采用体外运动分析研究肌球蛋白和原肌球蛋白异构体对肌动球蛋白相互作用的相互影响。

Study of reciprocal effects of cardiac myosin and tropomyosin isoforms on actin-myosin interaction with in vitro motility assay.

机构信息

Institute of Immunology and Physiology, Russian Academy of Sciences, Yekaterinburg 620041, Russia.

出版信息

Biochem Biophys Res Commun. 2011 Nov 11;415(1):104-8. doi: 10.1016/j.bbrc.2011.10.022. Epub 2011 Oct 12.

DOI:10.1016/j.bbrc.2011.10.022

PMID:22020102

Abstract

Interaction of myosin with actin in striated muscle is controlled by Ca(2+) via thin filament associated proteins: troponin and tropomyosin. In cardiac muscle there is a whole pattern of myosin and tropomyosin isoforms. The aim of the current work is to study regulatory effect of tropomyosin on sliding velocity of actin filaments in the in vitro motility assay over cardiac isomyosins. It was found that tropomyosins of different content of α- and β-chains being added to actin filament effects the sliding velocity of filaments in different ways. On the other hand the velocity of filaments with the same tropomyosins depends on both heavy and light chains isoforms of cardiac myosin.

摘要

在横纹肌中，肌球蛋白与肌动蛋白的相互作用受 Ca(2+) 通过细丝相关蛋白：肌钙蛋白和原肌球蛋白的控制。在心肌中有一整套肌球蛋白和原肌球蛋白同工型。目前这项工作的目的是研究原肌球蛋白对体外运动分析中不同心脏肌球蛋白的肌动蛋白丝滑动速度的调节作用。结果发现，加入肌动蛋白丝的具有不同 α-和 β-链含量的原肌球蛋白以不同的方式影响纤维丝的滑动速度。另一方面，具有相同原肌球蛋白的纤维丝的速度取决于心脏肌球蛋白的重链和轻链同工型。