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  • Articles  (175)
  • Latest Papers from Table of Contents or Articles in Press  (175)
  • Cells, Cultured  (175)
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  • Latest Papers from Table of Contents or Articles in Press  (175)
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  • 101
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    Burst firing in dopamine neurons induced by N-methyl-D-aspartate: role of electrogenic sodium pump (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-10-23
    Description: Dopamine-containing neurons of the mammalian midbrain are required for normal behavior and movements. In vivo they fire action potentials in bursts, but in vitro they discharge regularly spaced action potentials. Burst firing in vitro has now been shown to be robustly induced by the glutamate agonist N-methyl-D-aspartate (NMDA) although not by the non-NMDA agonists kainate or quisqualate. The hyperpolarization between bursts of action potentials results from electrogenic sodium ion extrusion by a ouabain-sensitive pump. This mechanism of burst generation in mammalian neurons may be important in the pathophysiology of schizophrenia and Parkinson's disease.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Johnson, S W -- Seutin, V -- North, R A -- New York, N.Y. -- Science. 1992 Oct 23;258(5082):665-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Vollum Institute, Oregon Health Sciences University, Portland 97201.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1329209" target="_blank"〉PubMed〈/a〉
    Keywords: Action Potentials/physiology ; Animals ; Cells, Cultured ; Dopamine/*physiology ; Kainic Acid/pharmacology ; N-Methylaspartate/*pharmacology ; Neurons/*drug effects/physiology ; Quisqualic Acid/pharmacology ; Rats ; Sodium/physiology ; Sodium-Potassium-Exchanging ATPase/*physiology ; Synaptic Transmission/*physiology
    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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  • 102
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    Intercellular propagation of calcium waves mediated by inositol trisphosphate (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-10-09
    Description: Two types of calcium (Ca2+) signaling-propagating intercellular Ca2+ waves of increasing intracellular Ca2+ concentration ([Ca2+]i) and nonpropagating oscillations in [Ca2+]i-co-exist in a variety of cell types. To investigate this difference in Ca2+ signaling, airway epithelial cells were loaded with heparin, an inositol 1,4,5-triphosphate (IP3) receptor antagonist, by pulsed, high-frequency electroporation. Heparin inhibited propagation of intercellular Ca2+ waves but not oscillations of [Ca2+]i. In heparin-free cells, Ca2+ waves propagated through cells displaying [Ca2+]i oscillations. Depletion of intracellular Ca2+ pools with the Ca2+-pump inhibitor thapsigargin also inhibited the propagation of Ca2+ waves. These studies demonstrate that the release of Ca2+ by IP3 is necessary for the propagation of intercellular Ca2+ waves and suggest that IP3 moves through gap junctions to communicate intercellular Ca2+ waves.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Boitano, S -- Dirksen, E R -- Sanderson, M J -- New York, N.Y. -- Science. 1992 Oct 9;258(5080):292-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Anatomy, UCLA School of Medicine, CA 90024.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1411526" target="_blank"〉PubMed〈/a〉
    Keywords: Calcium/*metabolism ; Cells, Cultured ; Chondroitin Sulfates/pharmacology ; Electric Stimulation ; Epithelium/drug effects/metabolism ; Fluorescent Dyes ; Heparin/pharmacology ; Inositol 1,4,5-Trisphosphate/pharmacology/*physiology ; Intercellular Junctions/physiology ; Respiratory System/drug effects/metabolism ; Signal Transduction/*physiology ; Terpenes/pharmacology ; Thapsigargin
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  • 103
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    CD19: lowering the threshold for antigen receptor stimulation of B lymphocytes (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-04-03
    Description: Lymphocytes must proliferate and differentiate in response to low concentrations of a vast array of antigens. The requirements of broad specificity and sensitivity conflict because the former is met by low-affinity antigen receptors, which precludes achieving the latter with high-affinity receptors. Coligation of the membrane protein CD19 with the antigen receptor of B lymphocytes decreased the threshold for antigen receptor-dependent stimulation by two orders of magnitude. B lymphocytes proliferated when approximately 100 antigen receptors per cell, 0.03 percent of the total, were coligated with CD19. The B cell resolves its dilemma by having an accessory protein that enables activation when few antigen receptors are occupied.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Carter, R H -- Fearon, D T -- AI-22833/AI/NIAID NIH HHS/ -- AI-28191/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1992 Apr 3;256(5053):105-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine, Johns Hopkins University School of Medicine, Baltimore, MD 21205.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1373518" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antibodies, Monoclonal/immunology ; Antigens, CD/genetics/*immunology ; Antigens, CD19 ; Antigens, Differentiation, B-Lymphocyte/genetics/*immunology ; B-Lymphocytes/*immunology ; Cell Line ; Cells, Cultured ; DNA Replication ; Humans ; Kinetics ; L Cells (Cell Line) ; *Lymphocyte Activation ; Mice ; Receptors, Antigen, B-Cell/*immunology ; Recombinant Proteins/immunology ; Thymidine/metabolism
    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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  • 104
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    Negative inotropic effects of cytokines on the heart mediated by nitric oxide (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-07-17
    Description: The direct effects of pro-inflammatory cytokines on the contractility of mammalian heart were studied. Tumor necrosis factor alpha, interleukin-6, and interleukin-2 inhibited contractility of isolated hamster papillary muscles in a concentration-dependent, reversible manner. The nitric oxide synthase inhibitor NG-monomethyl-L-arginine (L-NMMA) blocked these negative inotropic effects. L-Arginine reversed the inhibition by L-NMMA. Removal of the endocardial endothelium did not alter these responses. These findings demonstrate that the direct negative inotropic effect of cytokines is mediated through a myocardial nitric oxide synthase. The regulation of pro-inflammatory cytokines and myocardial nitric oxide synthase may provide new therapeutic strategies for the treatment of cardiac disease.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Finkel, M S -- Oddis, C V -- Jacob, T D -- Watkins, S C -- Hattler, B G -- Simmons, R L -- GM-37753/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1992 Jul 17;257(5068):387-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine, University of Pittsburgh School of Medicine, PA 15213.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1631560" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Arginine/analogs & derivatives/pharmacology ; Cells, Cultured ; Cricetinae ; Cytokines/*pharmacology ; Dose-Response Relationship, Drug ; Drug Interactions ; Endocardium/cytology ; Epithelium/physiology ; Interleukin-2/pharmacology ; Interleukin-6/pharmacology ; Microscopy, Electron ; Myocardial Contraction/*drug effects ; Nitric Oxide/*pharmacology ; Tumor Necrosis Factor-alpha/pharmacology ; omega-N-Methylarginine
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  • 105
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    Restoration of viral immunity in immunodeficient humans by the adoptive transfer of T cell clones (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-07-10
    Description: The adoptive transfer of antigen-specific T cells to establish immunity is an effective therapy for viral infections and tumors in animal models. The application of this approach to human disease would require the isolation and in vitro expansion of human antigen-specific T cells and evidence that such T cells persist and function in vivo after transfer. Cytomegalovirus-specific CD8+ cytotoxic T cell (CTL) clones could be isolated from bone marrow donors, propagated in vitro, and adoptively transferred to immunodeficient bone marrow transplant recipients. No toxicity developed and the clones provided persistent reconstitution of CD8+ cytomegalovirus-specific CTL responses.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Riddell, S R -- Watanabe, K S -- Goodrich, J M -- Li, C R -- Agha, M E -- Greenberg, P D -- CA18029/CA/NCI NIH HHS/ -- P01 CA018029/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1992 Jul 10;257(5067):238-41.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Fred Hutchinson Cancer Research Center, Seattle, WA 98104.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1352912" target="_blank"〉PubMed〈/a〉
    Keywords: Antigens, CD3 ; Antigens, CD8/immunology ; Antigens, Differentiation, T-Lymphocyte/immunology ; Bone Marrow Transplantation/immunology ; CD4-Positive T-Lymphocytes/immunology ; Cells, Cultured ; Cytomegalovirus Infections/*prevention & control ; Humans ; Receptors, Antigen, T-Cell/immunology ; T-Lymphocytes, Cytotoxic/*immunology ; Vaccination/*methods
    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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  • 106
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    Activation-induced ubiquitination of the T cell antigen receptor (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-08-07
    Description: The zeta subunit of the T cell antigen receptor (TCR) exists primarily as a disulfide-linked homodimer. This receptor subunit is important in TCR-mediated signal transduction and is a substrate for a TCR-activated protein tyrosine kinase. The zeta chain was found to undergo ubiquitination in response to receptor engagement. This posttranslational modification occurred in normal T cells and tumor lines. Both nonphosphorylated and phosphorylated zeta molecules were modified, and at least one other TCR subunit, CD3 delta, was also ubiquitinated after activation of the receptor. These findings suggest an expanded role for ubiquitination in transmembrane receptor function.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cenciarelli, C -- Hou, D -- Hsu, K C -- Rellahan, B L -- Wiest, D L -- Smith, H T -- Fried, V A -- Weissman, A M -- New York, N.Y. -- Science. 1992 Aug 7;257(5071):795-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Experimental Immunology Branch, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1323144" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens, CD3 ; Antigens, Differentiation, T-Lymphocyte/immunology/metabolism ; Cells, Cultured ; Hybridomas/immunology ; Lymphocyte Activation/*physiology ; Macromolecular Substances ; Mice ; Mice, Inbred C57BL ; Molecular Weight ; *Protein Processing, Post-Translational ; Receptors, Antigen, T-Cell/immunology/isolation & purification/*metabolism ; Spleen/immunology ; T-Lymphocytes/*immunology ; Ubiquitins/isolation & purification/*metabolism
    Print ISSN: 0036-8075
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  • 107
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    Inhibition of myeloid differentiation by the helix-loop-helix protein Id (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-03-27
    Description: Id is a helix-loop-helix (HLH) protein that represses activity of several basic helix-loop-helix (bHLH) proteins involved in cell type--specific transcription and cell lineage commitment. The myeloid precursor cell line 32DC13(G) expressed Id messenger RNA, which was transiently decreased when cells were induced to terminally differentiate with granulocyte--colony-stimulating factor. Concomitant with the decrease of Id messenger RNA was the appearance in nuclear extracts of DNA binding proteins that recognized a canonical E-box motif, a DNA binding site for some bHLH proteins. Constitutive expression of an Id complementary DNA in 32DC13(G) cells blocked their ability to differentiate and to induce E-box-binding activity. These results suggest that Id and, hence, bHLH proteins function in the process of myeloid differentiation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kreider, B L -- Benezra, R -- Rovera, G -- Kadesch, T -- CA 10815/CA/NCI NIH HHS/ -- CA 21124/CA/NCI NIH HHS/ -- CA 25875/CA/NCI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1992 Mar 27;255(5052):1700-2.〈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/1372755" target="_blank"〉PubMed〈/a〉
    Keywords: Cell Differentiation/*drug effects ; Cells, Cultured ; DNA-Binding Proteins/*physiology ; Gene Expression ; Granulocyte Colony-Stimulating Factor/pharmacology ; Hematopoiesis/*drug effects ; In Vitro Techniques ; Inhibitor of Differentiation Protein 1 ; Interleukin-3/pharmacology ; Macromolecular Substances ; RNA, Messenger/genetics ; *Repressor Proteins ; *Transcription Factors
    Print ISSN: 0036-8075
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  • 108
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    Yeast biology enters a surprising new phase (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-03-20
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hoffman, M -- New York, N.Y. -- Science. 1992 Mar 20;255(5051):1510-1.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1549780" target="_blank"〉PubMed〈/a〉
    Keywords: Cells, Cultured ; Nitrogen/metabolism ; Saccharomyces cerevisiae/*physiology
    Print ISSN: 0036-8075
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  • 109
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    Functional modulation of GABAA receptors by cAMP-dependent protein phosphorylation (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-07-31
    Description: gamma-Aminobutyric acidA (GABAA) receptors are ligand-gated ion channels that mediate inhibitory synaptic transmission in the central nervous system. The role of protein phosphorylation in the modulation of GABAA receptor function was examined with cells transiently transfected with GABAA receptor subunits. GABAA receptors consisting of the alpha 1 and beta 1 or the alpha 1, beta 1, and gamma 2 subunits were directly phosphorylated on the beta 1 subunit by adenosine 3',5'-monophosphate (cAMP)-dependent protein kinase (PKA). The phosphorylation decreased the amplitude of the GABA response of both receptor types and the extent of rapid desensitization of the GABAA receptor that consisted of the alpha 1 and beta 1 subunits. Site-specific mutagenesis of the serine residue phosphorylated by PKA completely eliminated the PKA phosphorylation and modulation of the GABAA receptor. In primary embryonic rat neuronal cell cultures, a similar regulation of GABAA receptors by PKA was observed. These results demonstrate that the GABAA receptor is directly modulated by protein phosphorylation and suggest that neurotransmitters or neuropeptides that regulate intracellular cAMP levels may modulate the responses of neurons to GABA and consequently have profound effects on synaptic excitability.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Moss, S J -- Smart, T G -- Blackstone, C D -- Huganir, R L -- Wellcome Trust/United Kingdom -- New York, N.Y. -- Science. 1992 Jul 31;257(5070):661-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neuroscience, Howard Hughes Medical Institute, Johns Hopkins University School of Medicine, Baltimore, MD 21205.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1323140" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Line ; Cells, Cultured ; Colforsin/pharmacology ; Cyclic AMP/*pharmacology ; Electric Conductivity ; Immunosorbent Techniques ; Kinetics ; Mice ; Mutagenesis, Site-Directed ; Neurons/drug effects/physiology ; Peptide Mapping ; Phosphorylation ; Protein Kinases/*metabolism ; Rats ; Receptors, GABA-A/genetics/*physiology ; Recombinant Proteins/physiology ; Transfection ; Zinc/pharmacology ; gamma-Aminobutyric Acid/pharmacology
    Print ISSN: 0036-8075
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  • 110
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    Prevention of programmed cell death of sympathetic neurons by the bcl-2 proto-oncogene (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-10-09
    Description: Approximately half of the neurons produced during embryogenesis normally die before adulthood. Although target-derived neurotrophic factors are known to be major determinants of programmed cell death--apoptosis--the molecular mechanisms by which trophic factors interfere with cell death regulation are largely unknown. Overexpression of the bcl-2 proto-oncogene in cultured sympathetic neurons has now been shown to prevent apoptosis normally induced by deprivation of nerve growth factor. This finding, together with the previous demonstration of bcl-2 expression in the nervous system, suggests that the Bcl-2 protein may be a major mediator of the effects of neurotrophic factors on neuronal survival.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Garcia, I -- Martinou, I -- Tsujimoto, Y -- Martinou, J C -- CA-50551/CA/NCI NIH HHS/ -- CA-51864/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1992 Oct 9;258(5080):302-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pathology, Centre Medical Universitaire, Geneva, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1411528" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Apoptosis/*genetics ; Cell Death/*genetics ; Cells, Cultured ; Ganglia, Sympathetic/cytology ; Gene Expression ; Humans ; Nerve Growth Factors/physiology ; Neurons/*physiology ; Proto-Oncogene Proteins/*genetics ; Proto-Oncogene Proteins c-bcl-2 ; Rats ; Sympathetic Nervous System/*cytology ; Transfection
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  • 111
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    Post-transcriptional regulation of early T cell development by T cell receptor signals (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-11-27
    Description: During differentiation in the thymus, immature T cells progress through an ordered sequence of developmental stages that are best characterized by variable expression of the co-receptor molecules CD4 and CD8. Crosslinking of T cell receptor (TCR) molecules on precursor thymocytes was found to block their differentiation into CD4+CD8+ cells by eliminating messenger RNA's encoding two families of developmentally important molecules: the co-receptor molecules CD4 and CD8 and the recombination activating genes 1 and 2. TCR-induced post-transcriptional regulation in early thymocytes was specific for selective messenger RNA's, required protein synthesis, and was itself developmentally regulated. These data identify a post-transcriptional mechanism that is influenced by TCR signals and that regulates early thymocyte development.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Takahama, Y -- Singer, A -- New York, N.Y. -- Science. 1992 Nov 27;258(5087):1456-62.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Experimental Immunology Branch, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1439838" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens, CD4/genetics ; Antigens, CD8/genetics ; Cell Differentiation/physiology ; Cells, Cultured ; Fetus/cytology ; Gene Rearrangement, T-Lymphocyte/genetics ; Genes, RAG-1/genetics ; Mice ; Protein Synthesis Inhibitors/pharmacology ; Protein-Tyrosine Kinases/genetics ; RNA Processing, Post-Transcriptional/physiology ; RNA, Messenger/metabolism ; Receptors, Antigen, T-Cell, alpha-beta/genetics/*physiology ; Signal Transduction/physiology ; T-Lymphocytes/*cytology/drug effects ; Tetradecanoylphorbol Acetate/pharmacology ; Thymus Gland/cytology/embryology
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  • 112
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    Serotonin-mediated endocytosis of apCAM: an early step of learning-related synaptic growth in Aplysia (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-05-01
    Description: The long-term facilitation of synaptic efficacy that is induced by serotonin in dissociated cell cultures of sensory and motor neurons of Aplysia is accompanied by the growth of new synaptic connections. This growth is associated with a down-regulation in the sensory neuron of Aplysia cell adhesion molecules (apCAMs). To examine the mechanisms of this down-regulation, thin-section electron microscopy was combined with immunolabeling by gold-conjugated monoclonal antibodies specific to apCAM. Within 1 hour, serotonin led to a 50% decrease in the density of gold-labeled complexes at the surface membrane of the sensory neuron. This down-regulation was achieved by a heterologous, protein synthesis-dependent activation of the endosomal pathway, which leads to internalization and apparent degradation of apCAM. The internalization is particularly prominent at sites where the processes of the sensory neurons contact one another and may act there to destabilize process-to-process contacts that normally inhibit growth. In turn, the endocytic activation may lead to a redistribution of membrane components to sites where new synapses form.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bailey, C H -- Chen, M -- Keller, F -- Kandel, E R -- GM32099/GM/NIGMS NIH HHS/ -- MH37134/MH/NIMH NIH HHS/ -- New York, N.Y. -- Science. 1992 May 1;256(5057):645-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for Neurobiology and Behavior, College of Physicians and Surgeons of Columbia University, New York, NY.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1585177" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Anisomycin/pharmacology ; Antibodies, Monoclonal ; Aplysia/*physiology ; Cell Adhesion Molecules/*metabolism ; Cell Membrane/metabolism/ultrastructure ; Cells, Cultured ; Coated Pits, Cell-Membrane/metabolism/ultrastructure ; Endocytosis/*drug effects ; Immunohistochemistry ; Microscopy, Electron ; Motor Neurons/physiology/ultrastructure ; Neurons, Afferent/physiology/ultrastructure ; Serotonin/*pharmacology ; Synapses/*physiology/ultrastructure ; Wheat Germ Agglutinins/metabolism
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  • 113
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    Polyamine depletion and drug-induced chromosomal damage: new results (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-11-20
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tofilon, P J -- Deen, D F -- Marton, L J -- New York, N.Y. -- Science. 1992 Nov 20;258(5086):1378.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1455236" target="_blank"〉PubMed〈/a〉
    Keywords: Carmustine/toxicity ; Cell Death ; Cells, Cultured ; *DNA Damage ; In Vitro Techniques ; Polyamines/*metabolism ; Sister Chromatid Exchange/drug effects
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  • 114
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    Inhibition of development of Kaposi's sarcoma-related lesions by a bacterial cell wall complex (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-03-13
    Description: In vitro and in vivo model systems for the study of human immunodeficiency virus (HIV)-associated Kaposi's sarcoma (KS) were used to evaluate compounds for their potential as therapeutic agents. A sulfated polysaccharide-peptidoglycan compound (SP-PG) produced by bacteria controlled the in vitro growth of acquired immunodeficiency syndrome (AIDS)-associated, KS-derived spindle-shaped cells (AIDS-KS cells) at noncytotoxic concentrations. Angiogenesis induced by AIDS-KS cells in the chicken chorioallantoic membrane assay was blocked by SP-PG, which also inhibited the vascular hyperpermeability response and the angiogenesis associated with the induction of KS-like lesions that develop after subcutaneous inoculation of AIDS-KS cells into nude mice. Suramin, pentosan polysulfate, and interferon alpha, which are currently in use for therapy of KS, were either less effective than SP-PG or much more cytotoxic, or both.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nakamura, S -- Sakurada, S -- Salahuddin, S Z -- Osada, Y -- Tanaka, N G -- Sakamoto, N -- Sekiguchi, M -- Gallo, R C -- New York, N.Y. -- Science. 1992 Mar 13;255(5050):1437-40.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Internal Medicine, University of Southern California, Los Angeles 90033.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1371891" target="_blank"〉PubMed〈/a〉
    Keywords: Acquired Immunodeficiency Syndrome/complications ; Animals ; Arthrobacter ; Arylsulfatases ; Capillary Permeability/drug effects ; Cell Division/drug effects ; Cells, Cultured ; Endothelium, Vascular/cytology/drug effects ; Fibroblasts/drug effects ; Humans ; Mice ; Mice, Inbred BALB C ; Mice, Nude ; Neoplasm Transplantation ; Neovascularization, Pathologic/*prevention & control ; *Peptidoglycan ; Polysaccharides/*pharmacology ; Sarcoma, Kaposi/etiology/*pathology ; Tumor Cells, Cultured
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    No requirement for p56lck in the antigen-stimulated clonal deletion of thymocytes (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-07-03
    Description: Activation of protein-tyrosine kinases (PTKs) is required for signal transduction during T cell activation, although the pathway used during thymic selection is unknown. An in vitro system was established in which T cell receptor transgenic thymocytes underwent clonal deletion in response to peptide antigen. The effects of two PTK-specific inhibitors, herbimycin A and genistein, on the clonal deletion of immature thymocytes and the activation of mature thymocytes were examined. Clonal deletion occurred while T cell activation was inhibited and when no p56lck activity was evident. Thus, p56lck is not required for the antigen-stimulated step of clonal deletion of immature thymocytes, and negative selection proceeds via a distinct pathway.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nakayama, K -- Loh, D Y -- New York, N.Y. -- Science. 1992 Jul 3;257(5066):94-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Medicine, Washington University School of Medicine, St. Louis, MO 63110.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1621101" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Benzoquinones ; Cells, Cultured ; Chickens ; DNA Replication ; Genistein ; Isoflavones/pharmacology ; L Cells (Cell Line) ; Lactams, Macrocyclic ; *Lymphocyte Activation/drug effects ; Lymphocyte Specific Protein Tyrosine Kinase p56(lck) ; Mice ; Mice, Transgenic ; Ovalbumin/immunology ; Protein-Tyrosine Kinases/antagonists & inhibitors/*metabolism ; Quinones/pharmacology ; Receptors, Antigen, T-Cell/*genetics/immunology ; Rifabutin/analogs & derivatives ; *Signal Transduction ; T-Lymphocyte Subsets/immunology ; T-Lymphocytes/drug effects/*immunology ; Transfection
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  • 116
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    GnRH-induced Ca2+ oscillations and rhythmic hyperpolarizations of pituitary gonadotropes (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-01-24
    Description: Secretion of gonadotropic hormones from pituitary gonadotropes in response to gonadotropin-releasing hormone (GnRH) is essential for regulation of reproductive potential. Gonadotropes from male rats exhibited an unusual form of cellular excitation that resulted from periodic membrane hyperpolarization. GnRH induced an oscillatory release of intracellular Ca2+ via a guanosine triphosphate (GTP) binding protein-coupled phosphoinositide pathway and hyperpolarized the gonadotrope periodically by opening apamin-sensitive Ca(2+)-activated K+ (SK) channels. Each hyperpolarization was terminated by firing of a few action potentials that may result from removal of inactivation from voltage-gated Na+ and Ca2+ channels.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tse, A -- Hille, B -- New York, N.Y. -- Science. 1992 Jan 24;255(5043):462-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physiology and Biophysics, University of Washington School of Medicine, Seattle 98195.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1734523" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Apamin/pharmacology ; Calcium/*metabolism ; Cells, Cultured ; GTP-Binding Proteins/physiology ; Gonadotropin-Releasing Hormone/*physiology ; In Vitro Techniques ; Inositol 1,4,5-Trisphosphate/physiology ; Membrane Potentials ; Periodicity ; Pituitary Gland, Anterior/cytology/*physiology ; Potassium Channels/physiology ; Rats
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    Identification of envelope V3 loop as the major determinant of CD4 neutralization sensitivity of HIV-1 (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-07-24
    Description: Laboratory isolates of human immunodeficiency virus type-1 (HIV-1) such as HTLV-IIIB are generally T cell line-tropic and highly sensitive to neutralization by soluble CD4 (sCD4), a potential antiviral agent that is undergoing clinical trial. However, many primary HIV-1 isolates are macrophage-tropic and sCD4-resistant. Envelope V3 loop sequences derived from primary HIV-1 isolates were sufficient to confer on HTLV-IIIB not only the tissue tropism but also the degree of sCD4 neutralization resistance characteristic of their HIV-1 strains of origin. Single amino acid changes in the V3 loop enhanced sCD4 resistance by up to tenfold. These observations suggest that the tissue tropism and sCD4 neutralization sensitivity of HIV-1 isolates are regulated by similar mechanisms.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hwang, S S -- Boyle, T J -- Lyerly, H K -- Cullen, B R -- AI28233/AI/NIAID NIH HHS/ -- AI28662/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1992 Jul 24;257(5069):535-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology and Immunology, Duke University Medical Center, Durham, NC 27710.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1636088" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antigens, CD4/*immunology ; Cell Line ; Cells, Cultured ; Gene Products, gag/*immunology ; HIV Envelope Protein gp120/*immunology ; HIV-1/*immunology/isolation & purification ; Humans ; Kinetics ; Molecular Sequence Data ; Neutralization Tests ; Proviruses/immunology ; T-Lymphocyte Subsets/*immunology ; Transfection ; Virion/immunology
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    Encoding of a homolog of the IFN-gamma receptor by myxoma virus (1992)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1992-11-20
    Description: Many poxvirus-encoded virulence factors have been identified as proteins that are secreted from infected cells. The major secreted protein (37 kilodaltons) from cells infected with myxoma virus is encoded by the M-T7 open reading frame. This protein has significant sequence similarity to the human and mouse receptors for interferon-gamma (IFN-gamma). Furthermore, the myxoma M-T7 protein specifically binds rabbit IFN-gamma and inhibits the biological activity of extracellular IFN-gamma, one of the key regulatory cytokines in the host immune response against viral infections.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Upton, C -- Mossman, K -- McFadden, G -- New York, N.Y. -- Science. 1992 Nov 20;258(5086):1369-72.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, University of Alberta, Edmonton, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1455233" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Cells, Cultured ; Cloning, Molecular ; *Genes, Viral ; In Vitro Techniques ; Interferon-gamma/metabolism ; Molecular Sequence Data ; Myxoma virus/*genetics/pathogenicity ; Protein Binding ; Rabbits ; Receptors, Interferon/*genetics ; Restriction Mapping ; Sequence Alignment ; Sequence Homology, Amino Acid ; Viral Interference ; Viral Proteins/*genetics ; Viral Structural Proteins/*genetics
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  • 119
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    A phosphorylation site in the Na+ channel required for modulation by protein kinase C (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-11-08
    Description: Voltage-gated sodium channels are responsible for generation of action potentials in excitable cells. Activation of protein kinase C slows inactivation of sodium channels and reduces peak sodium currents. Phosphorylation of a single residue, serine 1506, that is located in the conserved intracellular loop between domains III and IV and is involved in inactivation of the sodium channel, is required for both modulatory effects. Mutant sodium channels lacking this phosphorylation site have normal functional properties in unstimulated cells but do not respond to activation of protein kinase C. Phosphorylation of this conserved site in sodium channel alpha subunits may regulate electrical activity in a wide range of excitable cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉West, J W -- Numann, R -- Murphy, B J -- Scheuer, T -- Catterall, W A -- GM07270/GM/NIGMS NIH HHS/ -- NS15751/NS/NINDS NIH HHS/ -- NS25704/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1991 Nov 8;254(5033):866-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, University of Washington, Seattle 98195.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1658937" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Cell Membrane/physiology ; Cells, Cultured ; Membrane Potentials ; Models, Structural ; Molecular Sequence Data ; Phosphorylation ; Protein Conformation ; Protein Kinase C/*metabolism ; Sodium Channels/metabolism/*physiology
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  • 120
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    Function of the homeodomain protein GHF1 in pituitary cell proliferation (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-07-12
    Description: Mutations that cause pituitary dwarfism in the mouse reside in the gene encoding the transcription factor growth hormone factor 1 (GHF1 or pit1). These dwarf mice (dw and dwJ) are deficient in growth hormone (GH) and prolactin (PRL) synthesis and exhibit pituitary hypoplasia, suggesting a stem cell defect. With antisense oligonucleotide technology, a cell culture model of this genetic defect was developed. Specific inhibition of GHF1 synthesis by complementary oligonucleotides led to a marked decrease in GH and PRL expression and to a marked decrease in proliferation of somatotrophic cell lines. These results provide direct evidence that the homeodomain protein GHF1 is required not only for the establishment and maintenance of the differentiated phenotype but for cell proliferation as well.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Castrillo, J L -- Theill, L E -- Karin, M -- DK38527/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1991 Jul 12;253(5016):197-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, School of Medicine, University of California, San Diego, La Jolla 92093.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1677216" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antisense Elements (Genetics) ; Base Sequence ; *Cell Division ; Cells, Cultured ; DNA/biosynthesis ; DNA-Binding Proteins/*physiology ; Dwarfism/genetics ; Gene Expression Regulation ; *Genes, Homeobox ; Growth Hormone/genetics ; In Vitro Techniques ; Mice ; Molecular Sequence Data ; Pituitary Gland/*cytology/physiology ; Prolactin/genetics ; Transcription Factor Pit-1 ; Transcription Factors/*physiology
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    Selective activation of the B natriuretic peptide receptor by C-type natriuretic peptide (CNP) (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-04-05
    Description: The natriuretic peptides are hormones that can stimulate natriuretic, diuretic, and vasorelaxant activity in vivo, presumably through the activation of two known cell surface receptor guanylyl cyclases (ANPR-A and ANPR-B). Although atrial natriuretic peptide (ANP) and, to a lesser extent, brain natriuretic peptide (BNP) are efficient activators of the ANPR-A guanylyl cyclase, neither hormone can significantly stimulate ANPR-B. A member of this hormone family, C-type natriuretic peptide (CNP), potently and selectively activated the human ANPR-B guanylyl cyclase. CNP does not increase guanosine 3',5'-monophosphate accumulation in cells expressing human ANPR-A. The affinity of CNP for ANPR-B is 50- or 500-fold higher than ANP or BNP, respectively. This ligand-receptor pair may be involved in the regulation of fluid homeostasis by the central nervous system.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Koller, K J -- Lowe, D G -- Bennett, G L -- Minamino, N -- Kangawa, K -- Matsuo, H -- Goeddel, D V -- New York, N.Y. -- Science. 1991 Apr 5;252(5002):120-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, Genentech, Inc., South San Francisco 94080.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1672777" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Atrial Natriuretic Factor/*physiology ; Cells, Cultured ; Cercopithecus aethiops ; Cloning, Molecular ; Dose-Response Relationship, Drug ; Guanylate Cyclase/metabolism ; Humans ; Natriuretic Peptide, Brain ; Natriuretic Peptide, C-Type ; Nerve Tissue Proteins/*pharmacology ; Receptors, Atrial Natriuretic Factor ; Receptors, Cell Surface/*physiology ; Recombinant Proteins ; Signal Transduction
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    Phosphorylation of c-Src on tyrosine 527 by another protein tyrosine kinase (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-10-25
    Description: The protein tyrosine kinase activity of the cellular Src protein is negatively regulated by phosphorylation at tyrosine residue 527 (Tyr527). It has not been established whether this regulatory modification of Src is mediated by autophosphorylation or by another cellular protein kinase. The phosphorylation of a modified form of c-Src that lacks kinase activity was examined in mouse cells that do not express endogenous Src (because of the targeted disruption of both src alleles). Phosphorylation of the inactive form of Src on Tyr527 occurred to a similar extent in cells lacking endogenous Src as it did in cells expressing Src. Therefore, Tyr527 phosphorylation, and thus negative control of Src kinase activity, is mediated by another cellular protein tyrosine kinase.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Thomas, J E -- Soriano, P -- Brugge, J S -- New York, N.Y. -- Science. 1991 Oct 25;254(5031):568-71.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Microbiology, University of Pennsylvania, School of Medicine, Philadelphia 19104.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1719633" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Cells, Cultured ; Cyanogen Bromide ; Embryo, Mammalian ; Mice ; Peptide Mapping ; Phosphopeptides/isolation & purification ; Phosphorylation ; Protein-Tyrosine Kinases ; Proto-Oncogene Proteins pp60(c-src)/*metabolism ; *Tyrosine
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  • 123
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    Stimulation of protein tyrosine phosphorylation by NMDA receptor activation (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-08-23
    Description: The N-methyl-D-aspartate (NMDA) receptor, a subtype of glutamate receptors, plays a key role in synaptic plasticity in the nervous system. After NMDA receptor activation, calcium entry into the postsynaptic neuron is a critical initial event. However, the subsequent mechanisms by which the NMDA receptor signal is processed are incompletely understood. Stimulation of cultured rat hippocampal cells with glutamate resulted in the rapid and transient tyrosine phosphorylation of a 39-kilodalton protein (p39). Tyrosine phosphorylation of p39 was triggered by the NMDA receptor and required an influx of Ca2+ from the extracellular medium. Because p39 was found to be highly related or identical to the microtubule-associated protein 2 kinase, the NMDA receptor signal may be processed by a sequential activation of protein kinases.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bading, H -- Greenberg, M E -- CA 43855/CA/NCI NIH HHS/ -- NS 28829/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1991 Aug 23;253(5022):912-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology and Molecular Genetics, Harvard Medical School, Boston, MA 02115.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1715095" target="_blank"〉PubMed〈/a〉
    Keywords: 2-Amino-5-phosphonovalerate/pharmacology ; Animals ; Calcium/metabolism ; Calcium-Calmodulin-Dependent Protein Kinases ; Cells, Cultured ; Glutamates/pharmacology ; Glutamic Acid ; Hippocampus/drug effects/metabolism ; Immunoblotting ; Kinetics ; Phosphoproteins/*metabolism ; Phosphorylation ; Phosphotyrosine ; Protein Kinases/metabolism ; Rats ; Receptors, N-Methyl-D-Aspartate/*metabolism ; Tyrosine/*analogs & derivatives/metabolism
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    Regulation of transendothelial neutrophil migration by endogenous interleukin-8 (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-10-04
    Description: Movement of neutrophils from the bloodstream to inflamed tissue depends on the activation of both the neutrophil and the endothelial cell. Endothelial cells lining the postcapillary venule respond to proinflammatory mediators by expressing adhesion molecules and synthesizing a variety of neutrophil-activating factors. Endothelial cell production of a 77-amino acid variant of interleukin-8 (IL-8) was found to be a requirement for the invasion of neutrophils through a vessel wall model. IL-8 secreted by cytokine- or lipopolysaccharide-stimulated endothelial cells induced the rapid shedding of neutrophil lectin adhesion molecule-1, the up-regulation of leukocyte beta 2 integrins, and the attachment and transmigration of the neutrophils. Thus, endogenous endothelial IL-8 regulates transvenular traffic during acute inflammatory responses.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Huber, A R -- Kunkel, S L -- Todd, R F 3rd -- Weiss, S J -- CA 39064/CA/NCI NIH HHS/ -- HL 28024/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1991 Oct 4;254(5028):99-102.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Internal Medicine, University of Michigan, Ann Arbor 48109.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1718038" target="_blank"〉PubMed〈/a〉
    Keywords: Antigens, CD/metabolism ; Antigens, CD18 ; Blotting, Northern ; Cell Adhesion Molecules/metabolism ; Cell Movement ; Cells, Cultured ; Chemotaxis, Leukocyte ; E-Selectin ; Endothelium, Vascular/*physiology ; Gene Expression ; Humans ; In Vitro Techniques ; Integrins/metabolism ; Intercellular Adhesion Molecule-1 ; Interleukin-1/pharmacology ; Interleukin-8/genetics/*physiology ; Lipopolysaccharides ; Neutrophils/*physiology ; Tumor Necrosis Factor-alpha/pharmacology
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    Requirement of microfilaments in sorting of actin messenger RNA (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-09-13
    Description: Specific messenger RNAs (mRNAs) can be sequestered within distinct cellular locations, but little is known about how this is accomplished. The participation of the three major cellular filaments in the localization of actin mRNA was studied in chicken embryo fibroblasts. Movement of actin mRNA to the cell periphery and maintenance of that regionalization required intact microfilaments (composed of actin) but not microtubules or intermediate filaments. The results presented here suggest that actin-binding proteins may participate in mRNA sorting.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sundell, C L -- Singer, R H -- HD18066/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 1991 Sep 13;253(5025):1275-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology, University of Massachusetts Medical School, Worcester 01655.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1891715" target="_blank"〉PubMed〈/a〉
    Keywords: Actin Cytoskeleton/drug effects/*physiology/ultrastructure ; Actins/*genetics ; Animals ; Cells, Cultured ; Chick Embryo ; Cytochalasin D/pharmacology ; Demecolcine/pharmacology ; Fibroblasts/cytology/physiology ; RNA, Messenger/analysis/drug effects/*genetics
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    Whole animal cell sorting of Drosophila embryos (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-01-04
    Description: Use of primary culture cells has been limited by the inability to purify most types of cells, particularly cells from early developmental stages. In whole animal cell sorting (WACS), live cells derived from animals harboring a lacZ transgene are purified according to their level of beta-galactosidase expression with a fluorogenic beta-galactosidase substrate and fluorescence-activated cell sorting. With WACS, incipient posterior compartment cells that express the engrailed gene were purified from early Drosophila embryos. Neuronal precursor cells were also purified, and they differentiated into neurons with high efficiency in culture. Because there are many lacZ strains, it may be possible to purify most types of Drosophila cells. The same approach is also applicable to other organisms for which germ-line transformation is possible.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Krasnow, M A -- Cumberledge, S -- Manning, G -- Herzenberg, L A -- Nolan, G P -- CA09151/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1991 Jan 4;251(4989):81-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, Stanford University, CA 94305.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1898782" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Animals, Genetically Modified ; Cell Separation/*methods ; Cells, Cultured ; Disaccharides ; Drosophila melanogaster/*embryology ; Escherichia coli/genetics ; Flow Cytometry ; Fluorescent Dyes ; Galactosides/analysis ; Lac Operon ; Neurons/cytology ; Stem Cells/cytology
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    Peripheral selection of the T cell repertoire (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-03-08
    Description: T lymphocytes undergo selection events not only in the thymus, but also after they leave the thymus and reside in the periphery. Peripheral selection was found to be dependent on T cell receptor (TCR)-ligand interactions but to differ from thymic selection with regard to specificity and mechanism. Unlike thymic selection, peripheral selection required binding of antigen to the TCR, and it induced expansion of T cell clones. Tolerance to self antigens that are restricted to the periphery occurred through the elimination of self-reactive T cells and by the clonal anergy, which was associated with down-regulation of the alpha beta TCR and CD8.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rocha, B -- von Boehmer, H -- New York, N.Y. -- Science. 1991 Mar 8;251(4998):1225-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Unite INSERM U-25 CNRS UA-122, Hopital Necker, Paris, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1900951" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens, CD4/immunology ; Antigens, CD8 ; Antigens, Differentiation, T-Lymphocyte/immunology ; Cells, Cultured ; Down-Regulation ; Female ; Histocompatibility Antigens Class I/immunology ; Immunotherapy, Adoptive ; Male ; Mice ; Mice, Nude ; Receptors, Antigen, T-Cell/*physiology ; T-Lymphocytes/*immunology ; Thymectomy ; Thymus Gland/*immunology
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    Inhibition of PDGF beta receptor signal transduction by coexpression of a truncated receptor (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-05-10
    Description: A mutated form of the platelet-derived growth factor (PDGF) beta receptor lacking most of its cytoplasmic domain was tested for its ability to block wild-type PDGF receptor function. PDGF induced the formation of complexes consisting of wild-type and truncated receptors. Such complexes were defective in autophosphorylation. When truncated receptors were expressed in excess compared to wild-type receptors, stimulation by PDGF of receptor autophosphorylation, association of phosphatidylinositol-3 kinase with the receptor, and calcium mobilization were blocked. Thus, a truncated receptor can inactivate wild-type receptor function by forming ligand-dependent receptor complexes (probably heterodimers) that are incapable of mediating the early steps of signal transduction.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ueno, H -- Colbert, H -- Escobedo, J A -- Williams, L T -- P01 HL-43821/HL/NHLBI NIH HHS/ -- R01 HL-32898/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1991 May 10;252(5007):844-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine, University of California, San Francisco 94143.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1851331" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cells, Cultured ; Centrifugation, Density Gradient ; Cricetinae ; In Vitro Techniques ; Ligands ; Mice ; Mice, Inbred BALB C ; Phosphorylation ; Platelet-Derived Growth Factor ; Receptors, Cell Surface/*antagonists & inhibitors/physiology ; Receptors, Platelet-Derived Growth Factor ; Signal Transduction/*physiology
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    Endothelial expression of a mononuclear leukocyte adhesion molecule during atherogenesis (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-02-25
    Description: An inducible rabbit endothelial adhesion molecule that is selective for mononuclear leukocytes has been identified. This adhesion protein was expressed on the surface of activated cultured endothelium in two forms, 118 and 98 kilodaltons, the amino-terminal sequence of each being highly homologous to human VCAM-1. In dietary hypercholesterolemic and Watanabe heritable hyperlipidemic rabbit models of atherosclerosis, this adhesion molecule was found to be expressed in a localized fashion by aortic endothelium that overlies early foam cell lesions. This lesion-localized expression suggests a potential endothelium-dependent mechanism for mononuclear leukocyte recruitment during atherogenesis and may provide a molecular marker for early atherosclerosis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cybulsky, M I -- Gimbrone, M A Jr -- P01-HL-36028/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1991 Feb 15;251(4995):788-91.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pathology, Brigham and Women's Hospital, Boston, MA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1990440" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antibodies, Monoclonal ; Arteriosclerosis/etiology/*metabolism ; Cell Adhesion Molecules/*biosynthesis ; Cells, Cultured ; Diet, Atherogenic ; Endothelium, Vascular/*metabolism ; Leukocytes, Mononuclear/*physiology ; Lipopolysaccharides ; Molecular Sequence Data ; Rabbits
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    Activity-dependent synaptic competition in vitro: heterosynaptic suppression of developing synapses (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-11-15
    Description: The development and stability of synaptic connections in the nervous system are influenced by the pattern of electrical activity and the competitive interaction between the adjacent nerve terminals. To investigate this influence, a culture system of nerve and muscle cells has been developed in which a single embryonic muscle cell is coinnervated by two spinal neurons. The effect of electrical activity on the synaptic efficacy was examined after repetitive electrical stimulation was applied to one or both neurons. Brief tetanic stimulation of one neuron resulted in immediate functional suppression of the synapse made by the unstimulated neuron innervating the same muscle cell. This heterosynaptic suppression was largely absent when the tetanic stimulation was applied concurrently to both neurons. This result demonstrates that activity-dependent synaptic competition can be studied in vitro at a cellular level.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lo, Y J -- Poo, M M -- NS 22764/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1991 Nov 15;254(5034):1019-22.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Sciences, Columbia University, New York, NY 10027.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1658939" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cells, Cultured ; Electric Stimulation ; In Vitro Techniques ; Muscle Contraction ; Muscles/embryology/*innervation/physiology ; Neuromuscular Junction/embryology/*physiology ; Spinal Nerves/*embryology/physiology ; Synapses/*physiology ; Synaptic Transmission ; Xenopus laevis
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    Rel-associated pp40: an inhibitor of the rel family of transcription factors (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-09-23
    Description: The Rel-associated protein pp40 is functionally related to I kappa B, an inhibitor of the transcription factor NF-kappa B. Purified pp40 inhibits the DNA binding activity of the NF-kappa B protein complex (p50:p65 heterodimers), p50:c-Rel heteromers, and c-Rel homodimers. The sequence of the complementary DNA encoding pp40 revealed similarity to the gene encoding MAD-3, a protein with mammalian I kappa B-like activity. Protein sequencing of I kappa B purified from rabbit lung confirmed that MAD-3 encodes a protein similar to I kappa B. The sequence similarity between MAD-3 and pp40 includes a casein kinase II and consensus tyrosine phosphorylation site, as well as five repeats of a sequence found in the human erythrocyte protein ankyrin. These results suggest that rel-related transcription factors, which are capable of cytosolic to nuclear translocation, may be held in the cytosol by interaction with related cytoplasmic anchor molecules.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Davis, N -- Ghosh, S -- Simmons, D L -- Tempst, P -- Liou, H C -- Baltimore, D -- Bose, H R Jr -- CA09583/CA/NCI NIH HHS/ -- CA2616/CA/NCI NIH HHS/ -- CA33192/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1991 Sep 13;253(5025):1268-71.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology, University of Texas, Austin 78712.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1891714" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Cells, Cultured ; Chick Embryo ; Cloning, Molecular ; DNA Probes ; Molecular Sequence Data ; NF-kappa B/*antagonists & inhibitors ; Oligonucleotide Probes ; Oncogene Proteins v-rel ; Open Reading Frames ; Phosphoproteins/*genetics/metabolism ; Protein-Tyrosine Kinases/antagonists & inhibitors ; RNA, Messenger/genetics ; Retroviridae Proteins, Oncogenic/*antagonists & inhibitors ; Sequence Homology, Nucleic Acid ; Transcription Factors/*antagonists & inhibitors
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    Control of embryonic motoneuron survival in vivo by ciliary neurotrophic factor (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-03-29
    Description: During development of the nervous system, neurons in many regions are overproduced by proliferation, after which the excess cells are eliminated by cell death. The survival of only a proportion of neurons during normal development is thought to be regulated by the limited availability of neurotrophic agents. One such putative trophic agent is ciliary neurotrophic factor (CNTF), a polypeptide that promotes the survival of ciliary, sensory, and sympathetic neurons in vitro. In contrast to the results of in vitro studies, however, the daily treatment of chick embryos in vivo with purified human recombinant CNTF failed to rescue any of these cell populations from cell death, whereas CNTF did promote the in vivo survival of spinal motoneurons. Thus, CNTF may not act as a neurotrophic agent in vivo for those embryonic neurons (especially ciliary neurons) on which it acts in vitro. Rather, CNTF may be required for in vivo survival of motoneurons.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Oppenheim, R W -- Prevette, D -- Yin, Q W -- Collins, F -- MacDonald, J -- NS 20402/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1991 Mar 29;251(5001):1616-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurobiology and Anatomy, Bowman Gray School of Medicine, Wake Forest University, Winston-Salem, NC 27103.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2011743" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Survival/drug effects ; Cells, Cultured ; Chick Embryo ; Ciliary Neurotrophic Factor ; Kinetics ; Motor Neurons/*cytology/drug effects ; Nerve Growth Factors/*pharmacology ; Nerve Tissue Proteins/*pharmacology ; Recombinant Proteins/pharmacology ; Spinal Cord/cytology/embryology
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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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    Experimental therapy of human glioma by means of a genetically engineered virus mutant (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-05-10
    Description: Malignant gliomas are the most common malignant brain tumors and are almost always fatal. A thymidine kinase-negative mutant of herpes simplex virus-1 (dlsptk) that is attenuated for neurovirulence was tested as a possible treatment for gliomas. In cell culture, dlsptk killed two long-term human glioma lines and three short-term human glioma cell populations. In nude mice with implanted subcutaneous and subrenal U87 human gliomas, intraneoplastic inoculation of dlsptk caused growth inhibition. In nude mice with intracranial U87 gliomas, intraneoplastic inoculation of dlsptk prolonged survival. Genetically engineered viruses such as dlsptk merit further evaluation as novel antineoplastic agents.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Martuza, R L -- Malick, A -- Markert, J M -- Ruffner, K L -- Coen, D M -- NS24279/NS/NINDS NIH HHS/ -- R01-AI26126/AI/NIAID NIH HHS/ -- SO7RRO5381/RR/NCRR NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1991 May 10;252(5007):854-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Molecular Neurogenetics Laboratory, Harvard Medical School, Massachusetts General Hospital-East, Charlestown 02129.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1851332" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antiviral Agents/pharmacology ; Brain Neoplasms/*therapy ; Cells, Cultured ; Dose-Response Relationship, Drug ; Foscarnet ; Glioma/*therapy ; Mice ; Mice, Nude ; Mutagenesis ; Phosphonoacetic Acid/analogs & derivatives/pharmacology ; Simplexvirus/genetics/*immunology ; Thymidine Kinase/genetics ; Vidarabine/pharmacology ; Viral Vaccines/*therapeutic use
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    Participation of postsynaptic PKC in cerebellar long-term depression in culture (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-12-13
    Description: Long-term depression (LTD) in the intact cerebellum is a decrease in the efficacy of the parallel fiber-Purkinje neuron synapse induced by coactivation of climbing fiber and parallel fiber inputs. In cultured Purkinje neurons, a similar depression can be induced by iontophoretic glutamate pulses and Purkinje neuron depolarization. This form of LTD is expressed as a depression of alpha-amino-3-hydroxy-5-methyl-4- isoxazole-propionic acid (AMPA)-mediated current, and its induction is dependent on activation of metabotropic quisqualate receptors. The effect of inhibitors of protein kinase C (PKC) on LTD induction was studied. Inhibitors of PKC blocked LTD induction, while phorbol-12,13-diacetate (PDA), a PKC activator, mimicked LTD. These results suggest that PKC activation is necessary for the induction of cerebellar LTD.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Linden, D J -- Connor, J A -- New York, N.Y. -- Science. 1991 Dec 13;254(5038):1656-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurosciences, Roche Institute of Molecular Biology, Roche Research Center, Nutley, NJ 07110.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1721243" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Calcium/physiology ; Cells, Cultured ; Cerebellum/*physiology ; Enzyme Activation/drug effects ; Ibotenic Acid/analogs & derivatives/pharmacology ; In Vitro Techniques ; *Indoles ; Mice ; *Naphthalenes ; Phorbol Esters/pharmacology ; Polycyclic Compounds/pharmacology ; Protein Kinase C/antagonists & inhibitors/pharmacology/*physiology ; Purkinje Cells/*physiology ; Quisqualic Acid/pharmacology ; Receptors, AMPA ; Receptors, Neurotransmitter/physiology ; Synaptic Membranes/*physiology ; alpha-Amino-3-hydroxy-5-methyl-4-isoxazolepropionic Acid
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    The ras oncoprotein and M-phase activity (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-07-05
    Description: The endogenous mos proto-oncogene product (Mos) is required for meiotic maturation. In Xenopus oocytes, the ras oncogene product (Ras) can induce meiotic maturation and high levels of M-phase--promoting factor (MPF) independent of endogenous Mos, indicating that a parallel pathway to metaphase exists. In addition, Ras, like Mos and cytostatic factor, can arrest Xenopus embryonic cell cleavage in mitosis and maintain high levels of MPF. Thus, in the Xenopus oocyte and embryo systems Ras functions in the M phase of the cell cycle. The embryonic cleavage arrest assay is a rapid and sensitive test for Ras function.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Daar, I -- Nebreda, A R -- Yew, N -- Sass, P -- Paules, R -- Santos, E -- Wigler, M -- Vande Woude, G F -- N01-CO-74101/CO/NCI NIH HHS/ -- New York, N.Y. -- Science. 1991 Jul 5;253(5015):74-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉ABL-Basic Research Program, National Cancer Institute-Frederick Cancer Research and Development Center, MD 21701.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1829549" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cells, Cultured ; In Vitro Techniques ; Maturation-Promoting Factor/*metabolism ; Meiosis/*drug effects ; Oncogene Protein p21(ras)/*pharmacology ; Oncogene Proteins v-mos ; Oogenesis/*drug effects ; Progesterone/pharmacology ; Retroviridae Proteins, Oncogenic/pharmacology ; Xenopus laevis
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    Programmed cell death of T cells signaled by the T cell receptor and the alpha 3 domain of class I MHC (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-06-07
    Description: As well as being activated or rendered unresponsive, mature T lymphocytes can be deleted, depending on the signals received by the cell. Deletion by programmed cell death (apoptosis) is triggered if a T cell that has received a signal through its T cell receptor complex also receives a signal through the alpha 3 domain of its class I major histocompatibility complex (MHC) molecule. Such a signal can be delivered by a CD8 molecule, which recognizes the alpha 3 domain, or by an antibody to this domain. Precursors of both cytotoxic T lymphocytes (CTL's) and T helper cells are sensitive to this signal but become resistant at some point before completing differentiation into functioning CTL's or T helper cells. Because CTL's carry CD8, they can induce cell death in T cells that recognize them. This pathway may be important in both removal of autoreactive T cells and immunoregulation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sambhara, S R -- Miller, R G -- New York, N.Y. -- Science. 1991 Jun 7;252(5011):1424-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Ontario Cancer Institute, University of Toronto, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1828618" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens, CD8 ; Antigens, Differentiation, T-Lymphocyte/physiology ; Cell Survival/physiology ; Cells, Cultured ; Histocompatibility Antigens Class I/*physiology ; In Vitro Techniques ; Interleukin-2/analysis ; Lymphocyte Culture Test, Mixed ; Mice ; Receptors, Antigen, T-Cell/*physiology ; Signal Transduction ; T-Lymphocytes/*physiology ; T-Lymphocytes, Cytotoxic/physiology
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    Regulation of kainate receptors by cAMP-dependent protein kinase and phosphatases (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-09-06
    Description: In the mammalian central nervous system, receptors for excitatory amino acid neurotransmitters such as the alpha-amino-3-hydroxy-5-methyl-4- isoxazolepropionic acid (AMPA)-kainate receptor mediate a large fraction of excitatory transmission. Currents induced by activation of the AMPA-kainate receptor were potentiated by agents that specifically stimulate adenosine 3',5'-monophosphate (cAMP)-dependent protein kinase A (PKA) activity or were supported by intracellular application of the catalytic subunit of PKA by itself or in combination with cAMP. Furthermore, depression of these currents by a competitive inhibitor of PKA indicates that AMPA-kainate receptors are regulated by endogenous PKA. Endogenous protein phosphatases also regulate these receptors because an inhibitor of cellular phosphates enhanced kainate currents. Modulation of PKA and phosphatases may regulate the function of these receptors and thus contribute to synaptic plasticity in hippocampal neurons.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wang, L Y -- Salter, M W -- MacDonald, J F -- New York, N.Y. -- Science. 1991 Sep 6;253(5024):1132-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physiology, University of Toronto, Ontario, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1653455" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cells, Cultured ; Cyclic AMP/pharmacology/physiology ; Ethers, Cyclic/*pharmacology ; Fetus ; Hippocampus/*physiology ; Homeostasis ; Kainic Acid/*metabolism ; Kinetics ; Macromolecular Substances ; Membrane Potentials/drug effects ; Mice ; N-Methylaspartate/pharmacology ; Neurons/drug effects/*physiology ; Okadaic Acid ; Phosphoprotein Phosphatases/*metabolism ; Protein Kinase Inhibitors ; Protein Kinases/*metabolism ; Receptors, Kainic Acid ; Receptors, Neurotransmitter/drug effects/*physiology
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    Enhancement of the glutamate response by cAMP-dependent protein kinase in hippocampal neurons (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-09-06
    Description: Receptor channels activated by glutamate, an excitatory neurotransmitter in the mammalian brain, are involved in processes such as long-term potentiation and excitotoxicity. Studies of glutamate receptor channels expressed in cultured hippocampal pyramidal neurons reveal that these channels are subject to neuromodulatory regulation through the adenylate cyclase cascade. The whole-cell current response to glutamate and kainate [a non-NMDA (N-methyl-D-aspartate) receptor agonist] was enhanced by forskolin, an activator of adenylate cyclase. Single-channel analysis revealed that an adenosine 3',5'-monophosphate-dependent protein kinase (PKA) increases the opening frequency and the mean open time of the non-NMDA-type glutamate receptor channels. Analysis of synaptic events indicated that forskolin, acting through PKA, increased the amplitude and decay time of spontaneous excitatory postsynaptic currents.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Greengard, P -- Jen, J -- Nairn, A C -- Stevens, C F -- New York, N.Y. -- Science. 1991 Sep 6;253(5024):1135-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Molecular and Cellular Neuroscience, Rockefeller University, New York, NY 10021.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1716001" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphate/pharmacology ; Animals ; Animals, Newborn ; Cells, Cultured ; Colforsin/pharmacology ; Electric Conductivity/drug effects ; Glutamates/metabolism/*pharmacology ; Hippocampus/*physiology ; Ion Channel Gating/drug effects ; Ion Channels/drug effects/*physiology ; Kainic Acid/*pharmacology ; Kinetics ; Membrane Potentials/drug effects ; N-Methylaspartate/*pharmacology ; Neurons/drug effects/*physiology ; Protein Kinases/*metabolism ; Rats ; Receptors, Glutamate ; Receptors, Neurotransmitter/drug effects/*physiology
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    The true source of HIV? (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-05-10
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Palca, J -- New York, N.Y. -- Science. 1991 May 10;252(5007):771.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1851330" target="_blank"〉PubMed〈/a〉
    Keywords: Cells, Cultured ; HIV/*isolation & purification ; Humans ; Male ; United States ; United States Office of Research Integrity
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 141
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    Contributions of two types of calcium channels to synaptic transmission and plasticity (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-11-23
    Description: In Aplysia sensory and motor neurons in culture, the contributions of the major classes of calcium current can be selectively examined while transmitter release and its modulation are examined. A slowly inactivating, dihydropyridine-sensitive calcium current does not contribute either to normal synaptic transmission or to any of three different forms of plasticity: presynaptic inhibition, homosynaptic depression, and presynaptic facilitation. This current does contribute, however, to a fourth form of plasticity--modulation of transmitter release by tonic depolarization of the sensory neuron. By contrast, a second calcium current, which is rapidly inactivating and dihydropyridine-insensitive, contributes to release elicited by the transient depolarization of an action potential and to the other three forms of plasticity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Edmonds, B -- Klein, M -- Dale, N -- Kandel, E R -- New York, N.Y. -- Science. 1990 Nov 23;250(4984):1142-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, University College of London, United Kingdom.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2174573" target="_blank"〉PubMed〈/a〉
    Keywords: Action Potentials ; Animals ; Aplysia/*physiology ; Cadmium/pharmacology ; Calcium Channels/drug effects/*physiology ; Cells, Cultured ; Dihydropyridines/antagonists & inhibitors/pharmacology ; Electric Conductivity ; FMRFamide ; Motor Neurons/physiology ; Neuronal Plasticity/*physiology ; Neurons, Afferent/physiology ; Neuropeptides/pharmacology ; Nifedipine/pharmacology ; Serotonin/pharmacology ; Synapses/*physiology ; Synaptic Transmission/*physiology
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    The dominant W42 spotting phenotype results from a missense mutation in the c-kit receptor kinase (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-01-12
    Description: The murine white spotting locus (W) is allelic with the proto-oncogene c-kit, which encodes a transmembrane tyrosine protein kinase receptor for an unknown ligand. Mutations at the W locus affect various aspects of hematopoiesis and the proliferation and migration of primordial germ cells and melanoblasts during development to varying degrees of severity. The W42 mutation has a particularly severe effect in both the homozygous and the heterozygous states. The molecular basis of the W42 mutation was determined. The c-kit protein products in homozygous mutant mast cells were expressed normally but displayed a defective tyrosine kinase activity in vitro. Nucleotide sequence analysis of mutant complementary DNAs revealed a missense mutation that replaces aspartic acid with asparagine at position 790 in the c-kit protein product. Aspartic acid-790 is a conserved residue in all protein kinases. These results provide an explanation for the dominant nature of the W42 mutation and provide insight into the mechanism of c-kit-mediated signal transduction.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tan, J C -- Nocka, K -- Ray, P -- Traktman, P -- Besmer, P -- P01-CA-16599/CA/NCI NIH HHS/ -- R01-CA-32926/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1990 Jan 12;247(4939):209-12.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Molecular Biology Program, Sloan Kettering Institute, New York, NY 10021.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1688471" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Cells, Cultured ; DNA/genetics ; Gene Expression ; Homozygote ; Liver/analysis/cytology/embryology ; Mast Cells/metabolism ; Mice ; Molecular Sequence Data ; *Mutation ; *Phenotype ; Polymerase Chain Reaction ; Protein-Tyrosine Kinases/*genetics ; Proto-Oncogene Proteins/*genetics ; Proto-Oncogene Proteins c-kit ; RNA/analysis ; Receptors, Cell Surface/genetics ; Signal Transduction
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    "Pure" human hematopoietic progenitors: permissive action of basic fibroblast growth factor (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-09-28
    Description: Methodology has been developed that enables virtually complete purification and abundant recovery of early hematopoietic progenitors from normal human adult peripheral blood. A fraction of the pure progenitors is multipotent (generates mixed colonies) and exhibits self-renewal capacity (gives rise to blast cell colonies). This methodology provides a fundamental tool for basic and clinical studies on hematopoiesis. Optimal in vitro cloning of virtually pure progenitors requires not only the stimulatory effect of interleukin-3, granulocyte-macrophage colony-stimulating factor, and erythropoietin, but also the permissive action of basic fibroblast growth factor. These findings suggest a regulatory role for this growth factor in early hematopoiesis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gabbianelli, M -- Sargiacomo, M -- Pelosi, E -- Testa, U -- Isacchi, G -- Peschle, C -- New York, N.Y. -- Science. 1990 Sep 28;249(4976):1561-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Hematology and Oncology, Istituto Superiore di Sanita, Rome, Italy.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2218497" target="_blank"〉PubMed〈/a〉
    Keywords: Adult ; Antibodies, Monoclonal/immunology ; Cell Separation ; Cells, Cultured ; Clone Cells ; Erythropoietin/pharmacology ; Fibroblast Growth Factor 2/*pharmacology ; Granulocyte-Macrophage Colony-Stimulating Factor/pharmacology ; Hematopoietic Stem Cells/*cytology/drug effects ; Humans ; Interleukin-3/pharmacology ; Monocytes/*cytology/drug effects ; Recombinant Proteins/pharmacology
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    Recovery of mitogenic activity of a growth factor mutant with a nuclear translocation sequence (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-09-28
    Description: Heparin-binding growth factor-1 (HBGF-1) is an angiogenic polypeptide mitogen for mesoderm- and neuroectoderm-derived cells in vitro and remains biologically active after truncation of the amino-terminal domain (HBGF-1 alpha) of the HBGF-1 beta precursor. Polymerase chain reaction mutagenesis and prokaryotic expression systems were used to prepare a mutant of HBGF-1 alpha lacking a putative nuclear translocation sequence (amino acid residues 21 to 27; HBGF-1U). Although HBGF-1U retains its ability to bind to heparin, HBGF-1U fails to induce DNA synthesis and cell proliferation at concentrations sufficient to induce intracellular receptor-mediated tyrosine phosphorylation and c-fos expression. Attachment of the nuclear translocation sequence from yeast histone 2B at the amino terminus of HBGF-1U yields a chimeric polypeptide (HBGF-1U2) with mitogenic activity in vitro and indicates that nuclear translocation is important for this biological response.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Imamura, T -- Engleka, K -- Zhan, X -- Tokita, Y -- Forough, R -- Roeder, D -- Jackson, A -- Maier, J A -- Hla, T -- Maciag, T -- HL 32348/HL/NHLBI NIH HHS/ -- HL 35627/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1990 Sep 28;249(4976):1567-70.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Molecular Biology, Jerome H. Holland Laboratory for the Biomedical Sciences, American Red Cross, Rockville, MD 20855.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1699274" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Binding, Competitive ; Cattle ; Cell Division/drug effects ; Cell Line ; Cell Nucleus/metabolism ; Cells, Cultured ; DNA Replication/drug effects ; Endothelium, Vascular/drug effects/metabolism ; Fibroblast Growth Factor 1/*genetics/metabolism/pharmacology ; Kinetics ; Mice ; Mitogens/pharmacology ; Molecular Sequence Data ; *Mutation ; Oligonucleotide Probes ; Receptors, Mitogen/metabolism ; Receptors, Vascular Endothelial Growth Factor ; Recombinant Proteins/metabolism/pharmacology ; Transcription, Genetic/drug effects
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    Gerontology research comes of age (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-11-02
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gibbons, A -- New York, N.Y. -- Science. 1990 Nov 2;250(4981):622-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2237413" target="_blank"〉PubMed〈/a〉
    Keywords: Aging/*physiology ; Animals ; Cells, Cultured ; DNA Damage ; Free Radicals ; Humans ; Life Expectancy
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    Effect of phospholipase C-gamma overexpression on PDGF-induced second messengers and mitogenesis (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-05-04
    Description: Platelet-derived growth factor (PDGF) stimulates phospholipase C (PLC) activity and the phosphorylation of the gamma isozyme of PLC (PLC-gamma) in vitro and in living cells. The role of PLC-gamma in the phosphoinositide signaling pathway was addressed by examining the effect of overexpression of PLC-gamma on cellular responses to PDGF. Overexpression of PLC-gamma correlated with PDGF-induced tyrosine phosphorylation of PLC-gamma and with PDGF-induced breakdown of phosphatidylinositol 4,5-bisphosphate (PIP2). However, neither bradykinin- nor lysophosphatidic acid-induced phosphoinositide metabolism was enhanced in the transfected cells, suggesting that the G protein-coupled phosphoinositide responses to these ligands are mediated by other PLC isozymes. The enhanced PDGF-induced generation of inositol trisphosphate (IP3) did not enhance intracellular calcium signaling or influence PDGF-induced DNA synthesis. Thus, enzymes other than PLC-gamma may limit PDGF-induced calcium signaling and DNA synthesis. Alternatively, PDGF-induced calcium signaling and DNA synthesis may use biochemical pathways other than phosphoinositide metabolism for signal transduction.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Margolis, B -- Zilberstein, A -- Franks, C -- Felder, S -- Kremer, S -- Ullrich, A -- Rhee, S G -- Skorecki, K -- Schlessinger, J -- New York, N.Y. -- Science. 1990 May 4;248(4955):607-10.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Rorer Biotechnology, King of Prussia, PA 19406.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2333512" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Calcium/physiology ; Cattle ; Cell Division/*drug effects ; Cells, Cultured ; DNA Replication/drug effects ; Genetic Vectors ; Inositol Phosphates/metabolism ; Isoenzymes/biosynthesis/*genetics/metabolism ; Kinetics ; Mice ; Platelet-Derived Growth Factor/*pharmacology ; Second Messenger Systems/*drug effects ; Transfection ; Type C Phospholipases/biosynthesis/*genetics/metabolism
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    Requirement for activin A and transforming growth factor--beta 1 pro-regions in homodimer assembly (1990)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1990-03-16
    Description: Many proteins are initially synthesized as part of a large precursor. The role of the pro-region in the biosynthesis of transforming growth factor--beta 1 (TGF-beta 1) and activin A, two structurally related disulfide-linked homodimers synthesized as large precursors, was studied. Vectors that expressed either the pro-region or the mature regions of these molecules were used in complementation experiments, only when the pro-region was coexpressed with the mature region did intracellular dimerization and secretion of biologically active homodimers occur. The pro-regions of activin A and TGF-beta 1, therefore, aid the folding, disulfide bond formation, and export of their respective homodimers.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gray, A M -- Mason, A J -- New York, N.Y. -- Science. 1990 Mar 16;247(4948):1328-30.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Developmental 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/2315700" target="_blank"〉PubMed〈/a〉
    Keywords: Activins ; Amino Acid Sequence ; Cells, Cultured ; Genetic Complementation Test ; Humans ; Inhibins/*biosynthesis/ultrastructure ; Macromolecular Substances ; Molecular Sequence Data ; Protein Processing, Post-Translational ; Protein Sorting Signals/physiology ; Transfection ; Transforming Growth Factors/*biosynthesis
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    Carrel's cultures (1990)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1990-03-23
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Witkowski, J A -- New York, N.Y. -- Science. 1990 Mar 23;247(4949 Pt 1):1385-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2181660" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cells, Cultured ; Chick Embryo ; History, 20th Century ; United States
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    Evidence that beta-amyloid protein in Alzheimer's disease is not derived by normal processing (1990)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1990-04-27
    Description: The beta-amyloid protein (beta/A4), derived from a larger amyloid precursor protein (APP), is the principal component of senile plaques in Alzheimer's disease. APP is an integral membrane glycoprotein and is secreted as a carboxyl-terminal truncated molecule. APP cleavage, which is a membrane-associated event, occurred at a site located within the beta/A4 region. This suggests that an intact amyloidogenic beta/A4 fragment is not generated during normal APP catabolism. Therefore, an early event in amyloid formation may involve altered APP processing that results in the release and subsequent deposition of intact beta/A4.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sisodia, S S -- Koo, E H -- Beyreuther, K -- Unterbeck, A -- Price, D L -- AG 03359/AG/NIA NIH HHS/ -- AG 05146/AG/NIA NIH HHS/ -- AG 07914/AG/NIA NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1990 Apr 27;248(4954):492-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pathology, Johns Hopkins University School of Medicine, Baltimore, MD 21205-2181.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1691865" target="_blank"〉PubMed〈/a〉
    Keywords: Aged ; Alzheimer Disease/*metabolism ; Amyloid/genetics/*metabolism ; Amyloid beta-Peptides ; Amyloid beta-Protein Precursor ; Animals ; Cell Membrane ; Cells, Cultured ; Cloning, Molecular ; DNA, Recombinant ; Glycosylation ; Half-Life ; Humans ; Immunoblotting ; Molecular Weight ; Plasmids ; Protein Precursors/genetics/*metabolism ; *Protein Processing, Post-Translational ; Recombinant Fusion Proteins/metabolism ; Substance P/genetics ; Transfection
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    HIV-1 coat protein neurotoxicity prevented by calcium channel antagonists (1990)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1990-04-20
    Description: Coat protein gp120 from the human immunodeficiency virus type-1 (HIV-1) increased intracellular free calcium and injured rodent retinal ganglion cells and hippocampal neurons in culture. Highly purified recombinant gp120 envelope protein produced these effects in a dose-dependent fashion at picomolar concentrations. Immunoprecipitation with antibody to gp120, but not with control immunoglobulin-containing serum, depleted solutions of the viral envelope protein and also prevented both the rise in intracellular calcium and neuronal toxicity. The gp120-induced increase in intracellular calcium was abrogated by transiently lowering extracellular calcium or by adding the dihydropyridine calcium channel antagonist nimodipine (100 nM). Calcium channel antagonists also prevented gp120-induced neuronal injury. In addition, intracellular stores appeared to contribute substantially to the increase in calcium elicited by gp120. Since increases in intracellular calcium have been associated with neurotoxicity, it is possible that an injurious effect of gp120 on neurons might be related to this mechanism and that treatment with calcium channel antagonists may prove useful in mitigating HIV-1-related neuronal injury.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dreyer, E B -- Kaiser, P K -- Offermann, J T -- Lipton, S A -- EY 05477/EY/NEI NIH HHS/ -- NS 01395/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1990 Apr 20;248(4953):364-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurology, Children's Hospital, Boston, MA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2326646" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Calcium/*metabolism ; Calcium Channel Blockers/*pharmacology ; Cells, Cultured ; HIV Envelope Protein gp120/administration & dosage/antagonists & ; inhibitors/*physiology ; HIV-1/*analysis ; Hippocampus/cytology ; Neurons/*drug effects/metabolism ; Nimodipine/pharmacology ; Rats ; Recombinant Proteins/pharmacology ; Retinal Ganglion Cells/drug effects/metabolism
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    Flunarizine protects neurons from death after axotomy or NGF deprivation (1990)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1990-06-15
    Description: Systemically administered flunarizine enhanced neuronal survival in lumbar sensory ganglia in newborn rats after axotomy. Flunarizine-treated rats lost 71 percent fewer neurons than the untreated control rats at the end of 1 week. In cell culture, flunarizine at 30 to 40 microM also prevented neuronal death in nerve growth factor-dependent embryonic sensory and sympathetic neurons after the abrupt withdrawal of neurotrophic support. The drug may cause this effect by acting at an intracellular site, one distinct from its blockade of voltage-dependent calcium channels.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rich, K M -- Hollowell, J P -- HL20604/HL/NHLBI NIH HHS/ -- NS18071/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1990 Jun 15;248(4961):1419-21.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurosurgery, Washington University School of Medicine, St. Louis, Mo 63110.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2356470" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Animals, Newborn ; Cell Survival/drug effects ; Cells, Cultured ; Dose-Response Relationship, Drug ; Flunarizine/administration & dosage/*pharmacology ; Ganglia, Spinal/cytology/embryology ; Ganglia, Sympathetic/cytology/embryology ; Microscopy, Electron, Scanning ; Nerve Crush ; Nerve Growth Factors/administration & dosage/*pharmacology ; Neurons/*cytology/drug effects ; Rats ; Sciatic Nerve/physiology/surgery
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    Adhesion of human B cells to germinal centers in vitro involves VLA-4 and INCAM-110 (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-08-31
    Description: Human B lymphocytes localize and differentiate within the microenvironment of lymphoid germinal centers. A frozen section binding assay was developed for the identification of those molecules involved in the adhesive interactions between B cells and lymphoid follicles. Activated human B cells and B cell lines were found to selectively adhere to germinal centers. The VLA-4 molecule on the lymphocyte and the adhesion molecule INCAM-110, expressed on follicular dendritic cells, supported this interaction. This cellular interaction model can be used for the study of how B cells differentiate.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Freedman, A S -- Munro, J M -- Rice, G E -- Bevilacqua, M P -- Morimoto, C -- McIntyre, B W -- Rhynhart, K -- Pober, J S -- Nadler, L M -- 5T32HL07627-03/HL/NHLBI NIH HHS/ -- AR33713/AR/NIAMS NIH HHS/ -- CA40216/CA/NCI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1990 Aug 31;249(4972):1030-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Tumor Immunology, Dana-Farber Cancer Institute and Boston, MA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1697696" target="_blank"〉PubMed〈/a〉
    Keywords: Antibodies, Monoclonal ; Antigens, CD/analysis ; B-Lymphocytes/cytology/*immunology/ultrastructure ; Cell Adhesion ; Cell Adhesion Molecules/*immunology ; Cells, Cultured ; Humans ; Palatine Tonsil/cytology/immunology ; Receptors, Very Late Antigen/*immunology ; Spleen/immunology ; Vascular Cell Adhesion Molecule-1
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    cdc2 gene expression at the G1 to S transition in human T lymphocytes (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-11-09
    Description: The product of the cdc2 gene, designated p34cdc2, is a serine-threonine protein kinase that controls entry of eukaryotic cells into mitosis. Freshly isolated human T lymphocytes (G0 phase) were found to have very low amounts of p34cdc2 and cdc2 messenger RNA. Expression of cdc2 increased 18 to 24 hours after exposure of T cells to phytohemagglutinin, coincident with the G1 to S transition. Antisense oligodeoxynucleotides could reduce the increase in cdc2 expression and inhibited DNA synthesis, but had no effect on several early and mid-G1 events, including blastogenesis and expression of interleukin-2 receptors, transferrin receptors, c-myb, and c-myc. Induction of cdc2 required prior induction of c-myb and c-myc. These results suggest that cdc2 induction is part of an orderly sequence of events that occurs at the G1 to S transition in T cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Furukawa, Y -- Piwnica-Worms, H -- Ernst, T J -- Kanakura, Y -- Griffin, J D -- CA36167/CA/NCI NIH HHS/ -- CA47843/CA/NCI NIH HHS/ -- CA50767/CA/NCI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1990 Nov 9;250(4982):805-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Tumor Immunology, Dana-Farber Cancer Institute, Boston, MA 02115.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2237430" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Blotting, Northern ; CDC2 Protein Kinase/biosynthesis/*genetics ; Cells, Cultured ; DNA/biosynthesis/genetics ; Flow Cytometry ; *G1 Phase ; *Gene Expression Regulation ; Genes, Retinoblastoma ; Genes, myc ; Humans ; Lymphocyte Activation ; Molecular Sequence Data ; Phosphorylation ; Polymerase Chain Reaction ; Proto-Oncogene Proteins/genetics ; Proto-Oncogene Proteins c-myb ; RNA, Messenger/biosynthesis/genetics ; *S Phase ; T-Lymphocytes/*cytology/metabolism
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Extension of the life-span of human endothelial cells by an interleukin-1 alpha antisense oligomer (1990)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1990-09-28
    Description: The proliferative potential of human diploid endothelial cells is finite, and cellular senescence in vitro is accompanied by the failure of the endothelial cell to respond to exogenous growth factors. Senescent human endothelial cells were shown to contain high amounts of the transcript for the cytokine interleukin-1 alpha (IL-1 alpha), a potent inhibitor of endothelial cell proliferation in vitro. In contrast, transformed human endothelial cells did not contain detectable IL-1 alpha messenger RNA. Treatment of human endothelial cell populations with an antisense oligodeoxynucleotide to the human IL-1 alpha transcript prevented cell senescence and extended the proliferative life-span of the cells in vitro. Removal of the IL-1 alpha antisense oligomer resulted in the generation of the senescent phenotype and loss of proliferative potential. These data suggest that human endothelial cell senescence in vitro is a dynamic process regulated by the potential intracellular activity of IL-1 alpha.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Maier, J A -- Voulalas, P -- Roeder, D -- Maciag, T -- AG07450/AG/NIA NIH HHS/ -- HL32348/HL/NHLBI NIH HHS/ -- HL35627/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1990 Sep 28;249(4976):1570-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Molecular Biology, Jerome H. Holland, Laboratory for the Biomedical Sciences, American Red Cross, Rockville, MD 20855.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2218499" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Cell Division ; Cell Survival ; Cells, Cultured ; Endothelium, Vascular/*cytology/physiology ; Humans ; Interleukin-1/*genetics ; Kinetics ; Molecular Sequence Data ; Oligonucleotide Probes ; RNA, Antisense/*genetics
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  • 155
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    Activin-binding protein from rat ovary is follistatin (1990)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1990-02-16
    Description: Activin, a member of the transforming growth factor beta protein family, was originally isolated from gonadal fluids and stimulates the release of pituitary follicle-stimulating hormone (FSH). Activin has numerous functions in both normal and neoplastic cells. Various cells synthesize activin and have a specific binding site for this peptide. However, the molecular basis for its actions is unknown. A binding protein for activin was purified from rat ovary and was identical to follistatin, a specific inhibitor of FSH release. It is likely that the binding protein participates in the diverse regulatory actions of activin.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nakamura, T -- Takio, K -- Eto, Y -- Shibai, H -- Titani, K -- Sugino, H -- New York, N.Y. -- Science. 1990 Feb 16;247(4944):836-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Frontier Research Program, Institute of Physical and Chemical Research (RIKEN), Saitama, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2106159" target="_blank"〉PubMed〈/a〉
    Keywords: Activins ; Animals ; *Carrier Proteins ; Cells, Cultured ; Female ; Follicle Stimulating Hormone/secretion ; Inhibins/isolation & purification/*metabolism/pharmacology ; Kinetics ; Molecular Weight ; Ovary/*metabolism ; Pituitary Gland/drug effects/secretion ; Protein Binding ; Rats
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  • 156
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    Inhibition of T cell receptor expression and function in immature CD4+CD8+ cells by CD4 (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-09-28
    Description: Most immature CD4+CD8+ thymocytes express only a small number of T cell receptor (TCR) molecules on their surface, and the TCR molecules they do express are only marginally capable of transducing intracellular signals. TCR expression and function was not intrinsically low in immature CD4+CD8+ thymocytes, but was found to be actively inhibited by CD4-mediated signals. Indeed, release of CD4+CD8+ thymocytes from CD4-mediated signals resulted in significant increases in both TCR expression and signaling function. These results suggest that, in CD4+CD8+ cells developing in the thymus, increased TCR expression and function requires release from CD4-mediated inhibition.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nakayama, T -- June, C H -- Munitz, T I -- Sheard, M -- McCarthy, S A -- Sharrow, S O -- Samelson, L E -- Singer, A -- New York, N.Y. -- Science. 1990 Sep 28;249(4976):1558-61.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Experimental Immunology Branch, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2120773" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antibodies, Monoclonal/immunology ; Antigens, CD4/*immunology ; Antigens, CD8 ; Antigens, Differentiation, T-Lymphocyte/*immunology ; Cell Membrane/immunology ; Cells, Cultured ; Histocompatibility Antigens Class II/immunology ; Mice ; Mice, Inbred C57BL ; Receptors, Antigen, T-Cell/biosynthesis/*physiology ; T-Lymphocytes/*immunology
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Glutamate induces calcium waves in cultured astrocytes: long-range glial signaling (1990)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1990-01-26
    Description: The finding that astrocytes possess glutamate-sensitive ion channels hinted at a previously unrecognized signaling role for these cells. Now it is reported that cultured hippocampal astrocytes can respond to glutamate with a prompt and oscillatory elevation of cytoplasmic free calcium, visible through use of the fluorescent calcium indicator fluo-3. Two types of glutamate receptor--one preferring quisqualate and releasing calcium from intracellular stores and the other preferring kainate and promoting surface-membrane calcium influx--appear to be involved. Moreover, glutamate-induced increases in cytoplasmic free calcium frequently propagate as waves within the cytoplasm of individual astrocytes and between adjacent astrocytes in confluent cultures. These propagating waves of calcium suggest that networks of astrocytes may constitute a long-range signaling system within the brain.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cornell-Bell, A H -- Finkbeiner, S M -- Cooper, M S -- Smith, S J -- GM 07205/GM/NIGMS NIH HHS/ -- NS-12961-14/NS/NINDS NIH HHS/ -- NS16671-09/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1990 Jan 26;247(4941):470-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Section of Molecular Neurobiology, Howard Hughes Medical Institute, New Haven, CT.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1967852" target="_blank"〉PubMed〈/a〉
    Keywords: Aniline Compounds ; Astrocytes/drug effects/*metabolism ; Calcium/*metabolism ; Cells, Cultured ; Cytoplasm/metabolism ; Fluorescent Dyes ; Glutamates/*pharmacology ; Glutamic Acid ; Hippocampus/cytology ; Intercellular Junctions/metabolism ; Kainic Acid/metabolism/pharmacology ; Oxadiazoles/metabolism/pharmacology ; Periodicity ; Quisqualic Acid ; Receptors, Glutamate ; Receptors, Neurotransmitter/physiology ; Xanthenes
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    Binding of GAP to activated PDGF receptors (1990)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1990-03-30
    Description: The ras proto-oncogene products appear to relay intracellular signals via the Ras guanosine triphosphatase (GTPase) activator protein, GAP. In dog epithelial cells expressing human platelet-derived growth factor (PDGF) receptors, binding of PDGF caused approximately one-tenth of the total GAP molecules to complex with the receptor. Studies with mutant PDGF receptors showed that maximum association required both receptor kinase activity and phosphorylatable tyrosine residues at both the identified sites of receptor autophosphorylation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kazlauskas, A -- Ellis, C -- Pawson, T -- Cooper, J A -- CA-28151/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1990 Mar 30;247(4950):1578-81.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Fred Hutchinson Cancer Research Center, Seattle, WA 98104.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2157284" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cells, Cultured ; Electrophoresis, Gel, Two-Dimensional ; Electrophoresis, Polyacrylamide Gel ; GTP Phosphohydrolases/metabolism ; GTPase-Activating Proteins ; Humans ; Immunoblotting ; Oncogene Protein p21(ras)/metabolism ; Peptide Mapping ; Phosphopeptides/analysis ; Phosphorylation ; Platelet-Derived Growth Factor/*metabolism ; Precipitin Tests ; Protein Kinases/analysis ; Proteins/*metabolism ; Receptors, Cell Surface/*metabolism ; Receptors, Platelet-Derived Growth Factor ; Tyrosine/metabolism ; ras GTPase-Activating Proteins
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    The high culture of neuroscience (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-10-12
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Barinaga, M -- New York, N.Y. -- Science. 1990 Oct 12;250(4978):206-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2218524" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cells, Cultured ; Culture Techniques/methods ; Neurons/cytology/*physiology
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    A muted victory for the biotech industry (1990)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1990-07-20
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Barinaga, M -- New York, N.Y. -- Science. 1990 Jul 20;249(4966):239.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2374922" target="_blank"〉PubMed〈/a〉
    Keywords: Biotechnology/*legislation & jurisprudence ; California ; Cells, Cultured ; Humans ; Informed Consent/*legislation & jurisprudence ; Research
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  • 161
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    Calcium mobilization and exocytosis after one mechanical stretch of lung epithelial cells (1990)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1990-11-30
    Description: Deep inflation of the lung stimulates surfactant secretion by unknown mechanisms. The hypothesis that mechanical distension directly stimulates type II cells to secrete surfactant was tested by stretching type II cells cultured on silastic membranes. The intracellular Ca2+ concentration was measured in single cells, before and after stretching. A single stretch of alveolar type II cells caused a transient (less than 60 seconds) increase in cytosolic Ca2+ followed by a sustained (15 to 30 minutes) stimulation of surfactant secretion. Both Ca2+ mobilization and exocytosis exhibited dose-dependence to the magnitude of the stretch-stimulus. Thus, mechanical factors can trigger complex cellular events in nonneuron, nonmuscle cells and may be involved in regulating normal lung functions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wirtz, H R -- Dobbs, L G -- HL-24075/HL/NHLBI NIH HHS/ -- HL-34356/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1990 Nov 30;250(4985):1266-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cardiovascular Research Institute, University of California, San Francisco 94143-0130.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2173861" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Biomechanical Phenomena ; Calcium/*metabolism ; Cells, Cultured ; Cyclic AMP/metabolism ; Epithelium/physiology ; *Exocytosis ; Kinetics ; Phosphatidylcholines/secretion ; Proteolipids/pharmacology ; Pulmonary Alveoli/*physiology ; Pulmonary Surfactant-Associated Proteins ; Pulmonary Surfactants/pharmacology/secretion ; Rats ; Surface Properties ; Tetradecanoylphorbol Acetate/pharmacology
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  • 162
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    Differential phosphorylation of c-Abl in cell cycle determined by cdc2 kinase and phosphatase activity (1990)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1990-04-13
    Description: The product of the c-abl proto-oncogene (c-Abl) is phosphorylated on three sites during interphase and seven additional sites during mitosis. Two interphase and all mitotic c-Abl sites are phosphorylated by cdc2 kinase isolated from either interphase or mitotic cells, with the mitotic cdc2 having an 11-fold higher activity. Inhibition of phosphatases with okadaic acid in interphase cells leads to the phosphorylation of c-Abl mitotic sites, indicating that those sites are preferentially dephosphorylated during interphase. The differential phosphorylation of c-Abl in the cell cycle is therefore determined by an equilibrium between cdc2 kinase and protein phosphatase activities. Treatment of interphase cells with okadaic acid leads to a rounded morphology similar to that observed during mitosis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kipreos, E T -- Wang, J Y -- CA43054/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1990 Apr 13;248(4952):217-20.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, University of California, San Diego, La Jolla 92093.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2183353" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; CDC2 Protein Kinase ; *Cell Cycle ; Cells, Cultured ; Ethers, Cyclic/pharmacology ; Interphase/drug effects ; Mice ; Mice, Inbred Strains ; Molecular Sequence Data ; Molecular Weight ; Okadaic Acid ; Peptide Fragments/isolation & purification ; Peptide Mapping ; Phosphoproteins/*metabolism ; Phosphorylation ; Protein-Tyrosine Kinases/*metabolism ; Proto-Oncogene Proteins/isolation & purification/*metabolism ; Proto-Oncogene Proteins c-abl
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    Evidence that the head of kinesin is sufficient for force generation and motility in vitro (1990)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1990-07-06
    Description: Kinesin is a mechanochemical protein that converts the chemical energy in adenosine triphosphate into mechanical force for movement of cellular components along microtubules. The regions of the kinesin molecule responsible for generating movement were determined by studying the heavy chain of Drosophila kinesin, and its truncated forms, expressed in Escherichia coli. The results demonstrate that (i) kinesin heavy chain alone, without the light chains and other eukaryotic factors, is able to induce microtubule movement in vitro, and (ii) a fragment likely to contain only the kinesin head is also capable of inducing microtubule motility. Thus, the amino-terminal 450 amino acids of kinesin contain all the basic elements needed to convert chemical energy into mechanical force.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yang, J T -- Saxton, W M -- Stewart, R J -- Raff, E C -- Goldstein, L S -- GM35252/GM/NIGMS NIH HHS/ -- HD16739/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 1990 Jul 6;249(4964):42-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cellular and Developmental Biology, Harvard University, Cambridge, MA 02138.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2142332" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphatases/biosynthesis/genetics/*physiology ; Amino Acid Sequence ; Animals ; Base Sequence ; Cells, Cultured ; Drosophila ; Escherichia coli/genetics/metabolism ; Kinesin ; Male ; Microtubule Proteins/biosynthesis/genetics/*physiology ; Microtubules/*physiology ; Molecular Sequence Data ; Movement ; Peptide Fragments/biosynthesis/genetics/*physiology ; Plasmids ; Recombinant Proteins/biosynthesis/genetics/physiology ; Sea Urchins ; Spermatozoa/physiology
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  • 164
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    Neurotrophic and neurotoxic effects of amyloid beta protein: reversal by tachykinin neuropeptides (1990)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1990-10-12
    Description: The amyloid beta protein is deposited in the brains of patients with Alzheimer's disease but its pathogenic role is unknown. In culture, the amyloid beta protein was neurotrophic to undifferentiated hippocampal neurons at low concentrations and neurotoxic to mature neurons at higher concentrations. In differentiated neurons, amyloid beta protein caused dendritic and axonal retraction followed by neuronal death. A portion of the amyloid beta protein (amino acids 25 to 35) mediated both the trophic and toxic effects and was homologous to the tachykinin neuropeptide family. The effects of the amyloid beta protein were mimicked by tachykinin antagonists and completely reversed by specific tachykinin agonists. Thus, the amyloid beta protein could function as a neurotrophic factor for differentiating neurons, but at high concentrations in mature neurons, as in Alzheimer's disease, could cause neuronal degeneration.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yankner, B A -- Duffy, L K -- Kirschner, D A -- AG08572/AG/NIA NIH HHS/ -- NS01240/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1990 Oct 12;250(4978):279-82.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurology, Harvard Medical School, Boston, MA 02115.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2218531" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Amyloid beta-Peptides/antagonists & inhibitors/*pharmacology ; Animals ; Cells, Cultured ; Embryo, Mammalian ; Hippocampus/cytology ; Molecular Sequence Data ; Neurons/*cytology/drug effects ; *Neurotoxins ; Peptide Fragments/pharmacology ; Rats ; Tachykinins/*pharmacology
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  • 165
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    In vitro reconstruction of the respiratory central pattern generator of the mollusk Lymnaea (1990)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1990-10-12
    Description: Most rhythmic behaviors such as respiration, locomotion, and feeding are under the control of networks of neurons in the central nervous system known as central pattern generators (CPGs). The respiratory rhythm of the pond snail Lymnaea stagnalis is a relatively simple, CPG-based behavior for which the underlying neural elements have been identified. A three-neuron network capable of generating the respiratory rhythm of this air-breathing mollusk has been reconstructed in culture. The intrinsic and network properties of this neural ensemble have been studied, and the mechanism of postinhibitory rebound excitation was found to be important for the rhythm generation. This in vitro model system enables a better understanding of the neural basis of rhythm generation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Syed, N I -- Bulloch, A G -- Lukowiak, K -- New York, N.Y. -- Science. 1990 Oct 12;250(4978):282-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Neuroscience Research Group, University of Calgary, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2218532" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cells, Cultured ; Dopamine/physiology ; Evoked Potentials ; Ganglia/cytology/physiology ; Interneurons/physiology ; Lymnaea/*physiology ; Membrane Potentials ; Models, Biological ; *Oxygen Consumption ; Synapses/physiology
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    Regulation of proteolysis at the neutrophil-substrate interface by secretory leukoprotease inhibitor (1990)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1990-07-13
    Description: Human neutrophils can initiate the rapid degradation of extracellular matrix macromolecules by localizing the destructive process to sites of cell-substrate contact. Although plasma and its filtrates contain multiple proteinase inhibitors, these inhibitors did not prevent neutrophils from attacking either underlying fibronectin or elastin. However, subjacent substrates could be protected from neutrophils by recombinant secretory leukoprotease inhibitor, a structurally unique serine proteinase inhibitor whose natural counterpart is normally confined to human mucous secretions. The identification of this extravascular proteinase inhibitor as a potent regulator of subjacent proteolysis could lead to the development of a new class of anti-inflammatory therapeutics.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rice, W G -- Weiss, S J -- AI 21301/AI/NIAID NIH HHS/ -- HL 28024/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1990 Jul 13;249(4965):178-81.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Internal Medicine, Simpson Memorial Research Institute, University of Michigan, Ann Arbor 48109.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2371565" target="_blank"〉PubMed〈/a〉
    Keywords: Cell Adhesion ; Cells, Cultured ; Elastin/metabolism ; Extracellular Matrix/*metabolism ; Fibronectins/metabolism ; Humans ; Neutrophils/*metabolism ; Proteinase Inhibitory Proteins, Secretory ; *Proteins ; Recombinant Proteins/metabolism ; Serine Proteinase Inhibitors/*metabolism ; Solubility
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  • 167
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    Endothelin stimulation of cytosolic calcium and gonadotropin secretion in anterior pituitary cells (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-06-29
    Description: The presence of endothelin, a vasoconstrictor peptide, in the hypothalamus and posterior pituitary suggests that it also regulates neural and other nonvascular target cells. In pituitary gonadotrophs, low doses of endothelin evoked oscillations in the intracellular calcium concentration, and high doses induced a biphasic calcium response. Mobilization of intracellular calcium predominated during the spike phase of the calcium response to endothelin, whereas calcium entry through dihydropyridine-sensitive channels contributed to both the spike and plateau phases of the calcium response. Endothelin was a potent as hypothalamic gonadotropin-releasing hormone (GnRH) in stimulation of gonadotropin release in perifused pituitary cells. Endothelin bound specifically to pituitary cells with a dissociation constant of 70 picomolar, and induced rapid formation of inositol trisphosphate and diacyglycerol. Although intracellular calcium concentration and gonadotropin secretory responses to endothelin were independent to the GnRH receptor, endothelin and GnRH appeared to have a common signal transduction mechanism. These observations suggest that endothelin can act as a neuropeptide to regulate anterior pituitary function.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stojilkovic, S S -- Merelli, F -- Iida, T -- Krsmanovic, L Z -- Catt, K J -- New York, N.Y. -- Science. 1990 Jun 29;248(4963):1663-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Endocrinology and Reproduction Research Branch, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2163546" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Calcium/*metabolism ; Cells, Cultured ; Cytosol/metabolism ; Endothelins ; Endothelium, Vascular ; Female ; Follicle Stimulating Hormone/*secretion ; Gonadotropin-Releasing Hormone/pharmacology ; Kinetics ; Luteinizing Hormone/*secretion ; Male ; Nifedipine/pharmacology ; Orchiectomy ; Peptides/metabolism/*pharmacology ; Pituitary Gland, Anterior/drug effects/*metabolism/secretion ; Rats ; Rats, Inbred Strains ; Receptors, Cell Surface/metabolism ; Receptors, Endothelin ; Reference Values
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 168
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    PDGF-induced activation of phospholipase C is not required for induction of DNA synthesis (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-06-29
    Description: Platelet-derived growth factor (PDGF) induction of DNA synthesis is believed to involve activation of phospholipase C (PLC) and subsequent accumulation of inositol 1,4,5-triphosphate [I(1,4,5)P3], increase in intracellular Ca2+, activation of protein kinase C (PKC), and receptor down regulation. Generation of these events is triggered by the tyrosine protein kinase (TPK) activity of the PDGF receptor. The TPK inhibitor genistein blocked PDGF induction of these events, including DNA synthesis, with the exception of receptor down regulation. PDGF-induced phosphotyrosine phosphorylations, including receptor autophosphorylation, were inhibited by genistein. Removal of genistein and PDGF resulted in DNA synthesis without the occurrence of PLC activation. These findings indicate that these early events, with the exception of receptor down regulation, are not necessary for PDGF-induced DNA synthesis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hill, T D -- Dean, N M -- Mordan, L J -- Lau, A F -- Kanemitsu, M Y -- Boynton, A L -- CA 2942/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1990 Jun 29;248(4963):1660-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cancer Research Center of Hawaii, University of Hawaii, Honolulu 96813.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2163545" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Calcium/metabolism ; Cells, Cultured ; Chlorides/pharmacology ; DNA Replication/*drug effects ; Dimethyl Sulfoxide/pharmacology ; Enzyme Activation ; Genistein ; Inositol Phosphates/metabolism ; Isoflavones/pharmacology ; Kinetics ; Lithium/pharmacology ; Lithium Chloride ; Mice ; Phosphatidylinositol 4,5-Diphosphate ; Phosphatidylinositols/metabolism ; Phosphorylation ; Platelet-Derived Growth Factor/*pharmacology ; Protein Kinase C/metabolism ; Protein-Tyrosine Kinases/metabolism ; Type C Phospholipases/*metabolism
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 169
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    Induction of CD4+ human cytolytic T cells specific for HIV-infected cells by a gp160 subunit vaccine (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-06-08
    Description: Cytolytic T lymphocyte (CTL) responses were evaluated in humans immunized with recombinant human immunodeficiency virus type 1 (HIV) envelope glycoprotein gp160. Some vaccinees had gp160-specific CTLs that were shown by cloning to be CD4+. Although induced by exogenous antigen, most gp160-specific CTL clones also recognized gp160 synthesized endogenously in target cells. These clones lysed autologous CD4+ T lymphoblasts infected with HIV. Of particular interest were certain vaccine-induced clones that lysed HIV-infected cells, recognized gp160 from diverse HIV isolates, and did not participate in "innocent bystander" killing of noninfected CD4+ T cells that had bound gp120.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Orentas, R J -- Hildreth, J E -- Obah, E -- Polydefkis, M -- Smith, G E -- Clements, M L -- Siliciano, R F -- 5T32CA09243/CA/NCI NIH HHS/ -- AI28108/AI/NIAID NIH HHS/ -- N01AI62515/AI/NIAID NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1990 Jun 8;248(4960):1234-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology and Molecular Sciences, Johns Hopkins University School of Medicine, Baltimore, MD 21205.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2190315" target="_blank"〉PubMed〈/a〉
    Keywords: Cells, Cultured ; Clone Cells ; Cytotoxicity, Immunologic ; Gene Products, env/*immunology ; HIV/*immunology ; HIV Envelope Protein gp160 ; HIV Seropositivity ; Humans ; Immunization ; Macromolecular Substances ; Protein Precursors/*immunology ; Recombinant Proteins/immunology ; T-Lymphocytes, Cytotoxic/*immunology ; Viral Vaccines/*immunology
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 170
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    Tumor cells exhibit deregulation of the cell cycle histone gene promoter factor HiNF-D (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-03-23
    Description: Cell cycle-regulated gene expression is essential for normal cell growth and development and loss of stringent growth control is associated with the acquisition of the transformed phenotype. The selective synthesis of histone proteins during the S phase of the cell cycle is required to render cells competent for the ordered packaging of replicating DNA into chromatin. Regulation of H4 histone gene transcription requires the proliferation-specific promoter binding factor HiNF-D. In normal diploid cells, HiNF-D binding activity is regulated during the cell cycle; nuclear protein extracts prepared from normal cells in S phase contain distinct and measurable HiNF-D binding activity, while this activity is barely detectable in G1 phase cells. In contrast, in tumor-derived or transformed cell lines, HiNF-D binding activity is constitutively elevated throughout the cell cycle and declines only with the onset of differentiation. The change from cell cycle-mediated to constitutive interaction of HiNF-D with the promoter of a cell growth-controlled gene is consistent with, and may be functionally related to, the loss of stringent cell growth regulation associated with neoplastic transformation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Holthuis, J -- Owen, T A -- van Wijnen, A J -- Wright, K L -- Ramsey-Ewing, A -- Kennedy, M B -- Carter, R -- Cosenza, S C -- Soprano, K J -- Lian, J B -- New York, N.Y. -- Science. 1990 Mar 23;247(4949 Pt 1):1454-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology, University of Massachusetts Medical School, Worcester 01655.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2321007" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Cell Cycle/*genetics ; Cell Line, Transformed ; Cells, Cultured ; DNA/genetics ; DNA-Binding Proteins/*metabolism ; Gene Expression Regulation, Neoplastic ; Histones/*genetics ; Humans ; Molecular Sequence Data ; Nuclear Proteins/*metabolism ; *Promoter Regions, Genetic ; RNA, Messenger/analysis ; Rats ; Sequence Homology, Nucleic Acid ; Transcription, Genetic ; Tumor Cells, Cultured
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  • 171
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    Neurotrophin-3: a neurotrophic factor related to NGF and BDNF (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-03-23
    Description: The development and maintenance of the nervous system depends on proteins known as neurotrophic factors. Although the prototypical neurotrophic factor, nerve growth factor (NGF), has been intensively studied for decades, the discovery and characterization of additional such factors has been impeded by their low abundance. Sequence homologies between NGF and the recently cloned brain-derived neurotrophic factor (BDNF) were used to design a strategy that has now resulted in the cloning of a gene encoding a novel neurotrophic factor, termed neurotrophin-3 (NT-3). The distribution of NT-3 messenger RNA and its biological activity on a variety of neuronal populations clearly distinguish NT-3 from NGF and BDNF, and provide compelling evidence that NT-3 is an authentic neurotrophic factor that has its own characteristic role in vivo.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Maisonpierre, P C -- Belluscio, L -- Squinto, S -- Ip, N Y -- Furth, M E -- Lindsay, R M -- Yancopoulos, G D -- New York, N.Y. -- Science. 1990 Mar 23;247(4949 Pt 1):1446-51.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Regeneron Pharmaceuticals, Inc., Tarrytown, New York 10591.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2321006" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Brain-Derived Neurotrophic Factor ; Cells, Cultured ; Cloning, Molecular ; DNA/genetics ; Mice ; Molecular Sequence Data ; Nerve Growth Factors/biosynthesis/*genetics/physiology ; Nerve Tissue Proteins/biosynthesis/*genetics/physiology ; Neurons/physiology ; Polymerase Chain Reaction ; Rats ; Restriction Mapping ; Sequence Homology, Nucleic Acid
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 172
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    Target-dependent structural changes accompanying long-term synaptic facilitation in Aplysia neurons (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-08-17
    Description: The mechanisms underlying structural changes that accompany learning and memory have been difficult to investigate in the intact nervous system. In order to make these changes more accessible for experimental analysis, dissociated cell culture and low-light-level video microscopy were used to examine Aplysia sensory neurons in the presence or absence of their target cells. Repeated applications of serotonin, a facilitating transmitter important in behavioral dishabituation and sensitization, produced growth of the sensory neurons that paralleled the long-term enhancement of synaptic strength. This growth required the presence of the postsynaptic motor neuron. Thus, both the structural changes and the synaptic facilitation of Aplysia sensorimotor synapses accompanying long-term behavioral sensitization can be produced in vitro by applying a single facilitating transmitter repeatedly. These structural changes depend on an interaction of the presynaptic neuron with an appropriate postsynaptic target.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Glanzman, D L -- Kandel, E R -- Schacher, S -- GM 323099/GM/NIGMS NIH HHS/ -- NS 19595/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1990 Aug 17;249(4970):799-802.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Columbia University, College of Physicians and Surgeons, New York, NY 10032.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2389145" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Aplysia/physiology/*ultrastructure ; Axons/ultrastructure ; Cells, Cultured ; Fluoresceins ; Fluorescent Dyes ; Memory/physiology ; Microscopy, Fluorescence ; Neurons, Afferent/drug effects/physiology/*ultrastructure ; Serotonin/pharmacology ; Synapses/physiology/*ultrastructure
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  • 173
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    Specific tropism of HIV-1 for microglial cells in primary human brain cultures (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-08-03
    Description: Human immunodeficiency virus (HIV) frequently causes neurological dysfunction and is abundantly expressed in the central nervous system (CNS) of acquired immunodeficiency syndrome (AIDS) patients with HIV encephalitis or myelopathy. The virus is found mostly in cells of the monocyte-macrophage lineage within the CNS, but the possibility of infection of other glial cells has been raised. Therefore, the effects of different HIV-1 and HIV-2 strains were studied in primary cultures of adult human brain containing microglial cells, the resident CNS macrophages, and astrocytes. These cultures could be productively infected with macrophage-adapted HIV-1 isolates but not with T lymphocyte-adapted HIV-1 isolates or two HIV-2 isolates. As determined with a triple-label procedure, primary astrocytes did not express HIV gag antigens and remained normal throughout the 3-week course of infection. In contrast, virus replicated in neighboring microglial cells, often leading to their cell fusion and death. The death of microglial cells, which normally serve immune functions in the CNS, may be a key factor in the pathogenesis of AIDS encephalitis or myelopathy.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Watkins, B A -- Dorn, H H -- Kelly, W B -- Armstrong, R C -- Potts, B J -- Michaels, F -- Kufta, C V -- Dubois-Dalcq, M -- New York, N.Y. -- Science. 1990 Aug 3;249(4968):549-53.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Viral and Molecular Pathogenesis, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2200125" target="_blank"〉PubMed〈/a〉
    Keywords: Adult ; Brain/*microbiology ; Cells, Cultured ; Fluorescent Antibody Technique ; HIV-1/pathogenicity/*physiology ; HIV-2/pathogenicity/physiology ; Humans ; Kinetics ; Neuroglia/*microbiology ; Species Specificity ; Virus Replication
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  • 174
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    A cell culture model for T lymphocyte clonal anergy (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-06-15
    Description: T lymphocytes respond to foreign antigens both by producing protein effector molecules known as lymphokines and by multiplying. Complete activation requires two signaling events, one through the antigen-specific receptor and one through the receptor for a costimulatory molecule. In the absence of the latter signal, the T cell makes only a partial response and, more importantly, enters an unresponsive state known as clonal anergy in which the T cell is incapable of producing its own growth hormone, interleukin-2, on restimulation. Our current understanding at the molecular level of this modulatory process and its relevance to T cell tolerance are reviewed.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schwartz, R H -- New York, N.Y. -- Science. 1990 Jun 15;248(4961):1349-56.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Cellular and Molecular Immunology, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2113314" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens, CD/immunology ; Antigens, CD4/immunology ; Antigens, CD8 ; Antigens, Differentiation, T-Lymphocyte/immunology ; Cells, Cultured ; Clone Cells/*immunology ; Gene Expression Regulation ; Gene Rearrangement, T-Lymphocyte ; *Immune Tolerance ; Interleukin-2/biosynthesis/genetics ; Mice ; *Models, Biological ; Receptors, Antigen, T-Cell/genetics/immunology ; Second Messenger Systems ; Signal Transduction ; T-Lymphocytes/*immunology ; Thymus Gland/immunology
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 175
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    Intercellular adhesion molecule-1 (ICAM-1) in the pathogenesis of asthma (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-01-26
    Description: Airway eosinophilia, epithelial desquamation, and hyperresponsiveness are characteristics of the airway inflammation underlying bronchial asthma. The contribution of intercellular adhesion molecule-1 (ICAM-1) to eosinophil migration and airway responsiveness was studied. ICAM-1 partially mediated eosinophil adhesion to to endothelium in vitro and was upregulated on inflamed bronchial endothelium in vivo. ICAM-1 expression was also upregulated on inflamed airway epithelium in vitro and in vivo. In a primate model of asthma, a monoclonal antibody to ICAM-1 attenuated airway eosinophilia and hyperresponsiveness. Thus, antagonism of ICAM-1 may provide a therapeutic approach to reducing airway inflammation, hyperresponsiveness, and asthma symptoms.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wegner, C D -- Gundel, R H -- Reilly, P -- Haynes, N -- Letts, L G -- Rothlein, R -- New York, N.Y. -- Science. 1990 Jan 26;247(4941):456-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, Boehringer Ingelheim Pharmaceuticals, Inc., Ridgefield, CT 06877.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1967851" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antibodies, Monoclonal ; Antigens/immunology ; Asthma/immunology/pathology/*physiopathology ; Cell Adhesion ; Cell Adhesion Molecules/analysis/immunology/*physiology ; Cells, Cultured ; Endothelium/pathology ; Eosinophils/*pathology ; Epithelium/metabolism ; Humans ; Immunization, Passive ; Immunohistochemistry ; Intercellular Adhesion Molecule-1 ; Interferon-gamma/pharmacology ; Interleukin-1/pharmacology ; Lung/metabolism/pathology ; Macaca fascicularis ; Recombinant Proteins ; Tumor Necrosis Factor-alpha/pharmacology
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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