Bcl-2 prevents TNF- and Fas-induced cell death but does not inhibit initial processing of caspase-3

Nobuko Shiraiwa, Hideyuki Okano, Masayuki Miura

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8 Citations (Scopus)


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 languageEnglish
Pages (from-to)405-411
Number of pages7
JournalBiomedical Research
Issue number6
Publication statusPublished - 1997 Dec


ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)

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