Calcium-activated neutral protease and its endogenous inhibitor. Activation at the cell membrane and biological function.
The structures of calcium-activated neutral protease (CANP) and its endogenous inhibitor elucidated recently have revealed novel features with respect to their structure-function relationship and enzyme activity regulation. The protease is regarded as a proenzyme which can be activated at the cell membrane in the presence of Ca2+ and phospholipid, and presumably regulates the functions of proteins, especially membrane-associated proteins, by limited proteolysis. Protein kinase C is hydrolysed and activated by CANP at the cell membrane to a cofactor-independent form. These results are reviewed and the possible involvement of CANP in signal transduction is discussed.
D000818:Animals; D002118:Calcium / Q000502:physiology*; D002154:Calpain / Q000037:antagonists & inhibitors / Q000502:physiology*; D002462:Cell Membrane / Q000201:enzymology; D004789:Enzyme Activation; D006801:Humans; D007527:Isoenzymes / Q000502:physiology; D011493:Protein Kinase C / Q000502:physiology*
D007527:Isoenzymes; D011493:Protein Kinase C; D002154:Calpain; D002118:Calcium