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  • Title: The properties of the actin-myosin interaction in the heart muscle depend on the isoforms of myosin but not of α-actin.
    Author: Kopylova G, Nabiev S, Nikitina L, Shchepkin D, Bershitsky S.
    Journal: Biochem Biophys Res Commun; 2016 Aug 05; 476(4):648-653. PubMed ID: 27264951.
    Abstract:
    In myocardium of mammals there are two isoforms of myosin heavy chains, α and β. In ventricle, together with ventricular isoforms of light chains they form two isomyosins: V1 and V3, homodimers of α- and β-heavy chains, respectively. In atria, α- and β-heavy chains together with atrial light chains form A1 (αα) and A2 (ββ) isomyosins. Besides in myocardium two isoforms of α-actin, skeletal and cardiac, are expressed. We assume that the differences in the amino acid sequence of cardiac and skeletal actin may affect its interaction with myosin. To test this hypothesis, we investigated characteristics of actin-myosin interactions of cardiac and skeletal isoforms of α-actin with the isoforms of cardiac myosin using an optical trap technique and an in vitro motility assay. It was found that the mechanical and kinetic characteristics of the interactions of the isoforms of cardiac myosin with actin depend on the isoforms of myosin not α-actin.
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