Document Detail

Evidence against a functional site for Bcl-2 downstream of caspase cascade in preventing apoptosis.
MedLine Citation:
PMID:  9365238     Owner:  NLM     Status:  MEDLINE    
Apoptotic cell death is driven by ICE family proteases (caspases) and negatively regulated by Bcl-2 family proteins. Although it has been shown that Bcl-2 exerts anti-apoptotic activity by blocking a step(s) leading to the activation of caspases, a role for Bcl-2 and Bcl-xL downstream of the caspase cascade has remained unclear. Here, we show that purified active caspase-3 (CPP32/Yama/apopain) and caspase-1 (ICE) induces apoptosis when microinjected into the cytoplasm of cells, confirming our recent observations, and that the apoptosis is not at all prevented by Bcl-2 and Bcl-xL, which are overexpressed more than sufficiently to prevent Fas-mediated and overexpressed procaspase-1-mediated apoptosis. Thus, Bcl-2 and Bcl-xL do not act downstream of the caspase cascade.
N Yasuhara; S Sahara; S Kamada; Y Eguchi; Y Tsujimoto
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Oncogene     Volume:  15     ISSN:  0950-9232     ISO Abbreviation:  Oncogene     Publication Date:  1997 Oct 
Date Detail:
Created Date:  1997-12-04     Completed Date:  1997-12-04     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  8711562     Medline TA:  Oncogene     Country:  ENGLAND    
Other Details:
Languages:  eng     Pagination:  1921-8     Citation Subset:  IM    
Department of Medical Genetics, Biomedical Research Center, Osaka University Medical School, Suita, Japan.
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MeSH Terms
Cysteine Endopeptidases / metabolism*
Cytoplasm / metabolism
Enzyme Precursors / metabolism
Hela Cells
Proto-Oncogene Proteins c-bcl-2 / metabolism*
Reg. No./Substance:
0/Enzyme Precursors; 0/Proto-Oncogene Proteins c-bcl-2; EC 3.4.22.-/Cysteine Endopeptidases

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