Cleavage of caspase family members by granzyme B: a comparative study in vitro
Details
Serval ID
serval:BIB_FDBAD5447EAC
Type
Article: article from journal or magazin.
Collection
Publications
Institution
Title
Cleavage of caspase family members by granzyme B: a comparative study in vitro
Journal
European Journal of Immunology
ISSN
0014-2980 (Print)
Publication state
Published
Issued date
05/1997
Volume
27
Number
5
Pages
1296-9
Notes
Comparative Study
Journal Article
Research Support, Non-U.S. Gov't --- Old month value: May
Journal Article
Research Support, Non-U.S. Gov't --- Old month value: May
Abstract
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.
Keywords
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
Create date
24/01/2008 16:19
Last modification date
20/08/2019 17:28