Activation of pro-caspase-7 by serine proteases includes a non-canonical specificity

被引：116

作者：

Zhou, Q ^{[1
]}

Salvesen, GS ^{[1
]}

机构：

[1] BURNHAM INST,PROGRAM AGING & CELL DEATH RES,SAN DIEGO,CA 92037

来源：

BIOCHEMICAL JOURNAL | 1997年 / 324卷

关键词：

D O I：

10.1042/bj3240361

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：

As a model to investigate the mechanism of caspase activation we have analysed the processing of pro-caspase-7 by serine proteases with varied specificities. The caspase-7 zymogen was rapidly activated by granzyme B and more slowly by subtilisin and cathepsin G, generating active enzymes with similar kinetic properties. Significantly, cathepsin G activated the zymogen by cleaving at a Gln-Ala bond, indicating that the canonical cleavage specificity at aspartic acid is not required for activation.

引用

页码：361 / 364

页数：4

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