The Release of Cytochrome c from Mitochondria: A Primary Site for Bcl-2 Regulation of Apoptosis

Author:

Kluck Ruth M.1,Bossy-Wetzel Ella1,Green Douglas R.1,Newmeyer Donald D.1

Affiliation:

1. Division of Cellular Immunology, La Jolla Institute for Allergy and Immunology, 10355 Science Park Drive, San Diego, CA 92121, USA.

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.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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