| Project/Area Number |
61304068
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| Research Category |
Grant-in-Aid for Co-operative Research (A)
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| Allocation Type | Single-year Grants |
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| Research Field |
分子遺伝学・分子生理学
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| Research Institution | Kyushu University |
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Principal Investigator |
OHTSUKI Iwao Kyushu University, Faculty of Medicine, Professor, 医学部, 教授 (70009992)
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| Co-Investigator(Kenkyū-buntansha) |
TAKAHASHI Koui Hokkaido University, Faculty of Agriculture, Assoc. Professor, 農学部, 助教授 (40001432)
MASAKI Tomoo Tsukuba University, Faculty of Medicine, Professor, 基礎医学系, 教授 (60009991)
YAMADA Kazuhiro Ooita Medical University, Professor, 教授 (20053027)
OBINATA Takashi Chiba University, Faculty of Science, Professor, 理学部, 教授 (40012413)
MARUYAMA Koscack Chiba University, Faculty of Science, Professor, 理学部, 教授 (60012267)
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| Project Period (FY) |
1986 – 1988
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| Project Status |
Completed (Fiscal Year 1988)
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| Budget Amount *help |
¥16,600,000 (Direct Cost: ¥16,600,000)
Fiscal Year 1988: ¥2,000,000 (Direct Cost: ¥2,000,000)
Fiscal Year 1987: ¥7,000,000 (Direct Cost: ¥7,000,000)
Fiscal Year 1986: ¥7,600,000 (Direct Cost: ¥7,600,000)
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| Keywords | Muscle / Muscle contraction / Calcium regulatory proteins / Cytoskeletal proteins / Skeletal muscle / 平滑筋 / トロポニン / トロポミオシン / コネクチン / αーアクチニン / α-アクチニン |
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| Research Abstract |
Structure and function of regulatory and cytoskeletal proteins of muscle were investigated with special reference to the role at physiological conditions as follows.
(1) Ca-regulatory proteins of striated muscle. CDTA-treated myofibrils was proved to be suitable for the research on the physiological role of troponin C in contractile response. Binding of four Ca^<2+> ions to troponin C molecule in the thin filament was found necessary for the activation of myofibrillar ATPase activity. Calorimetry of frog skeletal troponin C was carried out.
(2) Cytoskeletal proteins. Localization of connectin in relation to striation patterns was investigated by immunoelectron microscopy. It was found that connectin in A band is less extensible than that in I-band. Connectin filament itself was visualized electron microscopically in the myofibrils treated with gelsolin. Preparative procedures for paratropomyosin was also investigated.
(3) Structural regulatory proteins. Primary structure of -actinin molecules from smooth muscle and embryonic skeletal muscle was determined by the examining cDNA. Regulatory proteins of actin polymerization in chick embryonic muscle was investigated.
(4) Regulatory proteins of smooth muscle. Preparative procedure of natural actomyosin and the method for desensitization of natural actomyosin have been established successfully. Using this protein preparation properties of Ca^<2+> sensitizing protein such as leiotonin were investigated. Study was carried out on the proteins regulating the length of actin filament.
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