Study of regulatory effect of tropomyosin on actin-myosin interaction in skeletal muscle by in vitro motility assay |
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Authors: | G. V. Kopylova D. V. Shchepkin L. V. Nikitina |
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Affiliation: | 19728. Institute of Immunology and Physiology, Ural Division of the Russian Academy of Sciences, ul. Pervomaiskaya 91, 620041, Ekaterinburg, Russia
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Abstract: | The interaction between myosin and actin in striated muscle tissue is regulated by Ca2+ via thin filament regulatory proteins. Skeletal muscle possesses a whole pattern of myosin and tropomyosin isoforms. The regulatory effect of tropomyosin on actin-myosin interaction was investigated by measuring the sliding velocity of both actin and actin-tropomyosin filaments over fast and slow skeletal myosins using the in vitro motility assay. The actin-tropomyosin filaments were reconstructed with tropomyosin isoforms from striated muscle tissue. It was found that tropomyosins with different content of α-, β-, and γ-chains added to actin filaments affect the sliding velocity of filaments in different ways. On the other hand, the sliding velocity of filaments with the same content of α-, β-, and Γ-chains depends on myosin isoforms of striated muscle. The reciprocal effects of myosin and tropomyosin on actin-myosin interaction in striated muscle may play a significant role in maintenance of effective work of striated muscle both during ontogenesis and under pathological conditions. |
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