钙激活中性蛋白酶及其内源性抑制剂。在细胞膜上的激活及生物学功能。

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

作者信息

Suzuki K, Imajoh S, Emori Y, Kawasaki H, Minami Y, Ohno S

出版信息

FEBS Lett. 1987 Aug 17;220(2):271-7. doi: 10.1016/0014-5793(87)80828-1.

Abstract

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.

摘要

最近阐明的钙激活中性蛋白酶（CANP）及其内源性抑制剂的结构揭示了它们在结构-功能关系和酶活性调节方面的新特征。该蛋白酶被认为是一种前体酶，在Ca2+和磷脂存在的情况下可在细胞膜上被激活，并可能通过有限的蛋白水解作用调节蛋白质的功能，尤其是与膜相关的蛋白质。蛋白激酶C在细胞膜上被CANP水解并激活为不依赖辅因子的形式。本文对这些结果进行了综述，并讨论了CANP可能参与信号转导的情况。