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.