Effect of Cardiac Myosin-Binding Protein C on Tropomyosin Regulation of Actin—Myosin Interaction Using In Vitro Motility Assay
- Autores: Shchepkin D.1, Kopylova G.1, Nikitina L.1
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Afiliações:
- Institute of Immunology and Physiology, Ural Division of the Russian Academy of Sciences
- Edição: Volume 162, Nº 1 (2016)
- Páginas: 45-47
- Seção: 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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Resumo
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.
Sobre autores
D. Shchepkin
Institute of Immunology and Physiology, Ural Division of the Russian Academy of Sciences
Email: l.nikitina@iip.uran.ru
Rússia, Ekaterinburg
G. Kopylova
Institute of Immunology and Physiology, Ural Division of the Russian Academy of Sciences
Email: l.nikitina@iip.uran.ru
Rússia, Ekaterinburg
L. Nikitina
Institute of Immunology and Physiology, Ural Division of the Russian Academy of Sciences
Autor responsável pela correspondência
Email: l.nikitina@iip.uran.ru
Rússia, Ekaterinburg
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