Effects of cardiac myosin binding protein-C on the regulation of interaction of cardiac myosin with thin filament in an in vitro motility assay |
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Authors: | D.V. Shchepkin G.V. Kopylova L.V. Nikitina L.B. Katsnelson S.Y. Bershitsky |
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Affiliation: | Institute of Immunology and Physiology, Russian Academy of Sciences, Yekaterinburg 620041, Russia |
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Abstract: | Modulatory role of whole cardiac myosin binding protein-C (сMyBP-C) in regulation of cardiac muscle contractility was studied in the in vitro motility assay with rabbit cardiac myosin as a motor protein. The effects of cMyBP-C on the interaction of cardiac myosin with regulated thin filament were tested in both in vitro motility and ATPase assays. We demonstrate that the addition of cMyBP-C increases calcium regulated Mg-ATPase activity of cardiac myosin at submaximal calcium. The Hill coefficient for ‘pCa-velocity’ relation in the in vitro motility assay decreased and the calcium sensitivity increased when сMyBP-C was added. Results of our experiments testifies in favor of the hypothesis that сMyBP-C slows down cross-bridge kinetics when binding to actin. |
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Keywords: | Cardiac myosin Cardiac myosin binding protein-C In vitro motility assay |
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