned. The protein is not the ligand-binding subunit of the receptor but is a factor that is required for the ligand-binding subunit to translocate from the cytosol to the nucleus after binding ligand. The requirement for this factor distinguishes the Ah receptor from the glucocorticoid receptor, to which the Ah receptor has been presumed to be similar. Two portions of the 87-kilodalton protein share sequence similarities with two Drosophila proteins, Per and Sim. Another segment of the protein shows conformity to the consensus sequence for the basic helix-loop-helix motif found in proteins that bind DNA as homodimers or heterodimers.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hoffman, E C -- Reyes, H -- Chu, F F -- Sander, F -- Conley, L H -- Brooks, B A -- Hankinson, O -- CA 16048/CA/NCI NIH HHS/ -- CA 28868/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1991 May 17;252(5008):954-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pathology, University of California, Los Angeles 90024.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1852076" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Aryl Hydrocarbon Receptor Nuclear Translocator ; Base Sequence ; Cell Line ; Cell Nucleus/metabolism ; Cloning, Molecular ; Cytosol/metabolism ; *DNA-Binding Proteins ; Humans ; Macromolecular Substances ; Molecular Sequence Data ; Molecular Weight ; Oligonucleotide Probes ; Proteins/*genetics/metabolism ; RNA, Messenger/genetics ; Receptors, Aryl Hydrocarbon ; Receptors, Drug/genetics/*metabolism ; Sequence Homology, Nucleic Acid ; Tetrachlorodibenzodioxin/*metabolism ; *Transcription Factors ; Transfection
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  • 17
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    Putting new muscle into gene therapy (1991)
    American Association for the Advancement of Science (AAAS)
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    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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  • 18
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    A 32-kD GTP-binding protein associated with the CD4-p56lck and CD8-p56lck T cell receptor complexes (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-10-18
    Description: The guanosine triphosphate (GTP)-binding proteins include signal-transducing heterotrimeric G proteins (for example, Gs, Gi), smaller GTP-binding proteins that function in protein sorting, and the oncogenic protein p21ras. The T cell receptor complexes CD4-p56lck and CD8-p56lck were found to include a 32- to 33-kilodalton phosphoprotein (p32) that was recognized by an antiserum to a consensus GTP-binding region in G proteins. Immunoprecipitated CD4 and CD8 complexes bound GTP and hydrolyzed it to guanosine diphosphate (GDP). The p32 protein was covalently linked to [alpha-32P]GTP by ultraviolet photoaffinity labeling. These results demonstrate an interaction between T cell receptor complexes and an intracellular GTP-binding protein.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Telfer, J C -- Rudd, C E -- New York, N.Y. -- Science. 1991 Oct 18;254(5030):439-41.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Tumor Immunology, Dana-Farber Cancer Institute, Boston, MA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1925604" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Antigens, CD4/*metabolism ; Antigens, CD8/*metabolism ; Cell Line ; GTP-Binding Proteins/*metabolism ; Humans ; Lymphocyte Specific Protein Tyrosine Kinase p56(lck) ; Molecular Sequence Data ; Phosphoproteins/metabolism ; Precipitin Tests ; Protein Binding ; Protein-Tyrosine Kinases/*metabolism ; Receptors, Antigen, T-Cell/*metabolism
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 19
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    Genetic survey gains momentum (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-10-25
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Roberts, L -- New York, N.Y. -- Science. 1991 Oct 25;254(5031):517.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1948023" target="_blank"〉PubMed〈/a〉
    Keywords: *Anthropology ; Cell Line ; Continental Population Groups/*genetics ; DNA/blood/*genetics/isolation & purification ; *Human Genome Project ; Humans
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 20
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    Oligoclonal expansion and CD1 recognition by human intestinal intraepithelial lymphocytes (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-09-20
    Description: A human intestinal intraepithelial lymphocyte (IEL) T cell line was established from jejunum to characterize the structure and function of the alpha beta T cell antigen receptors (TCRs) expressed by this population. Single-sided polymerase chain reaction (PCR) amplification cloning and quantitative PCR amplification of the TCR chains from the cell line and from fresh IELs demonstrated that IELs were oligoclonal. The IEL T cell line exhibited CD1-specific cytotoxicity and a dominant IEL T cell clone was CD1c-specific. Thus, human jejunal intraepithelial lymphocytes are oligoclonal and recognize members of the CD1 gene family.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Balk, S P -- Ebert, E C -- Blumenthal, R L -- McDermott, F V -- Wucherpfennig, K W -- Landau, S B -- Blumberg, R S -- 5 KO8 DK01886/DK/NIDDK NIH HHS/ -- CA-01310/CA/NCI NIH HHS/ -- DK42166/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1991 Sep 20;253(5026):1411-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Hematology-Oncology Division, Beth Israel Hospital, Harvard Medical School, Boston, MA 02215.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1716785" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Antigens, CD/*genetics/immunology ; Antigens, CD1 ; Base Sequence ; Cell Line ; Clone Cells ; Epithelium/physiology ; Humans ; Jejunum/immunology ; Molecular Sequence Data ; Oligonucleotide Probes ; Polymerase Chain Reaction/methods ; Receptors, Antigen, T-Cell/*genetics ; T-Lymphocytes/*immunology
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  • 21
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    Deep UV photochemistry of chemisorbed monolayers: patterned coplanar molecular assemblies (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-04-26
    Description: Deep ultraviolet (UV) irradiation is shown to modify organosilane self-assembled monolayer (SAM) films by a photocleavage mechanism, which renders the surface amenable to further SAM modification. Patterned UV exposure creates alternating regions of intact SAM film and hydrophilic, reactive sites. The exposed regions can undergo a second chemisorption reaction to produce an assembly of SAMs in the same molecular plane with similar substrate attachment chemistry. The UV-patterned films are used as a template for selective buildup of fluorophores, metals, and biological cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dulcey, C S -- Georger, J H Jr -- Krauthamer, V -- Stenger, D A -- Fare, T L -- Calvert, J M -- New York, N.Y. -- Science. 1991 Apr 26;252(5005):551-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Geo-Centers, Inc., Fort Washington, MD 20744.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2020853" target="_blank"〉PubMed〈/a〉
    Keywords: Axons/physiology/*radiation effects ; Cell Adhesion/radiation effects ; Cell Line ; Cell Survival/radiation effects ; Humans ; Neuroblastoma ; Photochemistry ; *Ultraviolet Rays
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  • 22
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    Primary structure and functional expression of the 5HT3 receptor, a serotonin-gated ion channel (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    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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  • 23
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    Variable effects of phosphorylation of Pit-1 dictated by the DNA response elements (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-08-16
    Description: Pit-1, a tissue-specific POU domain transcription factor, is required for the activation of the prolactin, growth hormone, and Pit-1 promoters that confer regulation by epidermal growth factor, adenosine 3',5'-monophosphate (cAMP), and phorbol esters. Pit-1 is phosphorylated in pituitary cells at two distinct sites in response to phorbol esters and cAMP. Phosphorylation of Pit-1 modifies its conformation on DNA recognition elements and results in increased binding at certain sites and decreased binding at other sites, dependent on DNA sequences adjacent to the core Pit-1 binding motif. One residue (Thr220), located in the POU homeodomain within a sequence conserved throughout the POU-domain family, confers these responses.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kapiloff, M S -- Farkash, Y -- Wegner, M -- Rosenfeld, M G -- DK 18477/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1991 Aug 16;253(5021):786-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Eukaryotic Regulatory Biology Program, School of Medicine, University of California, San Diego, La Jolla 92093-0648.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1652153" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Binding Sites ; Cell Line ; Cyclic AMP/pharmacology ; DNA/metabolism ; DNA-Binding Proteins/chemistry/*physiology ; In Vitro Techniques ; Molecular Sequence Data ; Peptide Mapping ; Phosphorylation ; Phosphothreonine/metabolism ; Pituitary Gland/*physiology ; Protein Kinases/metabolism ; Regulatory Sequences, Nucleic Acid ; Structure-Activity Relationship ; Tetradecanoylphorbol Acetate/pharmacology ; Transcription Factor Pit-1 ; Transcription Factors/chemistry/*physiology ; Trypsin
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  • 24
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    The trk proto-oncogene product: a signal transducing receptor for nerve growth factor (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    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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  • 25
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    Identification of the hepatocyte growth factor receptor as the c-met proto-oncogene product (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-02-15
    Description: Hepatocyte growth factor (HGF) is a plasminogen-like protein thought to be a humoral mediator of liver regeneration. A 145-kilodalton tyrosyl phosphoprotein observed in rapid response to HGF treatment of intact target cells was identified by immunoblot analysis as the beta subunit of the c-met proto-oncogene product, a membrane-spanning tyrosine kinase. Covalent cross-linking of 125I-labeled ligand to cellular proteins of appropriate size that were recognized by antibodies to c-met directly established the c-met product as the cell-surface receptor for HGF.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bottaro, D P -- Rubin, J S -- Faletto, D L -- Chan, A M -- Kmiecik, T E -- Vande Woude, G F -- Aaronson, S A -- New York, N.Y. -- Science. 1991 Feb 15;251(4995):802-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Cellular and Molecular Biology, National Cancer Institute, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1846706" target="_blank"〉PubMed〈/a〉
    Keywords: Cell Line ; Cross-Linking Reagents ; Growth Substances/*metabolism/physiology ; Hepatocyte Growth Factor ; Humans ; Molecular Weight ; Phosphorylation ; Precipitin Tests ; Protein-Tyrosine Kinases/*metabolism ; Proto-Oncogene Proteins/*metabolism ; Proto-Oncogene Proteins c-met ; Receptors, Cell Surface/*metabolism
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  • 26
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    Effect of light chain V region duplication on IgG oligomerization and in vivo efficacy (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-05-03
    Description: A human immunoglobulin G1 (IgG1) antibody oligomer was isolated from a transfected myeloma cell line that produced a monoclonal antibody to group B streptococci. Compared to the IgG1 monomer, the oligomer was significantly more effective at protecting neonatal rats from infection in vivo. The oligomer was also shown to cross the placenta and to be stable in neonatal rats. Immunochemical analysis and complementary DNA sequencing showed that the transfected cell line produced two distinct kappa light chains: a normal light chain (Ln) with a molecular mass of 25 kilodaltons and a 37-kilodalton species (L37), the domain composition of which was variable-variable-constant (V-V-C). Cotransfection of vectors encoding the heavy chain and L37 resulted in production of oligomeric IgG.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shuford, W -- Raff, H V -- Finley, J W -- Esselstyn, J -- Harris, L J -- New York, N.Y. -- Science. 1991 May 3;252(5006):724-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Immune Sciences, Bristol-Myers Squibb Pharmaceutical Research Institute-Seattle, WA 98121.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1902593" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Animals, Newborn ; Antibodies, Bacterial/biosynthesis/immunology/pharmacokinetics ; Antibodies, Monoclonal/biosynthesis/immunology/pharmacokinetics ; Cell Line ; Female ; Humans ; Immunization, Passive ; Immunoglobulin G/*biosynthesis/genetics/immunology ; Immunoglobulin M/genetics ; Immunoglobulin Variable Region/*biosynthesis/genetics/immunology ; Immunoglobulin kappa-Chains/*biosynthesis/genetics/immunology ; Macromolecular Substances ; Maternal-Fetal Exchange ; Multiple Myeloma ; Pregnancy ; Rats ; Streptococcal Infections/prevention & control ; Streptococcus agalactiae/immunology ; Transfection
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  • 27
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    Structurally homologous ligand binding of integrin Mac-1 and viral glycoprotein C receptors (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-11-22
    Description: Three spatially distant surface loops were found to mediate the interaction of the coagulation protein factor X with the leukocyte integrin Mac-1. This interacting region, which by computational modeling defines a three-dimensional macromotif in the catalytic domain, was also recognized by glycoprotein C (gC), a factor X receptor expressed on herpes simplex virus (HSV)-infected endothelial cells. Peptidyl mimicry of each loop inhibited factor X binding to Mac-1 and gC, blocked monocyte generation of thrombin, and prevented monocyte adhesion to HSV-infected endothelium. These data link the ligand recognition of Mac-1 to established mechanisms of receptor-mediated vascular injury.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Altieri, D C -- Etingin, O R -- Fair, D S -- Brunck, T K -- Geltosky, J E -- Hajjar, D P -- Edgington, T S -- HL 46408/HL/NHLBI NIH HHS/ -- P01 HL 16411/HL/NHLBI NIH HHS/ -- R01 HL 43773/HL/NHLBI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1991 Nov 22;254(5035):1200-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Immunology, Scripps Research Institute, La Jolla, CA 92037.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1957171" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Binding, Competitive ; Cell Line ; Factor X/*metabolism/ultrastructure ; Humans ; In Vitro Techniques ; Ligands ; Macrophage-1 Antigen/*metabolism ; Models, Molecular ; Molecular Sequence Data ; Peptides/chemistry/metabolism ; Protein Conformation ; Viral Envelope Proteins/*metabolism
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Mechanism for regulating cell surface distribution of Na+,K(+)-ATPase in polarized epithelial cells (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-11-08
    Description: Restriction of sodium, potassium adenosine triphosphatase (Na+,K(+)-ATPase) to either the apical or basal-lateral membrane domain of polarized epithelial cells is fundamental to vectorial ion and solute transport in many tissues and organs. A restricted membrane distribution of Na+,K(+)-ATPase in Madin-Darby canine kidney (MDCK) epithelial cells was found experimentally to be generated by preferential retention of active enzyme in the basal-lateral membrane domain and selective inactivation and loss from the apical membrane domain, rather than by vectorial targeting of newly synthesized protein from the Golgi complex to the basal-lateral membrane domain. These results show how different distributions of the same subunits of Na+,K(+)-ATPase may be generated in normal polarized epithelial and in disease states.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hammerton, R W -- Krzeminski, K A -- Mays, R W -- Ryan, T A -- Wollner, D A -- Nelson, W J -- GM 35527/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1991 Nov 8;254(5033):847-50.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Cellular Physiology, Stanford University School of Medicine, CA 94305-5426.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1658934" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Binding Sites ; Cell Communication ; Cell Line ; Cell Membrane/*enzymology/physiology ; *Cell Polarity ; Dogs ; Epithelium/enzymology/physiology ; Kinetics ; Ouabain/metabolism ; Sodium-Potassium-Exchanging ATPase/*metabolism
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  • 29
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    Cell cycle-dependent coupling of the calcitonin receptor to different G proteins (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-03-01
    Description: Calcitonin is a calcium regulating peptide hormone with binding sites in kidney and bone as well as in the central nervous system. The mechanisms of signal transduction by calcitonin receptors were studied in a pig kidney cell line where the hormone was found to regulate sodium pumps. Calcitonin receptors activated the cyclic adenosine monophosphate (cAMP) or the protein kinase C (PKC) pathways. The two transduction pathways required guanosine triphosphate (GTP)-binding proteins (G proteins) (the choleratoxin sensitive Gs and the pertussis toxin sensitive Gi, respectively) and led to opposite biological responses. Moreover, selective activation of one or the other pathway was cell cycle-dependent. Therefore, calcitonin may induce different biological responses in target cells depending on their positions in the cell cycle. Such a modulation of ligand-induced responses could be of importance in rapidly growing cell populations such as during embryogenesis, growth, and tumor formation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chakraborty, M -- Chatterjee, D -- Kellokumpu, S -- Rasmussen, H -- Baron, R -- DE-04724/DE/NIDCR NIH HHS/ -- DK-19813/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1991 Mar 1;251(4997):1078-82.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Yale University School of Medicine, Department of Cell Biology, New Haven, CT 06510.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1847755" target="_blank"〉PubMed〈/a〉
    Keywords: Adenylyl Cyclases/physiology ; Animals ; Calcitonin/*physiology ; *Cell Cycle ; Cell Line ; GTP-Binding Proteins/*physiology ; Kidney ; Ouabain/metabolism ; Receptors, Calcitonin ; Receptors, Cell Surface/*physiology ; Signal Transduction ; Sodium-Potassium-Exchanging ATPase/*metabolism ; Swine
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  • 30
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    Dopamine activation of an orphan of the steroid receptor superfamily (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-06-14
    Description: The chicken ovalbumin upstream promoter transcription factor (COUP-TF) is a member of the steroid receptor superfamily and participates in the regulation of several genes. While a number of functions have been ascribed to COUP-TF, no ligand or activator molecule has been identified, and thus it is classified as one of a group of orphan receptors. Activation of COUP-TF by physiological concentrations of the neurotransmitter dopamine was observed in transient transfection assays. Treatment of transfected cells with the dopamine receptor agonist alpha-ergocryptine also activated COUP-dependent expression of a reporter gene. COUP-TF that contained a deletion in the COOH-terminal domain was not activated by these compounds. These observations suggest that dopamine may be a physiological activator of COUP-TF.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Power, R F -- Lydon, J P -- Conneely, O M -- O'Malley, B W -- New York, N.Y. -- Science. 1991 Jun 14;252(5012):1546-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology, Baylor College of Medicine, Houston, TX 77030.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2047861" target="_blank"〉PubMed〈/a〉
    Keywords: 8-Bromo Cyclic Adenosine Monophosphate/pharmacology ; Animals ; Cell Line ; Chickens ; Chimera ; Chloramphenicol O-Acetyltransferase/genetics/metabolism ; Dopamine/*pharmacology ; Ergolines/pharmacology ; Ethers, Cyclic/pharmacology ; Gene Expression/drug effects ; Okadaic Acid ; Ovalbumin/*genetics ; *Promoter Regions, Genetic ; Receptors, Steroid/drug effects/genetics/*metabolism ; Transcription Factors/*metabolism ; Transfection
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    Regulation of interleukin-2 gene enhancer activity by the T cell accessory molecule CD28 (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-01-18
    Description: The mechanism by which cell surface molecules regulate T cell production of lymphokines is poorly understood. Production of interleukin-2 (IL-2) can be regulated by signal transduction pathways distinct from those induced by the T cell antigen receptor. Stimulation of CD28, a molecule expressed on most human T cells, induced the formation of a protein complex that bound to a site on the IL-2 gene distinct from previously described binding sites and increased IL-2 enhancer activity fivefold. The CD28-responsive complex bound to the IL-2 gene between -164 and -154 base pairs from the transcription start site. The sequence of this element is similar to regions conserved in the 5' flanking regions of several other lymphokine genes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fraser, J D -- Irving, B A -- Crabtree, G R -- Weiss, A -- GM39553/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1991 Jan 18;251(4991):313-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, University of California, San Francisco 94143.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1846244" target="_blank"〉PubMed〈/a〉
    Keywords: Antigens, CD28 ; Antigens, Differentiation, T-Lymphocyte/*physiology ; Base Sequence ; Cell Line ; DNA Mutational Analysis ; *Enhancer Elements, Genetic ; Gene Expression Regulation ; Humans ; In Vitro Techniques ; Interleukin-2/*genetics ; Molecular Sequence Data ; Oligonucleotides/chemistry ; *Regulatory Sequences, Nucleic Acid ; Signal Transduction ; T-Lymphocytes/*physiology ; Transcription, Genetic
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    Prevention of apoptosis by a baculovirus gene during infection of insect cells (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-11-29
    Description: Programmed cell death is an active process of self destruction that is important in both the development and maintenance of multicellular animals. The molecular mechanisms controlling activation or suppression of programmed cell death are largely unknown. Apoptosis, a morphologically and biochemically defined type of programmed cell death commonly seen in vertebrates, was found to be initiated during baculovirus replication in insect cells. A specific viral gene product, p35, was identified as being responsible for blocking the apoptotic response. Identification of the function of this gene will allow further definition of the molecular pathways involved in the regulation of programmed cell death and may identify the role of apoptosis in invertebrate viral defense systems.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Clem, R J -- Fechheimer, M -- Miller, L K -- AI23719/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1991 Nov 29;254(5036):1388-90.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Genetics, University of Georgia, Athens 30602.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1962198" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Baculoviridae/*genetics ; Base Sequence ; *Cell Death ; Cell Line ; *Genes, Viral ; Insects ; Molecular Sequence Data ; Mutagenesis, Insertional ; Open Reading Frames ; Phenotype ; Restriction Mapping
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    Cloning of a serotonin transporter affected by antidepressants (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-10-25
    Description: A complementary DNA clone for a serotonin (5HT) transporter has been isolated from rat basophilic leukemia cells. The complementary DNA sequence predicts a 653-amino acid protein with 12 to 13 putative transmembrane domains. The 5HT transporter has significant homology to the gamma-aminobutyric acid, dopamine, and norepinephrine transporters. Uptake by CV-1 cells expressing the transporter complementary DNA resembles 5HT uptake by platelets and brain synaptosomes; it is sensitive to antidepressants, amphetamine derivatives, and cocaine.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hoffman, B J -- Mezey, E -- Brownstein, M J -- New York, N.Y. -- Science. 1991 Oct 25;254(5031):579-80.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Cell Biology, National Institute of Mental Health, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1948036" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antidepressive Agents/*pharmacology ; Base Sequence ; Carrier Proteins/drug effects/*genetics/metabolism ; Cell Line ; Cloning, Molecular ; Kinetics ; Leukemia, Basophilic, Acute ; Molecular Sequence Data ; Oligonucleotide Probes ; Rats ; Serotonin/*metabolism ; Transfection
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    Structure and functional expression of a human interleukin-8 receptor (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-09-13
    Description: Interleukin-8 (IL-8) is a member of a family of pro-inflammatory cytokines. Although the best characterized activities of IL-8 include the chemoattraction and activation of neutrophils, other members of this family have a wide range of specific actions including the chemotaxis and activation of monocytes, the selective chemotaxis of memory T cells, the inhibition of hematopoietic stem cell proliferation, and the induction of neutrophil infiltration in vivo. A complementary DNA encoding the IL-8 receptor from human neutrophils has now been isolated. The amino acid sequence shows that the receptor is a member of the superfamily of receptors that couple to guanine nucleotide binding proteins (G proteins). The sequence is 29% identical to that of receptors for the other neutrophil chemoattractants, fMet-Leu-Phe and C5a. Mammalian cells transfected with the IL-8 receptor cDNA clone bind IL-8 with high affinity and respond specifically to IL-8 by transiently mobilizing calcium. The IL-8 receptor may be part of a subfamily of related G protein-coupled receptors that transduce signals for the IL-8 family of pro-inflammatory cytokines.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Holmes, W E -- Lee, J -- Kuang, W J -- Rice, G C -- Wood, W I -- New York, N.Y. -- Science. 1991 Sep 13;253(5025):1278-80.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, Genentech, Inc., South San Francisco, CA 94080.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1840701" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Cell Line ; Cloning, Molecular ; DNA Probes ; Humans ; Interleukin-8/*metabolism ; Kinetics ; Molecular Sequence Data ; Nucleic Acid Hybridization ; Plasmids ; RNA, Messenger/genetics ; Receptors, Immunologic/*genetics/metabolism ; Receptors, Interleukin-8A ; Recombinant Proteins/metabolism ; Sequence Homology, Nucleic Acid ; Transfection
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    Enhanced motility in NIH 3T3 fibroblasts that overexpress gelsolin (1991)
    American Association for the Advancement of Science (AAAS)
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    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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    Suppression of tumorigenicity in Wilms tumor by the p15.5-p14 region of chromosome 11 (1991)
    American Association for the Advancement of Science (AAAS)
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    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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    Identification of a zinc finger protein that inhibits IL-2 gene expression (1991)
    American Association for the Advancement of Science (AAAS)
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    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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    Regulation of B cell antigen receptor signal transduction and phosphorylation by CD45 (1991)
    American Association for the Advancement of Science (AAAS)
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    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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  • 39
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    Association of B cell antigen receptor with protein tyrosine kinase Lyn (1991)
    American Association for the Advancement of Science (AAAS)
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    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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    Chimeric NGF-EGF receptors define domains responsible for neuronal differentiation (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-04-26
    Description: To determine the domains of the low-affinity nerve growth factor (NGF) receptor required for appropriate signal transduction, a series of hybrid receptors were constructed that consisted of the extracellular ligand-binding domain of the human epidermal growth factor (EGF) receptor (EGFR) fused to the transmembrane and cytoplasmic domains of the human low-affinity NGF receptor (NGFR). Transfection of these chimeric receptors into rat pheochromocytoma PC12 cells resulted in appropriate cell surface expression. Biological activity mediated by the EGF-NGF chimeric receptor was assayed by the induction of neurite outgrowth in response to EGF in stably transfected cells. Furthermore, the chimeric receptor mediated nuclear signaling, as evidenced by the specific induction of transin messenger RNA, an NGF-responsive gene. Neurite outgrowth was not observed with chimeric receptors that contained the transmembrane domain from the EGFR, suggesting that the membrane-spanning region and cytoplasmic domain of the low-affinity NGFR are necessary for signal transduction.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yan, H -- Schlessinger, J -- Chao, M V -- New York, N.Y. -- Science. 1991 Apr 26;252(5005):561-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology and Anatomy, Cornell University Medical College, New York, NY 10021.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1850551" target="_blank"〉PubMed〈/a〉
    Keywords: Adrenal Gland Neoplasms ; Animals ; Axons/drug effects/physiology/ultrastructure ; *Cell Differentiation ; Cell Line ; Chimera ; Epidermal Growth Factor/pharmacology ; Humans ; Nerve Growth Factors/pharmacology/*physiology ; Neurons/*cytology ; Pheochromocytoma ; Rats ; Receptor, Epidermal Growth Factor/genetics/*physiology ; Receptors, Cell Surface/genetics/*physiology ; Receptors, Nerve Growth Factor ; Transfection
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    Ability of the c-mos product to associate with and phosphorylate tubulin (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    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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    Intracellular signaling by 14-hydroxy-4,14-retro-retinol (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    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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    Signal transduction by interferon-alpha through arachidonic acid metabolism (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    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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    Identification of a competitive HGF antagonist encoded by an alternative transcript (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-11-29
    Description: We identified a naturally occurring hepatocyte growth factor (HGF) variant, whose predicted sequence extends only through the second kringle domain of this plasminogen-related molecule. This smaller molecule, derived from an alternative HGF transcript, lacked mitogenic activity but specifically inhibited HGF-induced mitogenesis. Cross-linking studies demonstrated that the truncated molecule competes with HGF for binding to the HGF receptor, which has been identified as the c-met protooncogene product. Thus, the same gene encodes both a growth factor and its direct antagonist.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chan, A M -- Rubin, J S -- Bottaro, D P -- Hirschfield, D W -- Chedid, M -- Aaronson, S A -- New York, N.Y. -- Science. 1991 Nov 29;254(5036):1382-5.〈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/1720571" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Blotting, Northern ; Cell Line ; Culture Media ; DNA/genetics ; DNA Replication/drug effects ; Epidermal Growth Factor/pharmacology ; Growth Substances/*genetics/isolation & purification/pharmacology ; Hepatocyte Growth Factor ; Humans ; Kinetics ; Molecular Sequence Data ; Oligodeoxyribonucleotides ; Plasmids ; Poly A/genetics/isolation & purification ; Polymerase Chain Reaction/methods ; RNA/genetics/isolation & purification ; RNA, Messenger ; Thymidine/metabolism ; *Transcription, Genetic ; Transfection
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    Generation of calcium oscillations in fibroblasts by positive feedback between calcium and IP3 (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-01-04
    Description: A wide variety of nonexcitable cells generate repetitive transient increases in cytosolic calcium ion concentration ([Ca2+]i) when stimulated with agonists that engage the phosphoinositide signalling pathway. Current theories regarding the mechanisms of oscillation disagree on whether Ca2+ inhibits or stimulates its own release from internal stores and whether inositol 1,4,5-trisphosphate (IP3) and diacylglycerol (DG) also undergo oscillations linked to the Ca2+ spikes. In this study, Ca2+ was found to stimulate its own release in REF52 fibroblasts primed by mitogens plus depolarization. However, unlike Ca2+ release in muscle and nerve cells, this amplification was insensitive to caffeine or ryanodine and required hormone receptor occupancy and functional IP3 receptors. Oscillations in [Ca2+]i were accompanied by oscillations in IP3 concentration but did not require functional protein kinase C. Therefore, the dominant feedback mechanism in this cell type appears to be Ca2+ stimulation of phospholipase C once this enzyme has been activated by hormone receptors.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Harootunian, A T -- Kao, J P -- Paranjape, S -- Tsien, R Y -- GM 31004/GM/NIGMS NIH HHS/ -- NS 27177/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1991 Jan 4;251(4989):75-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute M-047, University of California San Diego, La Jolla 92093-0647.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1986413" target="_blank"〉PubMed〈/a〉
    Keywords: Caffeine/pharmacology ; Calcium/*metabolism/pharmacology ; Cell Line ; Cytosol/metabolism ; Feedback ; Fibroblasts/drug effects/*metabolism ; Heparin/pharmacology ; Inositol 1,4,5-Trisphosphate/*metabolism ; Ionomycin/pharmacology ; *Periodicity ; Phorbol 12,13-Dibutyrate/pharmacology ; Protein Kinase C/antagonists & inhibitors/metabolism ; Ryanodine/pharmacology ; Type C Phospholipases/metabolism
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    Inhibition of entry of HIV-1 in neural cell lines by antibodies against galactosyl ceramide (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-07-19
    Description: Although the CD4 molecule is the principal cellular receptor for the human immunodeficiency virus (HIV), several CD4-negative cell lines are susceptible to infection with one or more HIV strains. These findings indicate that there are alternate modes of viral entry, perhaps involving one or more receptor molecules. Antibodies against galactosyl ceramide (galactocerebroside, or GalC) inhibited viral internalization and infection in two CD4-negative cell lines derived from the nervous system: U373-MG and SK-N-MC. Furthermore, recombinant HIV surface glycoprotein gp120 bound to GalC but not to other glycolipids. These results suggest a role for GalC or a highly related molecule in HIV entry into neural cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Harouse, J M -- Bhat, S -- Spitalnik, S L -- Laughlin, M -- Stefano, K -- Silberberg, D H -- Gonzalez-Scarano, F -- CA-45690/CA/NCI NIH HHS/ -- NS-11037/NS/NINDS NIH HHS/ -- NS-27405/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1991 Jul 19;253(5017):320-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurology, University of Pennsylvania Medical Center, Philadelphia 19104.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1857969" target="_blank"〉PubMed〈/a〉
    Keywords: *Antibodies ; Antigens, CD4/physiology ; Base Sequence ; Cell Line ; Galactosylceramides/*immunology ; Gene Products, gag/genetics ; Glioma ; HIV Envelope Protein gp120/immunology ; HIV-1/genetics/immunology/*physiology ; Humans ; Molecular Sequence Data ; Polymerase Chain Reaction ; Protein Binding ; Recombinant Proteins/immunology
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    Cell cycle regulation of histone H1 kinase activity associated with the adenoviral protein E1A (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-09-23
    Description: Several cellular proteins form stable complexes with the proteins encoded by the adenovirus early region 1A (E1A) gene in extracts derived from adenovirus infected or transformed cells. Two of the cellular proteins that bind to E1A have been identified; one, a 105-kilodalton protein (pRb), is the product of the retinoblastoma gene, and the other, a 60-kilodalton protein, is a human cyclin A. Two other proteins that bind E1A have now been shown to be related to p34cdc2. This E1A complex displayed histone H1-specific kinase activity; the kinase activity was modulated during the cell division cycle, and association of pRb with E1A apparently was not required for this activity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Giordano, A -- Lee, J H -- Scheppler, J A -- Herrmann, C -- Harlow, E -- Deuschle, U -- Beach, D -- Franza, B R Jr -- New York, N.Y. -- Science. 1991 Sep 13;253(5025):1271-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Freeman Laboratory of Cancer Cell Biology, Cold Spring Harbor Laboratory, NY 11724.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1653969" target="_blank"〉PubMed〈/a〉
    Keywords: Adenovirus Early Proteins ; Adenoviruses, Human/*genetics ; CDC2 Protein Kinase/*metabolism ; *Cell Cycle ; Cell Line ; Cell Transformation, Neoplastic ; DNA-Binding Proteins/metabolism ; HeLa Cells/cytology/physiology ; Humans ; Oncogene Proteins, Viral/genetics/*metabolism ; Protamine Kinase/*metabolism ; Protein Binding ; Recombination, Genetic
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    LAV revisited: origins of the early HIV-1 isolates from Institut Pasteur (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-05-17
    Description: Two of the first human immunodeficiency virus type-1 (HIV-1) strains isolated were authenticated by reanalyzing original cultured samples stored at the Collection Nationale de Culture des Microorganismes as well as uncultured primary material. Cloned polymerase chain reaction products were used to analyze coding sequences of the V3 loop in the gp120 glycoprotein. The original isolate HIV-1 Bru, formerly called LAV, was derived from patient BRU. HIV-1 Lai was derived from patient LAI and contaminated a HIV-1 Bru culture between 20 July and 3 August 1983. The culture became, in effect, HIV-1 Lai, identifiable by a unique motif in the V3 loop. Because of this contamination two, rather than one, HIV-1 isolates were sent to the Laboratory of Tumor Cell Biology at the National Cancer Institute on 23 September 1983. Original HIV-1 Bru was indeed present in the sample marked JBB/LAV. However the M2T-/B sample harbored HIV-1 Lai, a strain capable of growing on established cell lines. The striking similarity between HIV-1 Lai (formerly LAV-Bru) and HTLV-3B sequences remains.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wain-Hobson, S -- Vartanian, J P -- Henry, M -- Chenciner, N -- Cheynier, R -- Delassus, S -- Martins, L P -- Sala, M -- Nugeyre, M T -- Guetard, D -- New York, N.Y. -- Science. 1991 May 17;252(5008):961-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratoire de Retrovirologie Moleculaire, Institut Pasteur, Paris.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2035026" target="_blank"〉PubMed〈/a〉
    Keywords: Academies and Institutes ; Acquired Immunodeficiency Syndrome/*microbiology/pathology ; Amino Acid Sequence ; Base Sequence ; Biopsy ; Cell Line ; Cloning, Molecular ; DNA, Viral/genetics/isolation & purification ; France ; HIV Envelope Protein gp120/*genetics ; HIV-1/classification/genetics/growth & development/*isolation & purification ; Humans ; Lymph Nodes/microbiology/pathology ; Male ; Molecular Sequence Data ; National Institutes of Health (U.S.) ; Oligonucleotide Probes ; Polymerase Chain Reaction/methods ; Sequence Homology, Nucleic Acid ; United States ; Virology/methods
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    Systemic delivery of recombinant proteins by genetically modified myoblasts (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    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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    Distinct protein targets for signals acting at the c-fos serum response element (1991)
    American Association for the Advancement of Science (AAAS)
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    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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    The receptor for ciliary neurotrophic factor (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-07-05
    Description: Although neurotrophic factors were originally isolated on the basis of their ability to support the survival of neurons, these molecules are now thought to influence many aspects of the development and maintenance of the nervous system. Identifying the receptors for these neurotrophic factors should aid in identifying the cells on which these factors act and in understanding their precise mechanisms of action. A "tagged-ligand panning" procedure was used to clone a receptor for ciliary neurotrophic factor (CNTF). This receptor is expressed exclusively within the nervous system and skeletal muscle. The CNTF receptor has a structure unrelated to the receptors utilized by the nerve growth factor family of neurotrophic molecules, but instead is most homologous to the receptor for a cytokine, interleukin-6. This similarity suggestes that the CNTF receptor, like the interleukin-6 receptor, requires a second, signal-transducing component. In contrast to all known receptors, the CNTF receptor is anchored to cell membranes by a glycosyl-phosphatidylinositol linkage.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Davis, S -- Aldrich, T H -- Valenzuela, D M -- Wong, V V -- Furth, M E -- Squinto, S P -- Yancopoulos, G D -- New York, N.Y. -- Science. 1991 Jul 5;253(5015):59-63.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Regeneron Pharmaceuticals, Inc., Tarrytown, NY 10591.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1648265" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Blotting, Northern ; Cell Line ; Cloning, Molecular ; Electrophoresis, Agar Gel ; Gene Expression ; Humans ; In Vitro Techniques ; Molecular Sequence Data ; Muscles/metabolism ; Nervous System/metabolism ; Neuroblastoma/metabolism ; Rats ; Receptor, Ciliary Neurotrophic Factor ; Receptors, Cell Surface/blood/*genetics ; Sequence Homology, Nucleic Acid ; Transfection
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    Manifest destiny at the Scripps Research Institute (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-07-12
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Baskin, Y -- New York, N.Y. -- Science. 1991 Jul 12;253(5016):140-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1853198" target="_blank"〉PubMed〈/a〉
    Keywords: *Academies and Institutes ; Biology ; California ; Chemical Phenomena ; Chemistry ; Research Support as Topic
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    Regulation of phagocytosis and [Ca2+]i flux by distinct regions of an Fc receptor (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    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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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Recombinase-mediated gene activation and site-specific integration in mammalian cells (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-03-15
    Description: A binary system for gene activation and site-specific integration, based on the conditional recombination of transfected sequences mediated by the FLP recombinase from yeast, was implemented in mammalian cells. In several cell lines, FLP rapidly and precisely recombined copies of its specific target sequence to activate an otherwise silent beta-galactosidase reporter gene. Clones of marked cells were generated by excisional recombination within a chromosomally integrated copy of the silent reporter. By the reverse reaction, integration of transfected DNA was targeted to a specific chromosomal site. The results suggest that FLP could be used to mosaically activate or inactivate transgenes for analysis of vertebrate development, and to efficiently integrate transfected DNA at predetermined chromosomal locations.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉O'Gorman, S -- Fox, D T -- Wahl, G M -- New York, N.Y. -- Science. 1991 Mar 15;251(4999):1351-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Gene Expression Laboratory, Salk Institute for Biological Studies, La Jolla, CA 92037.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1900642" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Animals, Genetically Modified ; Cell Line ; DNA Nucleotidyltransferases/genetics/*metabolism ; In Vitro Techniques ; Mammals/*genetics ; *Recombination, Genetic ; Restriction Mapping ; *Transfection ; beta-Galactosidase/genetics
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    Primary structure and functional activity of a phosphatidylinositol-glycan-specific phospholipase D (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-04-19
    Description: A phosphatidylinositol-glycan-specific phospholipase D (PI-G PLD) that specifically hydrolyzes the inositol phosphate linkage in proteins anchored by phosphatidylinositol-glycans (PI-Gs) has recently been purified from human and bovine sera. The primary structure of bovine PI-G PLD has now been determined and the functional activity of the enzyme has been studied. Expression of PI-G PLD complementary DNA in COS cells produced a protein that specifically hydrolyzed the inositol phosphate linkage of the PI-G anchor. Cotransfection of PI-G PLD with a PI-G-anchored protein resulted in the secretion of the PI-G-anchored protein. The results suggest that the expression of PI-G PLD may influence the expression and location of PI-G-anchored proteins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Scallon, B J -- Fung, W J -- Tsang, T C -- Li, S -- Kado-Fong, H -- Huang, K S -- Kochan, J P -- New York, N.Y. -- Science. 1991 Apr 19;252(5004):446-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular/Cellular Biology and Biochemistry, Hoffmann-La Roche, Inc., Nutley, NJ 07110.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2017684" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Cattle ; Cell Line ; Cloning, Molecular ; DNA/genetics ; Gene Expression ; Glycosylphosphatidylinositols ; Humans ; Hydrolysis ; Molecular Sequence Data ; Peptide Fragments/chemistry ; Phosphatidylinositols/metabolism ; Phospholipase D/*chemistry/genetics/metabolism ; Polysaccharides/metabolism ; Sequence Homology, Nucleic Acid ; Transfection ; Trypsin
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    Cloning and expression of a cocaine-sensitive dopamine transporter complementary DNA (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-10-25
    Description: A rat dopamine (DA) transporter complementary DNA has been isolated with combined complementary DNA homology and expression approaches. The DA transporter is a 619-amino acid protein with 12 hydrophobic putative membrane-spanning domains and homology to the norepinephrine and gamma-aminobutyric acid transporters. The expressed complementary DNA confers transport of [3H]DA in Xenopus oocytes and in COS cells. Binding of the cocaine analog [3H]CFT ([3H]2 beta-carbomethoxy-3 beta-(4-fluorophenyl)tropane) to transfected COS cell membranes yields a pharmacological profile similar to that in striatal membranes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shimada, S -- Kitayama, S -- Lin, C L -- Patel, A -- Nanthakumar, E -- Gregor, P -- Kuhar, M -- Uhl, G -- New York, N.Y. -- Science. 1991 Oct 25;254(5031):576-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Molecular Neurobiology, National Institute on Drug Abuse, Baltimore, MD 21224.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1948034" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Carrier Proteins/drug effects/*genetics/metabolism ; Cell Line ; Cell Membrane/metabolism ; Cloning, Molecular ; Cocaine/analogs & derivatives/metabolism/*pharmacology ; Dopamine/*metabolism ; Dopamine Plasma Membrane Transport Proteins ; Female ; Kinetics ; *Membrane Glycoproteins ; *Membrane Transport Proteins ; Models, Structural ; Molecular Sequence Data ; *Nerve Tissue Proteins ; Oligodeoxyribonucleotides ; Oocytes/physiology ; Plasmids ; Polymerase Chain Reaction ; Protein Conformation ; RNA, Messenger/genetics ; Rats ; Transcription, Genetic ; Transfection ; Xenopus
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    In vivo footprinting of MHC class II genes: bare promoters in the bare lymphocyte syndrome (1991)
    American Association for the Advancement of Science (AAAS)
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    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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    Fibroblast growth factor receptor: does it have a role in the binding of herpes simplex virus? (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-07-12
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shieh, M T -- Spear, P G -- New York, N.Y. -- Science. 1991 Jul 12;253(5016):208-10.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1649495" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Line ; Cricetinae ; Fibroblast Growth Factors ; Heparitin Sulfate/metabolism ; Herpes Simplex/*metabolism ; In Vitro Techniques ; Receptors, Cell Surface/*physiology ; Receptors, Fibroblast Growth Factor ; Receptors, Virus/*physiology ; Simplexvirus/*metabolism
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    Transcriptional repression mediated by the WT1 Wilms tumor gene product (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-10-07
    Description: The wt1 gene, a putative tumor suppressor gene located at the Wilms tumor (WT) locus on chromosome 11p13, encodes a zinc finger-containing protein that binds to the same DNA sequence as EGR-1, a mitogen-inducible immediate-early gene product that activates transcription. The transcriptional regulatory potential of WT1 has not been demonstrated. In transient transfection assays, the WT1 protein functioned as a repressor of transcription when bound to the EGR-1 site. The repression function was mapped to the glutamine- and proline-rich NH2-terminus of WT1; fusion of this domain to the zinc finger region of EGR-1 converted EGR-1 into a transcriptional repressor.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Madden, S L -- Cook, D M -- Morris, J F -- Gashler, A -- Sukhatme, V P -- Rauscher, F J 3rd -- CA-0917-15/CA/NCI NIH HHS/ -- CA-23413/CA/NCI NIH HHS/ -- CA-52009/CA/NCI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1991 Sep 27;253(5027):1550-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Wistar Institute of Anatomy and Biology, Philadelphia, PA 19104.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1654597" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Cell Line ; Chromosomes, Human, Pair 11 ; DNA/genetics ; DNA-Binding Proteins/*genetics ; Gene Expression Regulation ; *Genes, Tumor Suppressor ; Humans ; Kidney Neoplasms/*genetics ; Molecular Sequence Data ; Repressor Proteins/*genetics ; *Transcription, Genetic ; Wilms Tumor/*genetics ; Zinc Fingers/*genetics
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    Viral persistence in neurons explained by lack of major histocompatibility class I expression (1991)
    American Association for the Advancement of Science (AAAS)
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    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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    Recognition by class II alloreactive T cells of processed determinants from human serum proteins (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-06-14
    Description: Alloreactive T cells recognize a complex composed of an allogeneic major histocompatibility complex (MHC) molecule and a peptide derived from the processing of nonpolymorphic proteins. A sizable fraction of MHC class II alloreactive T cells is shown to recognize peptides derived from constitutive processing of human serum proteins. One such epitope is a fragment of human serum albumin. This epitope bound selectively to the human class II molecule DRw11 and was constitutively present on antigen-presenting cells in vivo. These data indicate that, in the case of MHC class II, peptides involved in allorecognition may originate from exogenous proteins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Panina-Bordignon, P -- Corradin, G -- Roosnek, E -- Sette, A -- Lanzavecchia, A -- New York, N.Y. -- Science. 1991 Jun 14;252(5012):1548-50.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Basel Institute for Immunology, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1710827" target="_blank"〉PubMed〈/a〉
    Keywords: Antigen-Presenting Cells/*immunology ; Antigens, CD4/immunology ; Cell Line ; Clone Cells ; Epitopes/analysis/*immunology ; HLA-DR Antigens/*immunology ; HLA-DR Serological Subtypes ; Histocompatibility Antigens Class II/*immunology ; Humans ; Lymphocyte Activation ; Recombinant Proteins/immunology ; Serum Albumin/*immunology ; T-Lymphocytes/*immunology
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    Low affinity interaction of peptide-MHC complexes with T cell receptors (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-12-20
    Description: The interaction of antigen-specific T cell receptors (TCRs) with their ligands, peptides bound to molecules of the major histocompatibility complex (MHC), is central to most immune responses, yet little is known about its chemical characteristics. The binding to T cells of a labeled monoclonal antibody to the TCR was inhibited by soluble class II MHC heterodimers complexed to different peptides. Inhibition was both peptide- and TCR-specific and of low affinity, with a KD = 4 x 10(-5) to 6 x 10(-5) M, orders of magnitude weaker than comparable antibody-antigen interactions. This finding is consistent with the scanning nature of T cell recognition and suggests that antigen-independent adhesion precedes TCR engagement.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Matsui, K -- Boniface, J J -- Reay, P A -- Schild, H -- Fazekas de St Groth, B -- Davis, M M -- AI19512/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1991 Dec 20;254(5039):1788-91.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Stanford, CA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1763329" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antibodies, Monoclonal ; Antigen-Presenting Cells/immunology ; Cell Line ; Genetic Variation ; Immunoglobulin Fab Fragments/immunology ; Kinetics ; Macromolecular Substances ; *Major Histocompatibility Complex ; Models, Biological ; Molecular Sequence Data ; Peptides/immunology/*metabolism ; Protein Binding ; Receptors, Antigen, T-Cell/immunology/*physiology ; T-Lymphocytes/immunology
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    A homolog of the armadillo protein in Drosophila (plakoglobin) associated with E-cadherin (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-11-29
    Description: Three cytoplasmic proteins, called catenins, bind to the cytoplasmic tail of the epithelial cell-cell adhesion molecule E-cadherin. The complementary DNA sequence was determined for the 92-kilodalton beta catenin of Xenopus laevis. The sequence is homologous to mammalian plakoglobin, a protein of desmosomal and zonula adherens cell junctions, and to the plakoglobin homolog in Drosophila melanogaster, the product of the segment polarity gene armadillo. A monoclonal antibody to bovine plakoglobin recognizes the analogous beta catenin in the Madin-Darby canine kidney (MDCK) cell line. Armadillo plakoglobin may link E-cadherin to the underlying actin cytoskeleton at cell-cell junctions; the E-cadherin-catenin protein complex may also participate in the transmission of developmental information.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉McCrea, P D -- Turck, C W -- Gumbiner, B -- 5-F32-GM-13060/GM/NIGMS NIH HHS/ -- GM37432/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1991 Nov 29;254(5036):1359-61.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, University of California, San Francisco 94143.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1962194" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Cadherins/*genetics ; Cell Line ; Cytoskeletal Proteins/*genetics ; DNA/genetics ; Desmoplakins ; Drosophila melanogaster/*genetics ; Molecular Sequence Data ; Sequence Homology, Nucleic Acid ; *Trans-Activators ; Xenopus Proteins ; Xenopus laevis ; beta Catenin ; gamma Catenin
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    Dopaminergic and ligand-independent activation of steroid hormone receptors (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-12-13
    Description: The current view of how steroid hormone receptors affect gene transcription is that these receptors, on binding ligand, change to a state in which they can interact with chromatin and regulate transcription of target genes. Receptor activation is believed to be dependent only on this ligand-binding event. Selected steroid hormone receptors can be activated in a ligand-independent manner by a membrane receptor agonist, the neurotransmitter dopamine. In vitro, dopamine faithfully mimicked the effect of progesterone by causing a translocation of chicken progesterone receptor (cPR) from cytoplasm to nucleus. Dual activation by progesterone and dopamine was dissociable, and a serine residue in the cPR was identified that is not necessary for progesterone-dependent activation of cPR, but is essential for dopamine activation of this receptor.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Power, R F -- Mani, S K -- Codina, J -- Conneely, O M -- O'Malley, B W -- New York, N.Y. -- Science. 1991 Dec 13;254(5038):1636-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology, Baylor College of Medicine, Houston, TX 77030.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1749936" target="_blank"〉PubMed〈/a〉
    Keywords: 2,3,4,5-Tetrahydro-7,8-dihydroxy-1-phenyl-1H-3-benzazepine/pharmacology ; Adenylyl Cyclases/physiology ; Animals ; Cell Line ; Cercopithecus aethiops ; Dopamine/*pharmacology ; Epinephrine/pharmacology ; Ergolines/pharmacology ; Ethers, Cyclic/pharmacology ; Gene Expression Regulation/drug effects ; In Vitro Techniques ; Isoproterenol/pharmacology ; Ligands ; Norepinephrine/pharmacology ; Okadaic Acid ; Promoter Regions, Genetic ; Quinpirole ; Receptors, Dopamine/*physiology ; Receptors, Steroid/*physiology ; Regulatory Sequences, Nucleic Acid ; Signal Transduction ; Transcription Factors/physiology ; Transcription, Genetic/drug effects
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    At the crossroads of chemistry and immunology: catalytic antibodies (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-05-03
    Description: Immunochemistry has historically focused on the nature of antigenicity and antibody-antigen recognition. However, in the last 5 years, the field of immunochemistry has taken a new direction. With the aid of mechanistic and synthetic chemistry, the vast network of molecules and cells of the immune system has been tapped to produce antibodies with a new function--catalytic antibodies. Because antibodies can be generated that selectively bind almost any molecule of interest, this new technology offers the potential to tailor-make highly selective catalysts for applications in biology, chemistry, and medicine. In addition, catalytic antibodies provide fundamental insight into important aspects of biological catalysis, including the importance of transition-state stabilization, proximity effects, general acid and base catalysts, electrophilic and nucleophilic catalysis, and strain.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lerner, R A -- Benkovic, S J -- Schultz, P G -- New York, N.Y. -- Science. 1991 May 3;252(5006):659-67.〈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/2024118" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Antibodies/chemistry/immunology/metabolism ; Antibodies, Monoclonal/immunology/metabolism ; Antibody Specificity ; Antigens/chemistry/immunology/metabolism ; Binding Sites, Antibody ; *Catalysis ; Chemical Phenomena ; Chemistry ; Haptens ; Hydrogen-Ion Concentration ; Hydrolysis ; Metals ; Molecular Conformation ; Recombinant Proteins ; Thermodynamics ; Zinc
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 66
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    Enhancement of HIV-1 cytocidal effects in CD4+ lymphocytes by the AIDS-associated mycoplasma (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-03-01
    Description: Coinfection with Mycoplasma fermentans (incognitus strain) enhances the ability of human immunodeficiency virus type-1 (HIV-1) to induce cytopathic effects on human T lymphocytes in vitro. Syncytium formation of HIV-infected T cells was essentially eliminated in the presence of M. fermentans (incognitus strain), despite prominent cell death. However, replication and production of HIV-1 particles continued during the coinfection. Furthermore, the supernatant from cultures coinfected with HIV-1 and the mycoplasma contained a factor that inhibited the standard reverse transcriptase enzyme assay. The modification of the biological properties of HIV-1 by coinfection with mycoplasma may be involved in the pathogenesis of acquired immunodeficiency syndrome (AIDS).〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lo, S C -- Tsai, S -- Benish, J R -- Shih, J W -- Wear, D J -- Wong, D M -- New York, N.Y. -- Science. 1991 Mar 1;251(4997):1074-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Infections and Parasitic Diseases Pathology, Armed Forces Institute of Pathology, Washington, DC 20306.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1705362" target="_blank"〉PubMed〈/a〉
    Keywords: Acquired Immunodeficiency Syndrome/*microbiology ; CD4-Positive T-Lymphocytes/*microbiology ; Cell Fusion ; Cell Line ; Cytopathogenic Effect, Viral ; HIV-1/*pathogenicity ; Humans ; In Vitro Techniques ; Mycoplasma/*pathogenicity ; Mycoplasma Infections/*complications ; RNA-Directed DNA Polymerase/metabolism ; Virus Replication
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 67
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    Inhibition of HIV replication in acute and chronic infections in vitro by a Tat antagonist (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-12-20
    Description: The human immunodeficiency virus-1 (HIV-1) trans-activator Tat is an attractive target for the development of antiviral drugs because inhibition of Tat would arrest the virus at an early stage. The drug Ro 5-3335 [7-chloro-5-(2-pyrryl)-3H-1,4-benzodiazepine-2(H)-one], inhibited gene expression by HIV-1 at the level of transcriptional trans-activation by Tat. The compound did not inhibit the basal activity of the promoter. Both Tat and its target sequence TAR were required for the observed inhibitory activity. Ro 5-3335 reduced the amount of cell-associated viral RNA and antigen in acutely, as well as in chronically infected cells in vitro (median inhibition concentration 0.1 to 1 micromolar). Effective inhibition of viral replication was also observed 24 hours after cells were transfected with infectious recombinant HIV-1 DNA. The compound was active against both HIV-1 and HIV-2 and against 3'-azido-3'-deoxythymidine (AZT)-resistant clinical isolates.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hsu, M C -- Schutt, A D -- Holly, M -- Slice, L W -- Sherman, M I -- Richman, D D -- Potash, M J -- Volsky, D J -- AI 27397/AI/NIAID NIH HHS/ -- AI 27670/AI/NIAID NIH HHS/ -- AI 29164/AI/NIAID NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1991 Dec 20;254(5039):1799-802.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Virology, Hoffmann-La Roche, Nutley, NJ 07110.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1763331" target="_blank"〉PubMed〈/a〉
    Keywords: Antiviral Agents/*pharmacology ; Benzodiazepinones/*pharmacology ; Cell Line ; Gene Products, tat/*antagonists & inhibitors ; HIV Long Terminal Repeat/drug effects ; HIV-1/drug effects/genetics/*physiology ; HIV-2/drug effects/*physiology ; Humans ; Kinetics ; Promoter Regions, Genetic/drug effects ; Pyrroles/*pharmacology ; Virus Replication/*drug effects ; Zidovudine/pharmacology ; tat Gene Products, Human Immunodeficiency Virus
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 68
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    Treatment of established renal cancer by tumor cells engineered to secrete interleukin-4 (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    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
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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