Email this article Effect of Cardiac Myosin-Binding Protein C on Tropomyosin Regulation of Actin—Myosin Interaction Using In Vitro Motility Assay
- Authors: Shchepkin D.V.1, Kopylova G.V.1, Nikitina L.V.1
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Affiliations:
- Institute of Immunology and Physiology, Ural Division of the Russian Academy of Sciences
- Issue: Vol 162, No 1 (2016)
- Pages: 45-47
- Section: Article
- URL: https://journals.rcsi.science/0007-4888/article/view/237890
- DOI: https://doi.org/10.1007/s10517-016-3541-9
- ID: 237890
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Abstract
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.
About the authors
D. V. Shchepkin
Institute of Immunology and Physiology, Ural Division of the Russian Academy of Sciences
Email: l.nikitina@iip.uran.ru
Russian Federation, Ekaterinburg
G. V. Kopylova
Institute of Immunology and Physiology, Ural Division of the Russian Academy of Sciences
Email: l.nikitina@iip.uran.ru
Russian Federation, Ekaterinburg
L. V. Nikitina
Institute of Immunology and Physiology, Ural Division of the Russian Academy of Sciences
Author for correspondence.
Email: l.nikitina@iip.uran.ru
Russian Federation, Ekaterinburg
