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

Qun Chen; Edward J Lesnefsky

doi:10.1016/j.bbadis.2015.08.004

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

Biochim Biophys Acta. 2015 Nov;1852(11):2372-8. doi: 10.1016/j.bbadis.2015.08.004. Epub 2015 Aug 7.

Authors

Qun Chen¹, Edward J Lesnefsky²

Affiliations

¹ Department of Medicine (Division of Cardiology, Pauley Heart Center), Virginia Commonwealth University, Richmond, VA 23298, United States. Electronic address: qchen8@vcu.edu.
² Department of Medicine (Division of Cardiology, Pauley Heart Center), Virginia Commonwealth University, Richmond, VA 23298, United States; Department of Biochemistry, Virginia Commonwealth University, Richmond, VA 23298, United States; Department of Physiology, Virginia Commonwealth University, Richmond, VA 23298, United States; McGuire VA Medical Center, Richmond, VA 23249, United States.

PMID: 26259540
DOI: 10.1016/j.bbadis.2015.08.004

Abstract

Calpain 1 is an ubiquitous Ca(2+)-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.

Keywords: Complex I; Heart failure; Ischemia–reperfusion; Mitochondrial permeability transition pore; Oxidative stress; p53.

Publication types

Review