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 |
| Publication status | Published - 1997 Dec |
| Externally published | Yes |
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ASJC Scopus subject areas
- Biochemistry, Genetics and Molecular Biology(all)
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Bcl-2 prevents TNF- and Fas-induced cell death but does not inhibit initial processing of caspase-3. / Shiraiwa, Nobuko; Okano, Hideyuki; Miura, Masayuki.
In: Biomedical Research, Vol. 18, No. 6, 12.1997, p. 405-411.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Bcl-2 prevents TNF- and Fas-induced cell death but does not inhibit initial processing of caspase-3
AU - Shiraiwa, Nobuko
AU - Okano, Hideyuki
AU - Miura, Masayuki
PY - 1997/12
Y1 - 1997/12
N2 - 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.
AB - 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.
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UR - http://www.scopus.com/inward/citedby.url?scp=0031425807&partnerID=8YFLogxK
M3 - Article
AN - SCOPUS:0031425807
VL - 18
SP - 405
EP - 411
JO - Biomedical Research (Japan)
JF - Biomedical Research (Japan)
SN - 0388-6107
IS - 6
ER -