心肌中肌动蛋白-肌球蛋白相互作用的特性取决于肌球蛋白的同工型，而非α-肌动蛋白的同工型。
The properties of the actin-myosin interaction in the heart muscle depend on the isoforms of myosin but not of α-actin.
作者信息
Kopylova G, Nabiev S, Nikitina L, Shchepkin D, Bershitsky S
机构信息
Institute of Immunology and Physiology, Russian Academy of Sciences, Yekaterinburg, 620049, Russia.
Institute of Immunology and Physiology, Russian Academy of Sciences, Yekaterinburg, 620049, Russia.
出版信息
Biochem Biophys Res Commun. 2016 Aug 5;476(4):648-653. doi: 10.1016/j.bbrc.2016.06.013. Epub 2016 Jun 3.
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.
在哺乳动物的心肌中，存在两种肌球蛋白重链亚型，即α和β。在心室中，它们与轻链的心室亚型一起形成两种同型肌球蛋白：V1和V3，分别是α重链和β重链的同二聚体。在心房中，α重链和β重链与心房轻链一起形成A1（αα）和A2（ββ）同型肌球蛋白。此外，在心肌中还表达了两种α-肌动蛋白亚型，即骨骼肌型和心脏型。我们假设心脏型和骨骼肌型肌动蛋白的氨基酸序列差异可能会影响其与肌球蛋白的相互作用。为了验证这一假设，我们使用光镊技术和体外运动分析方法，研究了心脏型α-肌动蛋白的心脏型和骨骼肌型亚型与心肌球蛋白亚型之间肌动蛋白-肌球蛋白相互作用的特性。结果发现，心肌球蛋白亚型与肌动蛋白相互作用的力学和动力学特性取决于肌球蛋白亚型，而非α-肌动蛋白亚型。
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