| Project/Area Number |
03556040
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| Research Category |
Grant-in-Aid for Developmental Scientific Research (B)
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| Allocation Type | Single-year Grants |
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| Research Field |
基礎獣医学
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| Research Institution | The University of Tokyo |
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Principal Investigator |
KARAKI Hideaki Univ.Tokyo Fac.Agr Prof., 農学部, 教授 (60011912)
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| Co-Investigator(Kenkyū-buntansha) |
MAGAE Junji Tokyo Institute Department of Technology of Bioengineering Associate Prof., 生命理工学部, 講師 (60199643)
SHIOTA Kunio Univ.Tokyo Fac.Agr Associate Prof., 農学部, 助教授 (80196352)
FUSETANI Nobuhiro Univ.Tokyo Fac.Agr Prof., 農学部, 教授 (70012010)
HON Masatoshi Univ.Tokyo Fac.Agr Assistant Prof., 農学部, 助手 (70211547)
OZAKI Hiroshi Univ.Tokyo Fac.Agr Associate Prof., 農学部, 助教授 (30134505)
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| Project Period (FY) |
1991 – 1993
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| Project Status |
Completed (Fiscal Year 1993)
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| Budget Amount *help |
¥16,300,000 (Direct Cost: ¥16,300,000)
Fiscal Year 1993: ¥4,600,000 (Direct Cost: ¥4,600,000)
Fiscal Year 1992: ¥4,800,000 (Direct Cost: ¥4,800,000)
Fiscal Year 1991: ¥6,900,000 (Direct Cost: ¥6,900,000)
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| Keywords | phosphatase / smooth muscle / ion channel / cytoskeleton / ホスファターゼ / 平滑筋 / 海産毒 / ホスファタ-ゼ |
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| Research Abstract |
It was known that there are four phosphatase inhibitors, such as okadaic acid, calyculin-A, tautomycin and microcystin-LR.At first, we investigated the effects of these compounds on various types of phosphatase acitivities. okadaic acid and microcystin-LR selectively inhibited type 2A phosphatase purified from bovine cardiac muscle at low concentration. At high concentration, however, these compounds also inhibited type 1 phosphatase purified from turkey gizzard. In contrast, calyculin-A and tautomycin nonselectively inhibited type 1 and type 2A phosphatase. These compounds did not affect on type 2B and 2C phosphatases.
We inivestigated the physiological role of phosphatase on contractile elements, ion channels and cell structure, and clarified that the regulatory phosphatase of contractile elements may have type 1 like characterization for phosphatase inhibitors in smooth muscle, and that calyculin-A may facilitate the opening of the L-type Ca channels through the protein kinase C-dependent phosphorylation system in smooth muscle cells of guinea-pig taenia coli and that the changes in cytoskeletal structure may be caused by disturbing the balance of phosphorylation and dephosphorylation in the culured A10 cells.
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