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Calpain is known to play a variety of cellular functions in various cells by Ca2(+)-dependent limited proteolysis. Protein kinase C (PK-C) is a key enzyme in signal transduction. It is known that treatment of a cell with 12-0-tetradecanoylphorbol 13-acetate (TPA) causes down-regulation of PK-C, and that calpain can cleave PK-C into catalytic and regulatory fragments in vitro. In vivo involvement of calpain in down-regulation of PK-C was studied with neuroblastoma cells using various drugs, a synthetic peptide fragment of calpastatin and inhibitors against calpain. TPA-dependent down-regulation of PK-C was partially inhibited by pre-treatment with calpastatin peptide and inhibitors, suggesting in vivo involvement of calpain in down-regulation of PK-C during signal transduction.
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