ACTIVATION OF PRO-CASPASE-7 BY SERINE PROTEASES INCLUDES A NONCANONICAL SPECIFICITY

Authors
ZHOU Q SALVESEN GS
Citation
Q. Zhou et Gs. Salvesen, ACTIVATION OF PRO-CASPASE-7 BY SERINE PROTEASES INCLUDES A NONCANONICAL SPECIFICITY, Biochemical journal, 324, 1997, pp. 361-364
Citations number
30
Categorie Soggetti
Biology
Journal title
Biochemical journal → ACNP
ISSN journal
02646021
Volume
324
Year of publication
1997
Part
2
Pages
361 - 364
Database
ISI
SICI code
0264-6021(1997)324:<361:AOPBSP>2.0.ZU;2-1
Abstract
As a model to investigate the mechanism of caspase activation we have analysed the processing of pro-caspase-7 by serine proteases with vari ed specificities. The caspase-7 zymogen was rapidly activated by granz yme B and more slowly by subtilisin and cathepsin G, generating active enzymes with similar kinetic properties. Significantly, cathepsin G a ctivated the zymogen by cleaving at a Gln-Ala bond, indicating that th e canonical cleavage specificity at aspartic acid is not required for activation.