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Molecular physiological study of contractile element of failing heart

Research Project

Project/Area Number 06454285
Research Category

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

Allocation TypeSingle-year Grants
Research Field Circulatory organs internal medicine
Research InstitutionUniversity of Tokyo General

Principal Investigator

MOMOURA Shin-ichi (1995)  University of Tokyo, Faculty of Medicine, Assistant Professor, 医学部(病), 助手 (10190985)

芹澤 剛 (1994)  東京大学, 医学部(病), 講師 (90143429)

Co-Investigator(Kenkyū-buntansha) AOYAGI Teruhiko  University of Tokyo, Faculty of Medicine, Assistant Professor, 医学部(病), 助手 (10251240)
TAKAHASHI Toshiuyki  University of Tokyo, Faculty of Medicine, Assistant Professor, 医学部(病), 助手 (40236302)
池ノ内 浩  東京大学, 医学部(病), 助手
百村 伸一  東京大学, 医学部(病), 助手 (10190985)
Project Period (FY) 1994 – 1995
Project Status Completed (Fiscal Year 1995)
Budget Amount *help
¥6,700,000 (Direct Cost: ¥6,700,000)
Fiscal Year 1995: ¥1,000,000 (Direct Cost: ¥1,000,000)
Fiscal Year 1994: ¥5,700,000 (Direct Cost: ¥5,700,000)
Keywordsin vitro motility asaay / laser optical trap / centrifuge microscope / cardiac myosin / regulatory protein / 不全心
Research Abstract

1. We have shown that catlytic products of ATP,ADP and Pi, have an inhibitory action on actomyosin sliding in vitro, This result suggests that cardac myosin is more resistant to ischemia than skeletal one. I intact muscle, ATP regenerating system provides optimal condition for ATP hydrolysis by myosin.
2. In vitro sliding of thin filament reconstituted from actin and troponin-tropomyosin complex was regulated by calcium concentration. Calcium sensitivity was reduced under various conditions such as acidosis and hypothermia, but reversed by calcium sensitizer. This effect of calcium sensitizer seemed to be mediated by regulatory protein.
3. We compared the force generating ability of cardiac myosin isoforms (V1 and V3) using two different in vitro force measuring systems, centrifuge microscope and laser optical trap. The two isoforms had different kinetic properties, but had similar force generating ability.

Report

(3 results)
  • 1995 Annual Research Report   Final Research Report Summary
  • 1994 Annual Research Report
  • Research Products

    (21 results)

All Other

All Publications (21 results)

  • [Publications] Yamashita H et al: "ADP inhibits the sliding velocity of fluorescent actin filaments on cardiac and skeletal myosins." Circ Res. 74. 1027-1033 (1994)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      1995 Final Research Report Summary
  • [Publications] Sata M et al.: "A new in vitro motility assay technique to evaluate calcium sensitivity of the cardiac contractile proteins." Pflugers Arch. 429. 443-445 (1995)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      1995 Final Research Report Summary
  • [Publications] Sata M et al.: "MCI-154increases Ca^<2+>sensitivity of reconstituted thin filament A study using a novel i vitro motility assay technique" Circ Res. 76. 626-633 (1995)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      1995 Final Research Report Summary
  • [Publications] Sugiura S et al.: "Force-velocity relations of rat cardiac myosin isozymens sliding on algal cell actin cables in vitro." Biophys Biochim Acta. 1231. 69-75 (1995)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      1995 Final Research Report Summary
  • [Publications] Sata M et al: "Pimobendan directly sensitizes reconstituted thin filament to slide on cardiac myosin" Eur J Pharmacol. 290. 55-59 (1995)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      1995 Final Research Report Summary
  • [Publications] Sata M et al.: "Phosphocreatine shuttle provides optimal condition for mechanical interaction of cardiac actomyosin." Circulation. 93. 310-317 (1995)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      1995 Final Research Report Summary
  • [Publications] Yamahita H,Sata M,Sugiura S,Momomura S,Serizawa T,Iizuka M: "ADP inhibits the sliding velocity of fluorescent actin filaments on cardiac and skeletl myosins." Circ Res. 74. 1027-1033 (1994)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      1995 Final Research Report Summary
  • [Publications] Sata M,Yamashita H,Sugiura S,Fujita H,momomura S,Seirzawa T: "A new in vitro motility assay technique to evaluate calcium sensitivity of the cardiac contractile proteins" Pflugers Arch. 429. 443-445 (1995)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      1995 Final Research Report Summary
  • [Publications] Sata M,Sugiura S,Yamashita H,Fujita H,Momomura S,Serizawa T: "MCI-154 increases Ca2+sensitivity of reconstituted thin filament A study using a novel in vitro motility assay technique" Circ Res. 76. 626-633 (1995)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      1995 Final Research Report Summary
  • [Publications] Sugiura S,Yamashita H,Sata M,Momomura S,Serizawa T,Oiwa K,Chaen S,Shimmen T,Sugi H.: "Force-velocity relations of rat cardiac myosin isozymes sliding on algal cell actin cables in vitro." Biophys Biochim Acta. 1231. 69-75 (1995)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      1995 Final Research Report Summary
  • [Publications] Sata M,Sugiura S,Yamashita H,Aoyagi T,Momomura S,Serizawa T: "Pimobendan directly sensitizes reconstituted thin filament to slide on cardiac myosin" Eur J Pharmacol. 290. 55-59 (1995)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      1995 Final Research Report Summary
  • [Publications] Sata M,Sugiura S,Yamashita H,Fujita H,Momomura S,Serizawa T: "Phosphocreatine shuttle provides optimal condition for mechanical interaction of cardiac actomyosin." Circulation. 93. 310-317 (1995)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      1995 Final Research Report Summary
  • [Publications] Yamashita H.et al.: "ADP inhibits the sliding velocity of fluorescent actin filaments on cardiac and skeletal myosins." Circ Res. 74. 1027-1033 (1994)

    • Related Report
      1995 Annual Research Report
  • [Publications] Sata M.et al.: "A new in vitro motility assay technique to evaluate calcium sensitivity of the cardiac contractile proteins." Pflugers Arch. 429. 443-445 (1995)

    • Related Report
      1995 Annual Research Report
  • [Publications] Sata M.et al.: "MCI-154 increases Ca^<2+> sensitivity of reconstituted thin filament A study using a novel in vitro motility assay technique" Circ Res. 76. 626-633 (1995)

    • Related Report
      1995 Annual Research Report
  • [Publications] Sugiura S.et al.: "Force-velocity relations of rat cardiac myosin isozymes sliding on algal cell actin cables in vitro" Biophys Biochim Acta. 1231. 69-75 (1995)

    • Related Report
      1995 Annual Research Report
  • [Publications] Sata M.et al.: "Pimobendan directly sensitizes reconstituted thin filament to slide on cardiac myosin" Eur J Pharmacol. 290. 55-59 (1995)

    • Related Report
      1995 Annual Research Report
  • [Publications] Sata M.et al.: "Phosphocreatine shuttle provides optimal condition for mechanical interaction of cardiac actomyosin." Circulation. 93. 310-317 (1995)

    • Related Report
      1995 Annual Research Report
  • [Publications] Hiroshi Yamashita: "ADP inhibits sliding velocity of fluorescent actin filament on cardiac and skeletal myosins" Circulation Research. 74. 1027-1033 (1994)

    • Related Report
      1994 Annual Research Report
  • [Publications] Masataka Sata: "A new in vitro motility assay technique to evaluate calcium sensitivity of the cardiac contractile proteins." Pfliigers Arch. 429. 443-445 (1995)

    • Related Report
      1994 Annual Research Report
  • [Publications] Masataka Sata: "MCI-154 increases Ca^<2+> sensitivity of reconstituted thin filament.A study using a novel in vitro motility assay technique" Circulation Research. (in press).

    • Related Report
      1994 Annual Research Report

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Published: 1994-04-01   Modified: 2016-04-21  

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