Carol C. Gregorio and Velia M. Fowler are at the Department of Cell Biology, The Scripps Research Institute, La Jolla, California 92037, USA.
Trends Cardiovasc Med. 1996 May;6(4):136-41. doi: 10.1016/1050-1738(96)00022-9.
The regulation of thin filament length is a fundamental property of all striated muscles. Tropomodulin is an actin and tropomyosin binding protein that is exclusively associated with the free (pointed) ends of thin filaments. In vitro and in vivo studies reveal that tropomodulin is an actin filament pointed end capping protein, which is required to maintain the final length of thin filaments and is essential for contractile activity in embryonic chick cardiac myocytes. Understanding the mechanisms of thin filament assembly, as well as determining the roles of proteins modulating actin filament dynamics, is important for future considerations of the molecular bases for myopathies seen in various types of heart disease.
细肌丝长度的调节是所有横纹肌的基本特性。原肌球蛋白是一种肌动蛋白和原肌球蛋白结合蛋白，它只与细肌丝的游离（尖端）末端结合。体外和体内研究表明，原肌球蛋白是一种肌动蛋白丝尖端末端封闭蛋白，它对于维持细肌丝的最终长度是必需的，对于鸡胚心肌细胞的收缩活性也是必需的。了解细肌丝组装的机制，以及确定调节肌动蛋白丝动力学的蛋白质的作用，对于未来考虑各种类型心脏病中所见的肌病的分子基础是重要的。
