Sadayappan Sakthivel, de Tombe Pieter P
Department of Cell and Molecular Physiology, Stritch School of Medicine, Loyola University Chicago, 2160 South First Ave., Maywood, IL 60153, USA.
Biophys Rev. 2012 Jun 1;4(2):93-106. doi: 10.1007/s12551-012-0067-x.
Mutations of cardiac myosin binding protein-C (cMyBP-C) are inherited by an estimated 60 million people worldwide, and the protein is the target of several kinases. Recent evidence further suggests that cMyBP-C mutations alter Ca(2+) transients, leading to electrophysiological dysfunction. Thus, while the importance of studying this cardiac sarcomere protein is clear, preliminary data in the literature have raised many questions. Therefore, in this article, we propose to review the structure and function of cMyBP-C with particular respect to the role(s) in cardiac contractility and whether its release into the circulatory system is a potential biomarker of myocardial infarction. We also discuss future directions and experimental designs that may lead to expanding the role(s) of cMyBP-C in the heart. In conclusion, we suggest that cMyBP-C is a regulatory protein that could offer a broad clinical utility in maintaining normal cardiac function.
全世界估计有6000万人遗传了心肌肌球蛋白结合蛋白C（cMyBP-C）的突变，并且该蛋白是几种激酶的作用靶点。最近的证据进一步表明，cMyBP-C突变会改变Ca(2+)瞬变，导致电生理功能障碍。因此，虽然研究这种心肌肌节蛋白的重要性显而易见，但文献中的初步数据提出了许多问题。因此，在本文中，我们建议回顾cMyBP-C的结构和功能，特别关注其在心脏收缩性中的作用，以及它释放到循环系统中是否是心肌梗死的潜在生物标志物。我们还讨论了可能导致扩大cMyBP-C在心脏中作用的未来方向和实验设计。总之，我们认为cMyBP-C是一种调节蛋白，在维持正常心脏功能方面可能具有广泛的临床应用价值。
