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PMID: 9182691 Published · ppublish English Comparative Study Journal Article

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

The Biochemical journal ·Vol. 324 ( Pt 2) ·1997-06-01 ·Pages 361-4

Zhou Q, Salvesen GS

Abstract

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.

MeSH Terms
Amino Acid Sequence Caspase 7 Caspases Cathepsin G Cathepsins/metabolism Chymotrypsin/metabolism Cysteine Endopeptidases/genetics,metabolism DNA, Complementary/genetics Enzyme Activation Enzyme Precursors/genetics,metabolism Granzymes Humans Protein Sorting Signals/metabolism Recombinant Fusion Proteins/metabolism Serine Endopeptidases/metabolism Substrate Specificity Subtilisins/metabolism Trypsin/metabolism
Chemicals
DNA, Complementary Enzyme Precursors Protein Sorting Signals Recombinant Fusion Proteins Cathepsins GZMB protein, human Granzymes Serine Endopeptidases Subtilisins Chymotrypsin CTSG protein, human Cathepsin G Trypsin CASP7 protein, human Caspase 7 Caspases Cysteine Endopeptidases
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Zhou Q
Program in Aging and Cell Death Research, The Burnham Institute, San Diego, CA 92037, USA.
Salvesen G S
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Article Info
Journal
The Biochemical journal
Abbr.
Biochem J
ISSN
0264-6021
DOI
10.1042/bj3240361
Published
1997-06-01
Pages
361-4
Language
English
Region
England
NLM ID
2984726R
PMCID
PMC1218439
Subset
IM
External Links
PubMed source DOI: 10.1042/bj3240361 PMC Full Text View journal details
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