Calpains are a group of calcium-sensitive cysteine proteases that are ubiquitously expressed in mammals. This family contains 14 members with μ-calpain (calpain 1) and m-calpain (calpain 2) being the most well-characterized. Structurally, calpains contain two subunits; an 80 kDa catalytic subunit and a 28 kDa regulatory subunit that functions as a chaperone to stabilize the 80 kDa structure.
Calpains are regulated by Ca2+ concentration, phosphorylation, calpastatin and probably by altering their subcellular localization (limiting access to substrate). These endopeptidases have numerous functions including, but not limited to, remodeling of cytoskeletal attachments to the plasma membrane during cell fusion and cell motility, proteolytic modification of molecules in signal transduction pathways, degradation of enzymes controlling progression through the cell cycle, regulation of gene expression, substrate degradation in some apoptotic pathways, and an involvement in long-term potentiation.
Perturbations in calpain activity have been associated in pathophysiological processes contributing to type II diabetes (calpain 10), Alzheimer's disease (calpain 1), gastric cancer (calpain 9) and muscular dystrophy (calpain 3).View all products for Calpains »
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Literature for Calpains
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July 8 - 12, 2017