Abstract
Calpains are Ca2+ -dependent thiol proteases which have been identified in various tissues of eucaryotes, but their physiological function in the cell is uncertain. In the muscle fiber, two types of calpains are present which differ by their calcium sensitivity: calpain 1 and calpain 2, which require for their activity micro and millimolar concentrations of calcium respectively. These calpains are associated with protein kinase C activities in the differentiated fiber. The multinucleate myotube is formed by fusion of mononucleated precursor cells, myoblasts. Calpains have been reported to appear in myoblasts at around the time of fusion. Moreover, an apparent synthesis of 1,2 diacylglycerol, an activator of protein kinase C, was observed during fusion of myoblasts. However, more information is required to incriminate totally protein kinase C and calpains in the mechanism of myoblast fusion.
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