Effects of Sarcomere Length and Ca^<2+> Binding on SH Reactivity of Myofilament Bound Troponin C in Porcine Skinned Cardiac Muscle Fibers

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Author(s)

Abstract

Length dependence of cardiac Ca<sup>2+</sup> activation is an essential component of the Frank-Starling relation. The aim of this study is to examine the length effects on the Ca<sup>2+</sup>-induced conformational changes of filament-bound cTnC in skinned cardiac muscle fibers. The two cysteine residues (Cys-35 and Cys-84) in the regulatory domain of cTnC allow for the attachment of conformational probes to this region. Their incorporation with the fluorescent probe, 7-diethylamino-3-[4′-maleimidylphenyl]-4-methylcoumarin (CPM), was used to determine the varying cTnC conformations in cardiac fibers. The data obtained show that the length-dependent Ca<sup>2+</sup>-mediated conformational changes require strong-binding cross-bridges for cardiac activation.<br>

Journal

  • The Japanese Journal of Physiology

    The Japanese Journal of Physiology 51(3), 385-388, 2001-06

    THE PHYSIOLOGICAL SOCIETY OF JAPAN

References:  18

Codes

  • NII Article ID (NAID)
    10008293959
  • NII NACSIS-CAT ID (NCID)
    AA00691224
  • Text Lang
    ENG
  • Article Type
    SHO
  • ISSN
    0021521X
  • NDL Article ID
    5840358
  • NDL Source Classification
    ZS8(科学技術--医学--解剖学・生理学・生化学)
  • NDL Call No.
    Z53-D40
  • Data Source
    CJP  NDL  J-STAGE 
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