Kinase activities associated with calcium-activated neutral proteases.
Studies on the phosphorylation of calcium-activated neutral protease (CANP) revealed the presence of kinase activities closely associated with purified CANP preparations. The kinase activity in uCANP (CANP with high affinity for calcium) was cAMP-independent whereas the kinase activity in mCANP (CANP with low affinity for calcium) was cAMP-dependent, inhibited by kinase specific inhibitor and abolished when the mCANP was preincubated in calcium. The CANP-associated kinase(s) phosphorylate uCANP and mCANP , causing modulation of their proteolytic activities.
D000818:Animals; D002154:Calpain; D002846:Chromatography, Affinity; D000242:Cyclic AMP / Q000502:physiology; D003600:Cytosol / Q000201:enzymology; D010450:Endopeptidases / Q000378:metabolism*; D004789:Enzyme Activation; D009132:Muscles / Q000201:enzymology*; D010766:Phosphorylation; D010770:Phosphotransferases / Q000378:metabolism*; D051381:Rats
D000242:Cyclic AMP; D010770:Phosphotransferases; D010450:Endopeptidases; D002154:Calpain