Elastic filaments in skeletal muscle revealed by selective removal of thin filaments with plasma gelsolin

Takashi Funatsu*, Hideo Higuchi, Shin'ichi Ishiwata

*この研究の対応する著者

    研究成果査読

    113 被引用数 (Scopus)

    抄録

    Muscle needs an elastic framework to maintain its mechanical stability. Removal of thin filaments in rabbit skeletal muscle with plasma gelsolin has revealed the essential features of elastic filaments. The selective removal of thin filaments was confirmed by staining with phalloidin-rhodamine for fluorescence microscopy, examination of arrowhead formation with myosin subfragment 1 by electron microscopy, and analysis by SDS-PAGE. Thin section electron microscopy revealed the elastic fine filaments (∼4 nm in diameter) connecting thick filaments and the Z line. After removal of thin filaments, both rigor stiffness and active tension generation were lost, but the resting tension remained. These observations indicate that the thin filament-free fibers maintain a framework composed of the serial connections of thick filaments, the elastic filaments, and the Z line, which gives passive elasticity to the contractile system of skeletal muscle. The resting tension that remained in the thin filament-free fibers was decreased by mild trypsin treatment. The only protein component that was digested in parallel with the decrease in the resting tension and the disappearance of the elastic filaments was α-connectin (also called titin 1), which was transformed from the α to the β form (from titin 1 to 2, respectively). Thus, we conclude that the main protein component of the elastic filaments is α-connectin (titin 1).

    本文言語English
    ページ(範囲)53-62
    ページ数10
    ジャーナルJournal of Cell Biology
    110
    1
    出版ステータスPublished - 1990 1

    ASJC Scopus subject areas

    • 細胞生物学

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