Mechanism of action of a new component of the Ca2+-dependent proteolytic system in rat brain:: The calpain activator

被引：29

作者：

Melloni, E ^{[1
]}

Michetti, M ^{[1
]}

Salamino, F ^{[1
]}

Sparatore, B ^{[1
]}

Pontremoli, S ^{[1
]}

机构：

[1] Univ Genoa, Inst Biol Chem, I-16132 Genoa, Italy

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1998年 / 249卷 / 03期

关键词：

D O I：

10.1006/bbrc.1998.9200

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Rat brain contains a calpain activator specific for the mu-form of the proteinase. We now report that this protein factor binds to the catalytic 80 kDa calpain subunit, promoting the dissociation of the heterodimer structure of the proteinase. The successive steps of the activation process, namely the two autoproteolytic steps producing the 78 kDa and the 75 kDa calpain forms, result in a 100 times faster rate. The activator competes with calpastatin and associates with the inner surface of plasma membranes. Based on its properties, the calpain activator can be visualised as the molecule indicating the sites for calpain activation at which the proteinase can also elude the negative control exerted by calpastatin. (C) 1998 Academic Press.

引用

页码：583 / 588

页数：6

共 30 条

[1] STRUCTURAL MODIFICATIONS ASSOCIATED WITH THE CHANGE IN CA2+ SENSITIVITY ON ACTIVATION OF M-CALPAIN [J].