Abstract
The members of ICE/CED3 family of cysteine proteases (caspases) play important roles in the regulation of programmed cell death. Recent studies have revealed that processing and activation of CPP32 (CASP-3) are crucial for executing cell death in TNF-α- and Fas-induced apoptosis. Overexpression of Bcl-2 in HeLa cells inhibits the cell death and CASP-3 like protease activities which are induced by TNF-α or anti-Fas antibody. Preform of CASP-3 disappered after the treatment with TNF-α or anti-Fas antibody in both HeLa cells and HeLa/bcl-2 cells. These results suggest Bcl-2 prevents cell death and activation of CASP-3 but does not inhibit initial processing of CASP-3.
| Original language | English |
|---|---|
| Pages (from-to) | 405-411 |
| Number of pages | 7 |
| Journal | Biomedical Research |
| Volume | 18 |
| Issue number | 6 |
| DOIs | |
| Publication status | Published - 1997 Dec |
| Externally published | Yes |
ASJC Scopus subject areas
- Biochemistry, Genetics and Molecular Biology(all)
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Shiraiwa, N., Okano, H., & Miura, M. (1997). Bcl-2 prevents TNF- and Fas-induced cell death but does not inhibit initial processing of caspase-3. Biomedical Research, 18(6), 405-411. https://doi.org/10.2220/biomedres.18.405