doi: 10.1126/science.275.5303.1132.
The release of cytochrome c from mitochondria: a primary site for Bcl-2 regulation of apoptosis
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- PMID: 9027315
- DOI: 10.1126/science.275.5303.1132
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The release of cytochrome c from mitochondria: a primary site for Bcl-2 regulation of apoptosis
Science.
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Abstract
In a cell-free apoptosis system, mitochondria spontaneously released cytochrome c, which activated DEVD-specific caspases, leading to fodrin cleavage and apoptotic nuclear morphology. Bcl-2 acted in situ on mitochondria to prevent the release of cytochrome c and thus caspase activation. During apoptosis in intact cells, cytochrome c translocation was similarly blocked by Bcl-2 but not by a caspase inhibitor, zVAD-fmk. In vitro, exogenous cytochrome c bypassed the inhibitory effect of Bcl-2. Cytochrome c release was unaccompanied by changes in mitochondrial membrane potential. Thus, Bcl-2 acts to inhibit cytochrome c translocation, thereby blocking caspase activation and the apoptotic process.
Comment in
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Controlling cell death.Science. 1997 Feb 21;275(5303):1081-2. doi: 10.1126/science.275.5303.1081. Science. 1997. PMID: 9054009 No abstract available.
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