Heart mitochondria and calpain 1: Location, function, and targets

被引：33

作者：

Chen, Qun ^{[1
]}

Lesnefsky, Edward J. ^{[1
,2
,3
,4
]}

机构：

[1] Virginia Commonwealth Univ, Dept Med, Div Cardiol, Pauley Heart Ctr, Richmond, VA 23298 USA

[2] Virginia Commonwealth Univ, Dept Biochem, Richmond, VA 23298 USA

[3] Virginia Commonwealth Univ, Dept Physiol, Richmond, VA 23298 USA

[4] McGuire VA Med Ctr, Richmond, VA 23249 USA

来源：

BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR BASIS OF DISEASE | 2015年 / 1852卷 / 11期

关键词：

Mitochondrial permeability transition pore; Complex I; Ischemia-reperfusion; p53; Heart failure; Oxidative stress; ISCHEMIA-REPERFUSION; PERMEABILITY TRANSITION; CELL-DEATH; OXIDATIVE STRESS; CYTOCHROME-C; MU-CALPAIN; CARNITINE PALMITOYLTRANSFERASE; INTRACELLULAR ACIDOSIS; MYOCARDIAL-INFARCTION; NA+/K+-ATPASE;

D O I：

10.1016/j.bbadis.2015.08.004

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Calpain 1 is an ubiquitous Ca2+-dependent cysteine protease. Although calpain 1 has been found in cardiac mitochondria, the exact location within mitochondrial compartments and its function remain unclear. The aim of the current review is to discuss the localization of calpain 1 in different mitochondrial compartments in relationship to its function, especially in pathophysiological conditions. Briefly, mitochondrial calpain 1 (mit-CPN1) is located within the intermembrane space and mitochondrial matrix. Activation of the mit-CPN1 within intermembrane space cleaves apoptosis inducing factor (AIF), whereas the activated mit-CPN1 within matrix cleaves complex I subunits and metabolic enzymes. Inhibition of the mit-CPN1 could be a potential strategy to decrease cardiac injury during ischemia-reperfusion. (C) 2015 Elsevier B.V. All rights reserved.

引用

页码：2372 / 2378

页数：7

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