Accumulated strain mechanism for length determination of thick filaments in skeletal muscle. I. Experimental bases

Hideo Higuchi, Takashi Funatsu, Akihiko Ishijima, Nobuyuki Okamura, Shin'ichi Ishiwata

    Research output: Contribution to journalArticle

    4 Citations (Scopus)

    Abstract

    The kinetics of dissociation of myosin from both ends of thick filaments in glycerinated skeletal muscle fibres and myofibrils was studied in the presence of MgATP by use of an optical diffraction method and phase-contrast microscopy. The dissociation velocity, v (=-d L/d t where L is the length of thick filaments at time t), increased with increasing KCl concentration (0.225 to 0.5 m), or increasing pH (6.5 to 8.0) but hardly changed with temperature (5 and 25° C), micromolar concentrations of Ca2+ or sarcomere length (2.4 and 2.75 μm). Over a wide range of filament length, the dissociation velocity could be expressed by v0exp(αL), where v0 and α are positive constants depending upon the dissociation condition. When the effects of crossbridge formation are minimized it was thus shown that the structural stability of thick filaments in a muscle fibre and a myofibril gradually decreases from the central part to the tips of the filaments. On the basis of these results we propose that the length of thick filaments is largely regulated by an accumulated strain mechanism in which the free energy of association of myosin molecules increases with filament length.

    Original languageEnglish
    Pages (from-to)491-500
    Number of pages10
    JournalJournal of Muscle Research and Cell Motility
    Volume7
    Issue number6
    DOIs
    Publication statusPublished - 1986 Dec

    Fingerprint

    Myofibrils
    Myosins
    Muscle
    Skeletal Muscle
    Free Association
    Phase-Contrast Microscopy
    Sarcomeres
    Skeletal Muscle Fibers
    Adenosine Triphosphate
    Muscles
    Temperature
    Fibers
    Free energy
    Microscopic examination
    Diffraction
    Association reactions
    Molecules
    Kinetics

    ASJC Scopus subject areas

    • Physiology
    • Endocrinology
    • Clinical Biochemistry
    • Cell Biology

    Cite this

    Accumulated strain mechanism for length determination of thick filaments in skeletal muscle. I. Experimental bases. / Higuchi, Hideo; Funatsu, Takashi; Ishijima, Akihiko; Okamura, Nobuyuki; Ishiwata, Shin'ichi.

    In: Journal of Muscle Research and Cell Motility, Vol. 7, No. 6, 12.1986, p. 491-500.

    Research output: Contribution to journalArticle

    Higuchi, Hideo ; Funatsu, Takashi ; Ishijima, Akihiko ; Okamura, Nobuyuki ; Ishiwata, Shin'ichi. / Accumulated strain mechanism for length determination of thick filaments in skeletal muscle. I. Experimental bases. In: Journal of Muscle Research and Cell Motility. 1986 ; Vol. 7, No. 6. pp. 491-500.
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    abstract = "The kinetics of dissociation of myosin from both ends of thick filaments in glycerinated skeletal muscle fibres and myofibrils was studied in the presence of MgATP by use of an optical diffraction method and phase-contrast microscopy. The dissociation velocity, v (=-d L/d t where L is the length of thick filaments at time t), increased with increasing KCl concentration (0.225 to 0.5 m), or increasing pH (6.5 to 8.0) but hardly changed with temperature (5 and 25° C), micromolar concentrations of Ca2+ or sarcomere length (2.4 and 2.75 μm). Over a wide range of filament length, the dissociation velocity could be expressed by v0exp(αL), where v0 and α are positive constants depending upon the dissociation condition. When the effects of crossbridge formation are minimized it was thus shown that the structural stability of thick filaments in a muscle fibre and a myofibril gradually decreases from the central part to the tips of the filaments. On the basis of these results we propose that the length of thick filaments is largely regulated by an accumulated strain mechanism in which the free energy of association of myosin molecules increases with filament length.",
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    AU - Funatsu, Takashi

    AU - Ishijima, Akihiko

    AU - Okamura, Nobuyuki

    AU - Ishiwata, Shin'ichi

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    N2 - The kinetics of dissociation of myosin from both ends of thick filaments in glycerinated skeletal muscle fibres and myofibrils was studied in the presence of MgATP by use of an optical diffraction method and phase-contrast microscopy. The dissociation velocity, v (=-d L/d t where L is the length of thick filaments at time t), increased with increasing KCl concentration (0.225 to 0.5 m), or increasing pH (6.5 to 8.0) but hardly changed with temperature (5 and 25° C), micromolar concentrations of Ca2+ or sarcomere length (2.4 and 2.75 μm). Over a wide range of filament length, the dissociation velocity could be expressed by v0exp(αL), where v0 and α are positive constants depending upon the dissociation condition. When the effects of crossbridge formation are minimized it was thus shown that the structural stability of thick filaments in a muscle fibre and a myofibril gradually decreases from the central part to the tips of the filaments. On the basis of these results we propose that the length of thick filaments is largely regulated by an accumulated strain mechanism in which the free energy of association of myosin molecules increases with filament length.

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