Effect of Cardiac Myosin-Binding Protein C on Tropomyosin Regulation of Actin—Myosin Interaction Using In Vitro Motility Assay


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We studied the modulating role of cardiac myosin-binding protein C (cMyBP-C) in tropomyosin regulation of the actin—myosin interaction. The effect of cMyBP-C on the velocity of actin-tropomyosin filament sliding over cardiac and slow skeletal myosins was evaluated using in vitro motility assay. The effect of cMyBP-C on the actin-tropomyosin filaments sliding depended on the type of myosin. The regulatory effect of cMyBP-C differs for cardiac and slow skeletal myosin because of the presence of specific essential light chain (LC1sa) in slow skeletal myosin isoform.

作者简介

D. Shchepkin

Institute of Immunology and Physiology, Ural Division of the Russian Academy of Sciences

Email: l.nikitina@iip.uran.ru
俄罗斯联邦, Ekaterinburg

G. Kopylova

Institute of Immunology and Physiology, Ural Division of the Russian Academy of Sciences

Email: l.nikitina@iip.uran.ru
俄罗斯联邦, Ekaterinburg

L. Nikitina

Institute of Immunology and Physiology, Ural Division of the Russian Academy of Sciences

编辑信件的主要联系方式.
Email: l.nikitina@iip.uran.ru
俄罗斯联邦, Ekaterinburg


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