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Conversion of Bcl-2 to a Bax-like Death Effector by Caspases
Abstract
Caspases are a family of cysteine proteases implicated in the biochemical and morphological changes that occur during apoptosis (programmed cell death). The loop domain of Bcl-2 is cleaved at Asp 34 by caspase-3 (CPP32) in vitro, in cells overexpressing caspase-3, and after induction of apoptosis by Fas ligation and interleukin-3 withdrawal. The carboxyl-terminal Bcl-2 cleavage product triggered cell death and accelerated Sindbis virus–induced apoptosis, which was dependent on the BH3 homology and transmembrane domains of Bcl-2. Inhibitor studies indicated that cleavage of Bcl-2 may further activate downstream caspases and contribute to amplification of the caspase cascade. Cleavage-resistant mutants of Bcl-2 had increased protection from interleukin-3 withdrawal and Sindbis virus–induced apoptosis. Thus, cleavage of Bcl-2 by caspases may ensure the inevitability of cell death.
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Metadata
- Authors
- Cheng, E. H.-Y., Kirsch, D. G., Clem, R. J., Ravi, R., Kastan, M. B., Bedi, A., Ueno, K., & Hardwick, J. M.
- Venue
- Science
- Published
- 1997-12-12
- Volume
- 278
- Issue
- 5345
- Pages
- 1966-1968
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2092759765
- Cited by
- 1,107
- References
- 0
- FWCI
- 33.64
- Type
- journal article
- Language
- en
- Open access
- closed
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