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Development of novel therapeutic options for treating heart failure targeting the myosin light chain

Research Project

Project/Area Number 13670689
Research Category

Grant-in-Aid for Scientific Research (C)

Allocation TypeSingle-year Grants
Section一般
Research Field Circulatory organs internal medicine
Research InstitutionThe University of Tokyo

Principal Investigator

YAMASHITA Hiroshi  University of Tokyo, Graduate School of Medicine, Reseach Associate, 医学部附属病院, 助手 (50323572)

Co-Investigator(Kenkyū-buntansha) SATA Masataka  University of Tokyo, Graduate School of Medicine, Reseach Associate, 医学部附属病院, 助手 (80345214)
SUGIURA Seiryo  University of Tokyo, Graduate School of Frontier Sciences, Professor, 大学院・新領域創成科学研究科, 教授 (10272551)
青柳 昭彦  東京大学, 医学部・附属病院, 助手 (10251240)
Project Period (FY) 2001 – 2002
Project Status Completed (Fiscal Year 2002)
Budget Amount *help
¥3,800,000 (Direct Cost: ¥3,800,000)
Fiscal Year 2002: ¥700,000 (Direct Cost: ¥700,000)
Fiscal Year 2001: ¥3,100,000 (Direct Cost: ¥3,100,000)
Keywordscardiac myosin / myosin light chain / in vitro motility assay / 筋収縮 / 分子生物学 / ミオシン / カルシウムイオン / アデノウイルス / カーボンファイバー / 心筋
Research Abstract

A myosin molecule consists of two heavy chains and two pairs of light chains and converts chemical energy of ATP hydrolysis into mechanical work of muscle contraction. The light chains are located close to the heavy chain head domain which contains ATP- and actin-binding sites essential for the motor function. To study functional roles of the myosin light chains, we purified two cardiac myosins with identical heavy chain and different light chains and compared the motor function of these myosins using in vitro motility assay techniques, where mechanical interaction of actin and myosin was reconstituted in vitro. Although catalytic activity showed no difference, motor function of these myosin molecules showed remarkable difference : the myosin molecules with ventricular-type light chains generated higher average force compared to those with atrial-type light chains and had longer duration of force-generating interaction with actin, suggesting that the myosin light chains may play an important role in converting the chemical energy into mechanical work. The unique nature of the myosin light chain modifying force-generating ability of the molecule without changing ATP hydrolysis rate may provide a clue to novel treatment for heart failure augmenting contractile function without increasing ATP consumption and protecting cardiac muscles from deterioration in energy metabolism.

Report

(3 results)
  • 2002 Annual Research Report   Final Research Report Summary
  • 2001 Annual Research Report
  • Research Products

    (11 results)

All Other

All Publications (11 results)

  • [Publications] 山下 尋史: "ミオシンモーターの力学特性"呼吸と循環. 50巻1号. 59-73 (2002)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      2002 Final Research Report Summary
  • [Publications] Yasuda S, Sugiura S, Kobayakawa N, Fujita H, Yamashita H, Katoh K, Saeki Y, Kaneko H, Suda Y, Nagai R, Sugi H: "A novel method to study contraction characteristics of a single cardiac myocyte using carbon fibers coupled with a feedback system"Am J Physiol. 281. H144-H1446 (2001)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      2002 Final Research Report Summary
  • [Publications] Saeki Y, Takigiku K, Iwamoto H, Yasuda S, Yamashita H, Sugiura S, Sugi H: "Protein kinase A increases the rate of relaxation but not the rate of tension development in skinned rat cardiac muscle"Jpn J Physiol. 21. 427-433 (2001)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      2002 Final Research Report Summary
  • [Publications] Yamashita H: "Motor function of myosin molecule"Kokyu to Junkan. 50. 59-73 (2002)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      2002 Final Research Report Summary
  • [Publications] Yasuda S, Sugiura S, Kobayakawa N, Fujita H, Yamashita H, Katoh K, Saeki Y, Kaneko H, Suda Y, Nagai R, and Sugi H: "A novel method to study contraction characteristics of a single cardiac myocyte using carbon fibers coupled with a feedback system"Am J Physiol. 281. H1442-1446 (2001)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      2002 Final Research Report Summary
  • [Publications] Saeki Y, Takigiku K, Iwamoto H, Yasuda S, Yamashita H, Sugiura S and Sugi H: "Protein kinase A increases the rate of relaxation but not the rate of tension development in skinned rat cardiac muscle"Jpn J Physiol. 51. 427-433 (2001)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      2002 Final Research Report Summary
  • [Publications] 山下 尋史: "ミオシンモーターの力学特性"呼吸と循環. 50巻1号. 59-73 (2002)

    • Related Report
      2002 Annual Research Report
  • [Publications] Yasuda S, Sugiura S, Kobayakawa N, Fujita H, Yamashita H, Katoh K, Saeki Y, Kaneko H, Suda Y, Nagai R, Sugi H: "A novel method to study contraction characteristics of a single cardiac myocyte using carbon fibers coupled with a feedback system"Am J Physiol. 281. H144-H1446 (2001)

    • Related Report
      2002 Annual Research Report
  • [Publications] Saeki Y, Takigiku K, Iwamoto H, Yasuda S, Yamashita H, Sugiura S, Sugi H: "Protein Kinase A increases the rate of relaxation but not the rate of tension development in skinned rat cardiac muscle"Jpn J Physiol. 21. 427-433 (2001)

    • Related Report
      2002 Annual Research Report
  • [Publications] 山下 尋史: "ミオシンモーターの力学特性"呼吸と循環. 50巻1号. 59-73 (2002)

    • Related Report
      2001 Annual Research Report
  • [Publications] 保田 壮一郎: "A novel method to study contraction characteristics of a single cardiac myocyte using carbon gibers"American Journal of Physiology. 281. H1442-H1446 (2001)

    • Related Report
      2001 Annual Research Report

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Published: 2001-04-01   Modified: 2016-04-21  

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