Phosphorylation of bovine cardiac calcium-activated neutral protease by protein kinase-C.
Protein kinase C prepared from rat brain was used to phosphorylate a calcium-activated neutral protease, purified from bovine cardiac muscle. Attempts to phosphorylate the enzyme in the presence of calcium were unsuccessful, unless the protease inhibitor leupeptin was also present. Phosphorylation of the 74K subunit of the protease was completely inhibited in the absence of phosphatidylserine and diolein, indicating that phosphorylation of the enzyme was catalysed by the calcium and phospholipid-dependent protein kinase C.
D000818:Animals; D002154:Calpain / Q000378:metabolism*; D002417:Cattle; D004789:Enzyme Activation; D007976:Leupeptins / Q000494:pharmacology; D046911:Macromolecular Substances; D008970:Molecular Weight; D009206:Myocardium / Q000201:enzymology; D010766:Phosphorylation; D010769:Phosphothreonine / Q000378:metabolism; D011493:Protein Kinase C / Q000378:metabolism*
D007976:Leupeptins; D046911:Macromolecular Substances; D010769:Phosphothreonine; D011493:Protein Kinase C; D002154:Calpain; C032854:leupeptin