Calcium‐activated neutral protease and its endogenous inhibitor Activation at the cell membrane and biological function

[摘要]

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.

[学科分类] 生物化学/生物物理

[关键词] Ca2+-dependent protease;Enzyme inhibitor;Proenzyme activation;Protein kinase C;CANP;calcium-activated neutral protease. The terms calpain;calcium-dependent protease (CDP);and calcium-activated protease (CAP) are also used. To denote the two isozymes;I and II are sometimes used in place of μ and m;respectively. Calpastatin is another name for the CANP inhibitor