| Project/Area Number |
62480126
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| Research Category |
Grant-in-Aid for General Scientific Research (B)
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| Allocation Type | Single-year Grants |
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| Research Field |
General medical chemistry
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| Research Institution | Institute for Protein Research, Osaka University |
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Principal Investigator |
NAKAGAWA Hachiro Institute for Protein Research, Osaka University Professor, 蛋白質研究所, 教授 (20029937)
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| Co-Investigator(Kenkyū-buntansha) |
OKADA Masato Institute for Protein Research, Osaka University Research Assistant, 蛋白質研究所, 助手 (10177058)
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| Project Period (FY) |
1987 – 1988
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| Project Status |
Completed (Fiscal Year 1988)
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| Budget Amount *help |
¥5,700,000 (Direct Cost: ¥5,700,000)
Fiscal Year 1988: ¥1,500,000 (Direct Cost: ¥1,500,000)
Fiscal Year 1987: ¥4,200,000 (Direct Cost: ¥4,200,000)
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| Keywords | Protein tyrosine kinase / pp60^<c-src> / Protooncogene / pp60^<c-src> kinase / Phosphotyrosine protein phosphatase / Phosphotyrosyl protein phosphatase / 中枢神経系 / 分化・発育 / 蛋白質チロシンキナーゼ / 蛋白質チロシンホスファターゼ / インスリン受容体 / pp60^<c-src> / pp60^<c-src>Rinase / MAR-2 / 概日リズム / 神経分化 / インスリン / 自己りん酸化反応 / チロシンキナーゼ / プロテインチロシンホスファターゼ |
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| Research Abstract |
1. We identified three types of protein tyrosine kinase (PTK) in the membrane fraction of embryonal rat brain, and purified them separately. Two of these enzymes cross-reacted with the actiserum against pp60^<c-src>, an encoding product of protooncogene, src, whereas the third did not. The former two types were quite similar in their properties each other, identical to pp60^<c-src>. However, one of them occurred only in embryonic and neonatal stages, and thus it was named pp60^<nc-src>. The third one was found to phosphorylate Tyr-527 of pp60^<c-src> to inactivate it, demonstrating that it is pp60^<c-src> kinase. From the developmental changes that pp60<@1nc-src<@D1 and pp60<@D1c-src@>D1 kinase showed their maximal activities within a week after birth, it is suggested that they could be involved in the requlation of growth and differentiation of neuronal cells.
2. Four types of phosphotyrosine protein phosphatase (PTPpase) were isolated from the cytosolic fraction of rat brain, and highly purified respectively. Two of these enzymes are found only in the brain, and catalyzed the dephosphorylation of Tyr-527 of pp60^<c-src>, which induces the transforming activity.
3. We are now attempting preparation of poly- and monoclonal antibodies against PTKs and PTPPases. With these antibodies, we are going to examine how these enzymes are substantially involved in the differentiation and growth of neuronal cells.
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