| Project/Area Number |
08680680
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Functional biochemistry
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| Research Institution | Mie University |
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Principal Investigator |
IDO Masaru Mie University Faculty of Medicine, Lecturer, 医学部, 講師 (90167263)
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| Co-Investigator(Kenkyū-buntansha) |
SUZUKI Koji Mie University Faculty of Medicine, Professor, 医学部, 教授 (70077808)
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| Project Period (FY) |
1996 – 1997
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| Project Status |
Completed (Fiscal Year 1997)
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| Budget Amount *help |
¥2,500,000 (Direct Cost: ¥2,500,000)
Fiscal Year 1997: ¥1,300,000 (Direct Cost: ¥1,300,000)
Fiscal Year 1996: ¥1,200,000 (Direct Cost: ¥1,200,000)
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| Keywords | Thrombin receptor / Protein kinase / Platelet / Proteim Kinase / トロンビンレセプター |
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| Research Abstract |
Novel protein kinases that may associate with thrombin receptor were sought by a procedure based on the ability of these enzymes to undergo renaturation and catalyze the phosphorylation of a protein substrate fixed in a gel. We employed a fusion protein comprising of glutathione S-transferase and the substrate protein that corresponds to residues 375-421 of thrombin receptor (GST-TRCD). We report that platelets contain a serine/threonine protein kinase with molecular masse of about 33 kDa, which specifically bound to GST-TRCD.Treatment of platelets with thrombin increased the thrombin receptor-associated kinase (TRAK) activity by 700%. TRAK was also activated by a thrombin receptor agonist peptide, but not by hirudin-treated or diisopropylphosphate-inactivated thrombin. Activation of thrombin receptor resulted in phosphorylation of TRCD by TRAK in a Ca^<2+>-dependent way. In summary, our results provide evidence of a novel ligand-activated serine/threonine kinase that associates with the cytoplasmic domain of the thrombin receptor.
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