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1988 Fiscal Year Final Research Report Summary

Molcular control of platelets function by protein kinases

Research Project

Project/Area Number 62580116
Research Category

Grant-in-Aid for General Scientific Research (C)

Allocation TypeSingle-year Grants
Research Field 物質生物化学
Research InstitutionMie University

Principal Investigator

NAKA Michiko  Mie University School of Medicine, Assistant, 医学部, 助手 (10093139)

Project Period (FY) 1987 – 1988
KeywordsPlatet / protein phosphorylation / Myosin light chain kinase / Cキナーゼ
Research Abstract

Biological function of blood plateletsincluding aggregating, secretion and clot retraction are expressed through cellular contractile activity. The Ca^<2+>-calmodulin-dependent phosphorylation of 20K-Da myosin light chain(MLC)catalyzed by mlc kinase may be the major regulation system of contractile proteins in platelets,as well as in smooth muscle cells. Recentry, we found that protein kinase C is responsible for phosphorylation of 20K-Da MLC during platelet activation (particularly in resppnse to stimulation by TPA). Three forms of 20K-Da MLC,unphosphorylated, monophosphorylated and diphosphorylated MLC were observed in thrombin-stimulated human platelets by two different gel electrophoretic method; in the presence of glycerol urea or in two dimensions. after mon/-or diphosphorylated 20K-Da MLC from thrombin stimulated platelet was digsted with trypsin the analysis using two-dimensional peptide mapping demonstrated that two different sites were phosphorylated by MLC kinase and protein kinase C. Activation of protein kinase C and mobilzation of Ca^<2+>are induced separately in intact cells by treatment with TPA and Ca^<2+>ionophore respectively. We invastigated whether double phosphorylations of 20K-Da MLC were induced by TPA or Ca^<2+>ionophore. TPA activated both MLC kinase and protein kinase C but Ca^<2+>ionophre activated only MLC kinase.

  • Research Products

    (10 results)

All Other

All Publications (10 results)

  • [Publications] M.Naka.: Archives of Biochem.and Biophy.261. 235-240 (1988)

    • Description
      「研究成果報告書概要(和文)」より
  • [Publications] T.Tanaka.: Biochem.Pharm.37. 2537-2542 (1988)

    • Description
      「研究成果報告書概要(和文)」より
  • [Publications] M.Ikebe.: J.Biol.Chem.263. 10698-10704 (1988)

    • Description
      「研究成果報告書概要(和文)」より
  • [Publications] M.Saitoh.: J.Biol.Chem.262. 7796-7801 (1987)

    • Description
      「研究成果報告書概要(和文)」より
  • [Publications] T.Tanaka.: "Platelet Activation" Calcium-dependent protein phosphorylation in platelet activation and the selective inhibitors., 17-26 (1987)

    • Description
      「研究成果報告書概要(和文)」より
  • [Publications] M.Naka: "Two phosphorylated forms of myosin in thrombin-stimulated platelets." Archives of Biochem. and Biophy.261. 235-240 (1988)

    • Description
      「研究成果報告書概要(欧文)」より
  • [Publications] T.Tanaka: "Inhibition of human platelet secretion and of Ca^<2+>,calmodulin-dependent protein phosphorylation by the antiallergic agent GMCHA." Biochem. Pharm.37. 2537-2542 (1988)

    • Description
      「研究成果報告書概要(欧文)」より
  • [Publications] M.Ikebe: "Correlation of conformation and phosphorylation and dephosphoration of smooth muscle myosin." J. Biol. Chem.263. 10698-10704 (1988)

    • Description
      「研究成果報告書概要(欧文)」より
  • [Publications] M.Saitoh: "Selective inhibition of catalytic activity of smooth muscle myosin light chain kinase." J. Biol. Chem.262. 7796-7801 (1987)

    • Description
      「研究成果報告書概要(欧文)」より
  • [Publications] T.Tanaka: Calcium-dependent protein phosphorylation in platelet activation and the selective inhibitors.Platelet Activation., 17-26 (1987)

    • Description
      「研究成果報告書概要(欧文)」より

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Published: 1990-03-20  

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