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  • Signal Transduction
  • American Association for the Advancement of Science (AAAS)  (21)
  • American Chemical Society (ACS)
  • 2010-2014
  • 1990-1994  (21)
  • 1991  (21)
Collection
Keywords
Publisher
  • American Association for the Advancement of Science (AAAS)  (21)
  • American Chemical Society (ACS)
Years
  • 2010-2014
  • 1990-1994  (21)
Year
  • 1
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    Photoreceptor deactivation and retinal degeneration mediated by a photoreceptor-specific protein kinase C (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-12-06
    Description: The protein kinase C (PKC) family of serine-threonine kinases has been implicated in the regulation of a variety of signaling cascades. One member of this family, eye-PKC, is expressed exclusively in the Drosophila visual system. The inaC (inactivation-no-afterpotential C) locus was shown to be the structural gene for eye-PKC. Analysis of the light response from inaC mutants showed that this kinase is required for the deactivation and rapid desensitization of the visual cascade. Light adaptation was also defective in inaC mutant flies. In flies carrying the retinal degeneration mutation rdgB, absence of eye-PKC suppressed photoreceptor cell degeneration. These results indicate that eye-PKC functions in the light-dependent regulation of the phototransduction cascade in Drosophila.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Smith, D P -- Ranganathan, R -- Hardy, R W -- Marx, J -- Tsuchida, T -- Zuker, C S -- New York, N.Y. -- Science. 1991 Dec 6;254(5037):1478-84.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, University of California, San Diego, La Jolla.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1962207" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptation, Physiological/physiology ; Amino Acid Sequence ; Animals ; Calcium/physiology ; DNA Mutational Analysis ; Drosophila melanogaster/*genetics ; Eye/enzymology ; Genes ; Molecular Sequence Data ; Photoreceptor Cells/*physiology ; Protein Kinase C/chemistry/*physiology ; Restriction Mapping ; Retinal Degeneration/pathology/*physiopathology ; Signal Transduction ; *Vision, Ocular
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 2
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    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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  • 3
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    New clue found to growth factor action (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-03-08
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hoffman, M -- New York, N.Y. -- Science. 1991 Mar 8;251(4998):1181.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2006408" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Contractile Proteins/physiology ; Cytoskeleton/*physiology/ultrastructure ; Epidermal Growth Factor/*physiology ; Inositol 1,4,5-Trisphosphate/physiology ; Microfilament Proteins/*physiology ; Models, Biological ; Profilins ; Receptor, Epidermal Growth Factor/physiology ; Signal Transduction ; Type C Phospholipases/metabolism
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  • 4
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    Regulation of phospholipase C-gamma 1 by profilin and tyrosine phosphorylation (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-03-08
    Description: Epidermal growth factor and platelet-derived growth factor can stimulate the production of the second messenger inositol trisphosphate in responsive cells, but the biochemical pathway for these signaling events has been uncertain because the reactions have not been reconstituted with purified molecules in vitro. A reconstitution is described that requires not only the growth factor, its receptor with tyrosine kinase activity, and the soluble phospholipase C-gamma 1, but also the small soluble actin-binding protein profilin. Profilin binds to the substrate phosphatidylinositol 4,5-bisphosphate and inhibits its hydrolysis by unphosphorylated phospholipase C-gamma 1. Phosphorylation of phospholipase C-gamma 1 by the epidermal growth factor receptor tyrosine kinase overcomes the inhibitory effect of profilin and results in an effective activation of phospholipase C-gamma 1.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Goldschmidt-Clermont, P J -- Kim, J W -- Machesky, L M -- Rhee, S G -- Pollard, T D -- GM-26338/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1991 Mar 8;251(4998):1231-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology and Anatomy, 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/1848725" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Contractile Proteins/metabolism ; Epidermal Growth Factor/*metabolism ; Inositol Phosphates/metabolism ; Isoenzymes/*metabolism ; Kinetics ; Microfilament Proteins/*metabolism ; Phosphatidylinositol 4,5-Diphosphate ; Phosphatidylinositols/metabolism ; Phosphorylation ; Profilins ; Protein-Tyrosine Kinases/*metabolism ; Receptor, Epidermal Growth Factor/*metabolism ; Signal Transduction ; Type C Phospholipases/*metabolism ; Tyrosine
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  • 5
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    Cloning of complementary DNA encoding a functional human interleukin-8 receptor (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-09-13
    Description: Interleukin-8 (IL-8) is an inflammatory cytokine that activates neutrophil chemotaxis, degranulation, and the respiratory burst. Neutrophils express receptors for IL-8 that are coupled to guanine nucleotide-binding proteins (G proteins); binding of IL-8 to its receptor induces the mobilization of intracellular calcium stores. A cDNA clone from HL-60 neutrophils, designated p2, has now been isolated that encodes a human IL-8 receptor. When p2 is expressed in oocytes from Xenopus laevis, the oocytes bind 125I-labeled IL-8 specifically and respond to IL-8 by mobilizing calcium stores with an EC50 of 20 nM. This IL-8 receptor has 77% amino acid identity with a second human neutrophil receptor isotype that binds IL-8 with higher affinity. It also exhibits 69% amino acid identity with a protein reported to be an N-formyl peptide receptor from rabbit neutrophils, but less than 30% identity with all other known G protein-coupled receptors, including the human N-formyl peptide receptor.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Murphy, P M -- Tiffany, H L -- New York, N.Y. -- Science. 1991 Sep 13;253(5025):1280-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Host Defenses, 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/1891716" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Binding, Competitive ; Cloning, Molecular/methods ; DNA/genetics ; Gene Library ; Humans ; Interleukin-8/*metabolism/pharmacology ; Kinetics ; Molecular Sequence Data ; Neutrophils/immunology ; Oocytes/drug effects/physiology ; Protein Biosynthesis ; Rabbits ; Receptors, Immunologic/drug effects/*genetics/physiology ; Receptors, Interleukin-8A ; Recombinant Proteins/metabolism ; Sequence Homology, Nucleic Acid ; Signal Transduction ; Transcription, Genetic ; Xenopus
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  • 6
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    Cell cycle-dependent coupling of the calcitonin receptor to different G proteins (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-03-01
    Description: Calcitonin is a calcium regulating peptide hormone with binding sites in kidney and bone as well as in the central nervous system. The mechanisms of signal transduction by calcitonin receptors were studied in a pig kidney cell line where the hormone was found to regulate sodium pumps. Calcitonin receptors activated the cyclic adenosine monophosphate (cAMP) or the protein kinase C (PKC) pathways. The two transduction pathways required guanosine triphosphate (GTP)-binding proteins (G proteins) (the choleratoxin sensitive Gs and the pertussis toxin sensitive Gi, respectively) and led to opposite biological responses. Moreover, selective activation of one or the other pathway was cell cycle-dependent. Therefore, calcitonin may induce different biological responses in target cells depending on their positions in the cell cycle. Such a modulation of ligand-induced responses could be of importance in rapidly growing cell populations such as during embryogenesis, growth, and tumor formation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chakraborty, M -- Chatterjee, D -- Kellokumpu, S -- Rasmussen, H -- Baron, R -- DE-04724/DE/NIDCR NIH HHS/ -- DK-19813/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1991 Mar 1;251(4997):1078-82.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Yale University School of Medicine, Department of Cell Biology, New Haven, CT 06510.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1847755" target="_blank"〉PubMed〈/a〉
    Keywords: Adenylyl Cyclases/physiology ; Animals ; Calcitonin/*physiology ; *Cell Cycle ; Cell Line ; GTP-Binding Proteins/*physiology ; Kidney ; Ouabain/metabolism ; Receptors, Calcitonin ; Receptors, Cell Surface/*physiology ; Signal Transduction ; Sodium-Potassium-Exchanging ATPase/*metabolism ; Swine
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  • 7
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    GPI-anchored cell-surface molecules complexed to protein tyrosine kinases (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-11-15
    Description: Binding of ligand or antibody to certain cell-surface proteins that are anchored to the membrane by glycophosphatidylinositol (GPI) can cause activation of leukocytes. However, it is not known how these molecules, which lack intracellular domains, can transduce signals. The GPI-linked human molecules CD59, CD55, CD48, CD24, and CD14 as well as the mouse molecules Thy-1 and Ly-6 were found to associate with protein tyrosine kinases, key regulators of cell activation and signal transduction. A protein tyrosine kinase associated with the GPI-linked proteins CD59, CD55, and CD48 in human T cells, and with Thy-1 in mouse T cells was identified as p56lck, a protein tyrosine kinase related to Src. This interaction of GPI-linked molecules with protein tyrosine kinases suggests a potential mechanism of signal transduction in cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stefanova, I -- Horejsi, V -- Ansotegui, I J -- Knapp, W -- Stockinger, H -- New York, N.Y. -- Science. 1991 Nov 15;254(5034):1016-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Immunology-Vienna International Research Cooperation Center, University of Vienna, Austria.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1719635" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens, CD/*physiology ; Antigens, Differentiation/physiology ; Cell Adhesion Molecules/physiology ; Glycolipids/physiology ; Glycosylphosphatidylinositols ; Humans ; Membrane Glycoproteins/physiology ; Membrane Proteins/*physiology ; Mice ; Phosphatidylinositols/physiology ; Phosphorylation ; Phosphotyrosine ; Protein-Tyrosine Kinases/*physiology ; Receptor Aggregation ; Receptors, Cell Surface/*physiology ; Signal Transduction ; Tyrosine/analogs & derivatives/metabolism
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  • 8
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    Suppression of the immune response by a soluble complement receptor of B lymphocytes (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-10-04
    Description: The CD19-CR2 complex of B lymphocytes contains proteins that participate in two host-defense systems, the immune and complement systems. The ligand for the subunit of the immune system, CD19, is not known, but the complement receptor subunit, CR2 (CD21), binds activation fragments of the C3 component of the complement system and may mediate immunopotentiating effects of complement. A recombinant, soluble CR2 was prepared by fusing the C3-binding region of the receptor to immunoglobulin G1 (IgG1). The (CR2)2-IgG1 chimera competed with cellular CR2 for C3 binding and suppressed the antibody response to a T cell-dependent antigen when administered to mice at the time of immunization. This inhibitory effect of (CR2)2-IgG1 demonstrates the B cell-activating function of the CD19-CR2 complex and suggests a new method for humoral immunosuppression.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hebell, T -- Ahearn, J M -- Fearon, D T -- AI-22833/AI/NIAID NIH HHS/ -- AI-28191/AI/NIAID NIH HHS/ -- GM-43803/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1991 Oct 4;254(5028):102-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine, Johns Hopkins University School of Medicine, Baltimore, MD 21205.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1718035" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; *Antibody Formation ; Antigens, CD/*physiology ; Antigens, CD19 ; Antigens, Differentiation, B-Lymphocyte/chemistry/*physiology ; B-Lymphocytes/*physiology ; Base Sequence ; Binding, Competitive ; Cloning, Molecular ; Immunosuppression ; In Vitro Techniques ; Mice ; Mice, Inbred BALB C ; Mice, Inbred C3H ; Molecular Sequence Data ; Receptors, Complement/chemistry/*physiology ; Receptors, Complement 3d ; Recombinant Fusion Proteins ; Signal Transduction ; Solubility
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  • 9
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    Targets for cell cycle arrest by the immunosuppressant rapamycin in yeast (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-08-23
    Description: FK506 and rapamycin are related immunosuppressive compounds that block helper T cell activation by interfering with signal transduction. In vitro, both drugs bind and inhibit the FK506-binding protein (FKBP) proline rotamase. Saccharomyces cerevisiae cells treated with rapamycin irreversibly arrested in the G1 phase of the cell cycle. An FKBP-rapamycin complex is concluded to be the toxic agent because (i) strains that lack FKBP proline rotamase, encoded by FPR1, were viable and fully resistant to rapamycin and (ii) FK506 antagonized rapamycin toxicity in vivo. Mutations that conferred rapamycin resistance altered conserved residues in FKBP that are critical for drug binding. Two genes other than FPR1, named TOR1 and TOR2, that participate in rapamycin toxicity were identified. Nonallelic noncomplementation between FPR1, TOR1, and TOR2 alleles suggests that the products of these genes may interact as subunits of a protein complex. Such a complex may mediate nuclear entry of signals required for progression through the cell cycle.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Heitman, J -- Movva, N R -- Hall, M N -- New York, N.Y. -- Science. 1991 Aug 23;253(5022):905-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, University of Basel, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1715094" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Anti-Bacterial Agents/metabolism/pharmacology ; Base Sequence ; Binding Sites ; Carrier Proteins/antagonists & inhibitors/chemistry/genetics/metabolism ; Cell Cycle/*drug effects ; Cyclosporins/pharmacology ; Drug Resistance, Microbial/genetics ; G1 Phase/drug effects ; Humans ; Immunosuppressive Agents/pharmacology ; Molecular Sequence Data ; Molecular Structure ; Mutation ; Polyenes/metabolism/*pharmacology ; Saccharomyces cerevisiae/*cytology/drug effects ; Sequence Homology, Nucleic Acid ; Signal Transduction ; Sirolimus ; Tacrolimus ; Tacrolimus Binding Proteins
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  • 10
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    Regulation of interleukin-2 gene enhancer activity by the T cell accessory molecule CD28 (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-01-18
    Description: The mechanism by which cell surface molecules regulate T cell production of lymphokines is poorly understood. Production of interleukin-2 (IL-2) can be regulated by signal transduction pathways distinct from those induced by the T cell antigen receptor. Stimulation of CD28, a molecule expressed on most human T cells, induced the formation of a protein complex that bound to a site on the IL-2 gene distinct from previously described binding sites and increased IL-2 enhancer activity fivefold. The CD28-responsive complex bound to the IL-2 gene between -164 and -154 base pairs from the transcription start site. The sequence of this element is similar to regions conserved in the 5' flanking regions of several other lymphokine genes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fraser, J D -- Irving, B A -- Crabtree, G R -- Weiss, A -- GM39553/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1991 Jan 18;251(4991):313-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, University of California, San Francisco 94143.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1846244" target="_blank"〉PubMed〈/a〉
    Keywords: Antigens, CD28 ; Antigens, Differentiation, T-Lymphocyte/*physiology ; Base Sequence ; Cell Line ; DNA Mutational Analysis ; *Enhancer Elements, Genetic ; Gene Expression Regulation ; Humans ; In Vitro Techniques ; Interleukin-2/*genetics ; Molecular Sequence Data ; Oligonucleotides/chemistry ; *Regulatory Sequences, Nucleic Acid ; Signal Transduction ; T-Lymphocytes/*physiology ; Transcription, Genetic
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  • 11
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    Intrasubunit signal transduction by the aspartate chemoreceptor (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-12-23
    Description: Receptors that transmit signals across cell membranes are typically composed of multiple subunits. To test whether subunit interactions are required for transmembrane signaling by the bacterial aspartate receptor, dimers were constructed with (i) two full-length subunits, (ii) one full-length subunit and one subunit lacking the cytoplasmic domain, or (iii) one full-length subunit and one subunit lacking both the cytoplasmic and the transmembrane domains. Methylation of the cytoplasmic domain of all three receptor constructs was stimulated by the binding of aspartate. These findings demonstrate that transmembrane signaling does not require interactions between cytoplasmic or transmembrane domains of adjacent subunits and suggest that signaling occurs via conformational changes transduced through a single subunit.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Milligan, D L -- Koshland, D E Jr -- DK 09765/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1991 Dec 13;254(5038):1651-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Cell Biology, University of California, Berkeley 94720.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1661030" target="_blank"〉PubMed〈/a〉
    Keywords: Aspartic Acid/*physiology ; DNA Mutational Analysis ; Ligands ; Macromolecular Substances ; Methylation ; Protein Conformation ; *Receptors, Amino Acid ; Receptors, Cell Surface/*chemistry ; Recombinant Proteins ; Salmonella typhimurium ; Signal Transduction ; Structure-Activity Relationship
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  • 12
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    Effect of wnt-1 and related proteins on gap junctional communication in Xenopus embryos (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-05-24
    Description: The proto-oncogene wnt-1 (previously referred to as int-1) is thought to be important in embryonic pattern formation although its mechanisms of action are unknown. Premature and increased expression of the Wnt-1 protein, achieved by injection of synthetic wnt-1 RNA into fertilized Xenopus eggs, enhanced gap junctional communication between ventral cells of the developing embryo. This result is consistent with the hypothesis that Wnt proteins activate a receptor-mediated signal transduction pathway and that gap junctional communication can be a target of this pathway. The effects of two Wnt-1-related proteins on gap junctional communication were also investigated: overexpression of Xwnt-8 increased gap junctional coupling in a manner similar to Wnt-1, whereas Xwnt-5A did not. These findings are consistent with the existence of multiple receptors for Wnt proteins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Olson, D J -- Christian, J L -- Moon, R T -- DE-07023/DE/NIDCR NIH HHS/ -- KO4-AR01837/AR/NIAMS NIH HHS/ -- R01-AR40089/AR/NIAMS NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1991 May 24;252(5009):1173-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, 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/2031187" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Blastomeres/cytology/*physiology ; *Cell Communication ; Embryo, Nonmammalian/cytology/*physiology ; Female ; Intercellular Junctions/*physiology ; Male ; Protein-Tyrosine Kinases/genetics ; Proto-Oncogene Proteins/*genetics/physiology ; *Proto-Oncogenes ; Signal Transduction ; Sperm-Ovum Interactions ; Wnt Proteins ; Wnt1 Protein ; Xenopus ; Xenopus Proteins ; *Zebrafish Proteins
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  • 13
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    CREB: a Ca(2+)-regulated transcription factor phosphorylated by calmodulin-dependent kinases (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-06-07
    Description: The mechanism by which Ca2+ mediates gene induction in response to membrane depolarization was investigated. The adenosine 3',5'-monophosphate (cAMP) response element-binding protein (CREB) was shown to function as a Ca(2+)-regulated transcription factor and as a substrate for depolarization-activated Ca(2+)-calmodulin-dependent protein kinases (CaM kinases) I and II. CREB residue Ser133 was the major site of phosphorylation by the CaM kinases in vitro and of phosphorylation after membrane depolarization in vivo. Mutation of Ser133 impaired the ability of CREB to respond to Ca2+. These results suggest that CaM kinases may transduce electrical signals to the nucleus and that CREB functions to integrate Ca2+ and cAMP signals.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sheng, M -- Thompson, M A -- Greenberg, M E -- R01 CA 43855/CA/NCI NIH HHS/ -- R01 NS 28829/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1991 Jun 7;252(5011):1427-30.〈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/1646483" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Calcium/*pharmacology ; Calcium-Calmodulin-Dependent Protein Kinases ; Chromosome Mapping ; Cloning, Molecular ; Cyclic AMP/physiology ; Cyclic AMP Response Element-Binding Protein ; DNA-Binding Proteins/*physiology ; Electrophoresis, Polyacrylamide Gel ; Fungal Proteins/pharmacology ; Gene Expression Regulation/*drug effects ; Genes, Regulator/physiology ; Humans ; In Vitro Techniques ; Phosphorylation ; Protein Kinases/pharmacology ; Rats ; Recombinant Fusion Proteins/pharmacology ; *Saccharomyces cerevisiae Proteins ; Serine/chemistry ; Signal Transduction ; TATA Box ; Transcription Factors/*physiology ; Transcription, Genetic/drug effects ; Transcriptional Activation
    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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  • 14
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    Association of B cell antigen receptor with protein tyrosine kinase Lyn (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-01-11
    Description: Antigen is thought to cross-link membrane-bound immunoglobulins (Igs) of B cells, causing proliferation and differentiation or the inhibition of growth. Protein tyrosine kinases are probably involved in signal transduction for cell proliferation and differentiation. The Src-like protein tyrosine kinase Lyn is expressed preferentially in B cells. The Lyn protein and its kinase activity could be coimmunoprecipitated with IgM from detergent lysates. Cross-linking of membrane-bound IgM induced a rapid increase in tyrosine phosphorylation of at least ten distinct proteins of B cells. Thus, Lyn is physically associated with membrane-bound IgM, and is suggested to participate in antigen-mediated signal transduction.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yamanashi, Y -- Kakiuchi, T -- Mizuguchi, J -- Yamamoto, T -- Toyoshima, K -- New York, N.Y. -- Science. 1991 Jan 11;251(4990):192-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Oncology, University of Tokyo, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1702903" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; B-Lymphocytes/immunology ; Cell Line ; Detergents ; Electrophoresis, Polyacrylamide Gel ; Immunoblotting ; Immunoglobulin M/metabolism ; Immunosorbent Techniques ; Mice ; Molecular Weight ; Phosphoproteins/metabolism ; Phosphorylation ; Phosphotyrosine ; Protein-Tyrosine Kinases/genetics/*metabolism ; Receptors, Antigen, B-Cell/*metabolism ; Signal Transduction ; Tyrosine/analogs & derivatives/metabolism ; *src-Family Kinases
    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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  • 15
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    Growth factors and cancer (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-11-22
    Description: Signaling pathways that mediate the normal functions of growth factors are commonly subverted in cancer. Oncogenes identified by a variety of approaches have been shown to function at critical steps in mitogenic signaling. Progression through the cell cycle requires the coordinated actions of members of two complementary classes of growth factors, and oncogenes appear to replace the actions of one set of these growth factors. Growth factors can also influence normal cell differentiation, and constitutive activation of growth-promoting pathways in cancer cells can modulate the cell phenotype as well. Paracrine actions of growth factors and cytokines may also influence the stepwise series of genetic events that lead to malignancy. New approaches for cancer therapy are being developed that intervene at various steps in growth factor signaling pathways.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Aaronson, S A -- New York, N.Y. -- Science. 1991 Nov 22;254(5035):1146-53.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Cellular and Molecular Biology, National Cancer Institute, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1659742" target="_blank"〉PubMed〈/a〉
    Keywords: *Cell Division ; Growth Substances/*physiology ; Humans ; Mitogens ; Neoplasms/pathology/*physiopathology ; Oncogenes ; Protein-Tyrosine Kinases/physiology ; Proto-Oncogenes ; Receptors, Cell Surface/physiology ; Signal Transduction ; Substrate Specificity
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 16
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    Separation of IL-4 production from Th cell proliferation by an altered T cell receptor ligand (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-05-31
    Description: In the presence of antigen presenting cells, a murine T helper (Th) cell specific for murine hemoglobin (Hb) responded to its immunogenic peptide by both cytokine (interleukin-4) secretion and proliferation. An altered Hb peptide with a single amino acid substitution induced only cytokine secretion and did not induce proliferation. Interleukin-1 costimulated and restored the Th proliferative response to normal levels. The altered peptide also supported cognate T cell-B cell interactions indicative of T cell helper function. Thus, this result suggests that the T cell receptor has the capacity of differential signaling.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Evavold, B D -- Allen, P M -- AI24157/AI/NIAID NIH HHS/ -- ESO7066/ES/NIEHS NIH HHS/ -- New York, N.Y. -- Science. 1991 May 31;252(5010):1308-10.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pathology, Washington University School of Medicine, St. Louis, MO 63110.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1833816" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Cell Division ; Clone Cells ; Hemoglobins/chemistry/*immunology ; Interleukin-4/*biosynthesis ; Lymphocyte Activation/*immunology ; Mice ; Molecular Sequence Data ; Peptide Fragments/chemistry/*immunology ; Receptors, Antigen, T-Cell/immunology/*metabolism ; Signal Transduction ; T-Lymphocytes, Helper-Inducer/cytology/*immunology
    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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  • 17
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    Intracellular signaling by 14-hydroxy-4,14-retro-retinol (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-12-13
    Description: In mammals, retinol is the precursor for retinoids, which affect various aspects of morphogenesis and development. However, B lymphocytes, although retinol-dependent, do not use retinoic acid as mediator. Retinol is metabolized by B lymphocytes and other cell lines to optically active 14-hydroxy-4,14-retro-retinol; it is this compound that mediates the growth control. Thus another second messenger molecule, in addition to retinoic acid and retinal, is derived from retinol.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Buck, J -- Derguini, F -- Levi, E -- Nakanishi, K -- Hammerling, U -- AI38351/AI/NIAID NIH HHS/ -- CA49933/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1991 Dec 13;254(5038):1654-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Immunology, Memorial Sloan-Kettering Cancer Center, New York, New York 10021.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1749937" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; B-Lymphocytes/physiology ; Cell Line ; Growth Substances ; Humans ; Magnetic Resonance Spectroscopy ; Mice ; Retinoids/*chemistry ; Second Messenger Systems ; Signal Transduction ; Spectrophotometry, Ultraviolet ; Vitamin A/*analogs & derivatives/chemistry/physiology
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 18
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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)
    Details
    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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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 19
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    Presence of an SH2 domain in the actin-binding protein tensin (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-05-03
    Description: The molecular cloning of the complementary DNA coding for a 90-kilodalton fragment of tensin, an actin-binding component of focal contacts and other submembraneous cytoskeletal structures, is reported. The derived amino acid sequence revealed the presence of a Src homology 2 (SH2) domain. This domain is shared by a number of signal transduction proteins including nonreceptor tyrosine kinases such as Abl, Fps, Src, and Src family members, the transforming protein Crk, phospholipase C-gamma 1, PI-3 (phosphatidylinositol) kinase, and guanosine triphosphatase-activating protein (GAP). Like the SH2 domain found in Src, Crk, and Abl, the SH2 domain of tensin bound specifically to a number of phosphotyrosine-containing proteins from v-src-transformed cells. Tensin was also found to be phosphorylated on tyrosine residues. These findings suggest that by possessing both actin-binding and phosphotyrosine-binding activities and being itself a target for tyrosine kinases, tensin may link signal transduction pathways with the cytoskeleton.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Davis, S -- Lu, M L -- Lo, S H -- Lin, S -- Butler, J A -- Druker, B J -- Roberts, T M -- An, Q -- Chen, L B -- GM 22289/GM/NIGMS NIH HHS/ -- GM 38318/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1991 May 3;252(5006):712-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Cellular and Molecular Biology, Dana-Farber Cancer Institute, Harvard Medical School, Boston, MA 02115.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1708917" target="_blank"〉PubMed〈/a〉
    Keywords: Actins/*metabolism ; Amino Acid Sequence ; Animals ; Binding Sites ; Chick Embryo ; Cloning, Molecular ; Cytoskeletal Proteins/*chemistry/genetics/metabolism ; DNA/genetics ; Fluorescent Antibody Technique ; Immunoblotting ; *Microfilament Proteins ; Molecular Sequence Data ; Peptide Fragments/genetics ; Phosphotyrosine ; Protein-Tyrosine Kinases/genetics ; Sequence Homology, Nucleic Acid ; Signal Transduction ; Tyrosine/analogs & derivatives/metabolism
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 20
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    Dopaminergic and ligand-independent activation of steroid hormone receptors (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-12-13
    Description: The current view of how steroid hormone receptors affect gene transcription is that these receptors, on binding ligand, change to a state in which they can interact with chromatin and regulate transcription of target genes. Receptor activation is believed to be dependent only on this ligand-binding event. Selected steroid hormone receptors can be activated in a ligand-independent manner by a membrane receptor agonist, the neurotransmitter dopamine. In vitro, dopamine faithfully mimicked the effect of progesterone by causing a translocation of chicken progesterone receptor (cPR) from cytoplasm to nucleus. Dual activation by progesterone and dopamine was dissociable, and a serine residue in the cPR was identified that is not necessary for progesterone-dependent activation of cPR, but is essential for dopamine activation of this receptor.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Power, R F -- Mani, S K -- Codina, J -- Conneely, O M -- O'Malley, B W -- New York, N.Y. -- Science. 1991 Dec 13;254(5038):1636-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology, Baylor College of Medicine, Houston, TX 77030.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1749936" target="_blank"〉PubMed〈/a〉
    Keywords: 2,3,4,5-Tetrahydro-7,8-dihydroxy-1-phenyl-1H-3-benzazepine/pharmacology ; Adenylyl Cyclases/physiology ; Animals ; Cell Line ; Cercopithecus aethiops ; Dopamine/*pharmacology ; Epinephrine/pharmacology ; Ergolines/pharmacology ; Ethers, Cyclic/pharmacology ; Gene Expression Regulation/drug effects ; In Vitro Techniques ; Isoproterenol/pharmacology ; Ligands ; Norepinephrine/pharmacology ; Okadaic Acid ; Promoter Regions, Genetic ; Quinpirole ; Receptors, Dopamine/*physiology ; Receptors, Steroid/*physiology ; Regulatory Sequences, Nucleic Acid ; Signal Transduction ; Transcription Factors/physiology ; Transcription, Genetic/drug effects
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 21
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    Coordinate regulation of beta-lactamase induction and peptidoglycan composition by the amp operon (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-01-11
    Description: The amp operon, which is located on the Escherichia coli chromosome, modulates the induction of plasmid-borne beta-lactamase genes by extracellular beta-lactam antibiotics. This suggests that the gene products AmpD and AmpE may function in the transduction of external signals. beta-Lactam antibiotics are analogs of cell wall components that can be released during cell wall morphogenesis of enterobacteria. The amp operon was studied to determine its importance in signal transduction during cell wall morphogenesis. The peptidoglycan compositions of amp mutants were determined by high-performance liquid chromatography and fast atom bombardment mass spectrometry. When a chromosomal or plasmid-borne copy of ampD was present, the amount of pentapeptide-containing muropeptides in the cell wall increased upon addition of the cell wall constituent diaminopimelic acid to the growth medium. These results suggest that beta-lactamase induction and modulation of the composition of the cell wall share elements of a regulatory circuit that involves AmpD. Escherichia coli requires AmpD to respond to extracellular signaling amino acids, such as diaminopimelic acid, and this signal transduction system may regulate peptidoglycan composition in response to cell wall turnover products.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tuomanen, E -- Lindquist, S -- Sande, S -- Galleni, M -- Light, K -- Gage, D -- Normark, S -- AI23459/AI/NIAID NIH HHS/ -- AI27913/AI/NIAID NIH HHS/ -- DRR00480/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 1991 Jan 11;251(4990):201-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Microbiology, Rockefeller University, New York, NY 10021.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1987637" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Bacterial Proteins/*genetics/metabolism ; Carboxypeptidases/metabolism ; Cell Wall/metabolism ; Diaminopimelic Acid/pharmacology ; Enzyme Induction ; Escherichia coli/*genetics/metabolism ; *Gene Expression Regulation/drug effects ; Genotype ; Membrane Proteins/*genetics/metabolism ; Molecular Sequence Data ; Mutation ; *N-Acetylmuramoyl-L-alanine Amidase ; Oligopeptides/metabolism ; *Operon ; Peptidoglycan/metabolism ; Plasmids ; Signal Transduction ; Spectrometry, Mass, Fast Atom Bombardment ; beta-Lactamases/*biosynthesis/genetics
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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