高分子量钙调蛋白结合蛋白在心脏损伤中的潜在作用。
Potential role of high molecular weight calmodulin-binding protein in cardiac injury.
作者信息
Shrivastav Anuraag, Sharma Rajendra K
机构信息
Department of Pathology and Laboratory Medicine, College of Medicine, University of Saskatchewan, and Cancer Research Centre, Saskatchewan Cancer Agency, Saskatoon, Saskatchewan.
出版信息
Int J Angiol. 2009 Winter;18(4):161-6. doi: 10.1055/s-0031-1278346.
Ca(2+) is a major determinant of many biochemical processes in various cell types and is a critical second messenger in cell signalling. High molecular weight calmodulin-binding protein (HMWCaMBP) was originally discovered and purified in the authors' laboratory. It was identified as a homologue of calpastatin - an inhibitor of Ca(2+)-activated cysteine proteases (calpains). Decreased expression of HMWCaMBP in ischemia suggests that it is proteolyzed by calpains during ischemia and reperfusion. In normal myocardial muscle, HMWCaMBP may protect its substrate from calpains, but during an early stage of ischemia/reperfusion with increased Ca(2+) influx, calpain activity exceeds HMWCaMBP activity, leading to proteolysis of HMWCaMBP and other protein substrates, resulting in cellular damage. The role of HMWCaMBP in ischemia/reperfusion is yet to be explored. The present review summarizes developments from the authors' laboratory in the area of HMWCaMBP.
钙离子（Ca(2+)）是多种细胞类型中许多生化过程的主要决定因素，也是细胞信号传导中的关键第二信使。高分子量钙调蛋白结合蛋白（HMWCaMBP）最初是在作者的实验室中发现并纯化的。它被鉴定为钙蛋白酶抑制蛋白的同源物，钙蛋白酶抑制蛋白是一种Ca(2+)激活的半胱氨酸蛋白酶（钙蛋白酶）的抑制剂。缺血时HMWCaMBP表达降低表明它在缺血和再灌注期间被钙蛋白酶水解。在正常心肌中，HMWCaMBP可能保护其底物免受钙蛋白酶的作用，但在缺血/再灌注早期，随着Ca(2+)内流增加，钙蛋白酶活性超过HMWCaMBP活性，导致HMWCaMBP和其他蛋白质底物的蛋白水解，从而造成细胞损伤。HMWCaMBP在缺血/再灌注中的作用尚待探索。本综述总结了作者实验室在HMWCaMBP领域的研究进展。
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