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Calpains are a class of proteins that belong to the calcium-dependent, non-lysosomal cysteine proteases. There are three major types of calpains expressed in the skeletal muscle, namely, μ-calpain, m-calpain, and calpain 3, which show proteolytic activities. Skeletal muscle fibers possess all three calpains, and they are Ca2+-dependent proteases. The functional role of calpains was found to be associated with apoptosis and myogenesis. However, calpain 3 is likely to be involved in sarcomeric remodeling. A defect in the expression of calpain 3 leads to limb-girdle muscular dystrophy type 2A. Calpain 3 is found in skeletal muscle fibers at the N2A line of the large elastic protein, titin. A substantial proportion of calpain 3 is activated 24 h following a single bout of eccentric exercise. In vitro studies indicated that calpain 3 can be activated 2-4 fold higher than normal resting cytoplasmic [Ca2+]. Characterization of the calpain system in the developing muscle is essential to explain which calpain isoforms are present and whether both μ-calpain and m-calpain exist in differentiating myoblasts. Information from such studies is needed to clarify the role of the calpain system in skeletal muscle growth. It has been demonstrated that the activation of ubiquitous calpains and calpain 3 in skeletal muscle is very well regulated in the presence of huge and rapid changes in intracellular [Ca2+].