Subject(s)
Animals , Male , Mice , Apoptosis Inducing Factor/metabolism , Calpain/metabolism , Poly(ADP-ribose) Polymerases/physiology , Active Transport, Cell Nucleus/genetics , Apoptosis Inducing Factor/genetics , Cells, Cultured , Calpain/antagonists & inhibitors , Calpain/deficiency , Calpain/genetics , Cell Death/physiology , Enzyme Activation/genetics , Poly(ADP-ribose) Polymerases/geneticsABSTRACT
The number of mammalian calpain protease family members has grown as many as 15 till recent count. Although initially described as a cytosolic protease, calpains have now been found in almost all subcellular locations i.e., from mitochondria to endoplasmic reticulum and from caveolae to Golgi bodies. Importantly, some calpains do not possess the 28 kDa regulatory subunit and have only the 80 kDa catalytic subunit. In some instances, the 80 kDa subunit by itself confers the calpain proteolytic activity. Calpains have been shown to be involved in a number of physiological processes such as cell cycle progression, remodeling of cytoskeletal-cell membrane attachments, signal transduction, gene expression and apoptosis. Recent studies have linked calpain deficiencies or it’s over production with a variety of diseases, such as muscular dystrophies, gastropathy, diabetes, Alzheimer’s and Parkinson’s diseases, atherosclerosis and pulmonary hypertension. Herein, we present a brief overview on some implications of calpains on human health and some diseases.