Cleavage of caspase family members by granzyme B: a comparative study in vitro

Détails

ID Serval
serval:BIB_FDBAD5447EAC
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Institution
Titre
Cleavage of caspase family members by granzyme B: a comparative study in vitro
Périodique
European Journal of Immunology
Auteur(s)
Van de Craen  M., Van den Brande  I., Declercq  W., Irmler  M., Beyaert  R., Tschopp  J., Fiers  W., Vandenabeele  P.
ISSN
0014-2980 (Print)
Statut éditorial
Publié
Date de publication
05/1997
Volume
27
Numéro
5
Pages
1296-9
Notes
Comparative Study
Journal Article
Research Support, Non-U.S. Gov't --- Old month value: May
Résumé
The aspartase granzyme B is one of the major components of the granules involved in cell killing by cytotoxic T lymphocytes. Granzyme B has been shown to activate the apoptotic death pathway in the target cell, and this involves activation of members of the caspase (CASP) protein family. Therefore, activational cleavage of mouse (m) CASP proforms by granzyme B was examined in vitro. CASP can be subdivided in the CASP-1 (interleukin-1 beta-converting enzyme; ICE) subfamily, the CASP-2 (Ich1) subfamily, and the CASP-3 (CPP32) subfamily. Our results reveal that the proforms of the CASP-3 subfamily members mCASP-3 and mCASP-7 are hydrolyzed by granzyme B, while proforms of CASP-2 and CASP-1 subfamily members are not directly cleaved. Only one CASP-3 subfamily member, pro-mCASP-6, was not proteolytically cleaved by granzyme B. These results indicate that two members of the CASP-3 subfamily, but no others, become activated by granzyme B.
Mots-clé
Animals Caspase 1 Caspase 2 Caspase 3 *Caspases Cysteine Endopeptidases/genetics/metabolism Enzyme Precursors/genetics/metabolism Granzymes Hydrolysis Mice Protein Biosynthesis Proteins/genetics/metabolism Serine Endopeptidases/*metabolism Transcription, Genetic
Pubmed
Web of science
Création de la notice
24/01/2008 16:19
Dernière modification de la notice
20/08/2019 17:28
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