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

  • Ruth M. Kluck
    Division of Cellular Immunology, La Jolla Institute for Allergy and Immunology, 10355 Science Park Drive, San Diego, CA 92121, USA.
  • Ella Bossy-Wetzel
    Division of Cellular Immunology, La Jolla Institute for Allergy and Immunology, 10355 Science Park Drive, San Diego, CA 92121, USA.
  • Douglas R. Green
    Division of Cellular Immunology, La Jolla Institute for Allergy and Immunology, 10355 Science Park Drive, San Diego, CA 92121, USA.
  • Donald D. Newmeyer
    Division of Cellular Immunology, La Jolla Institute for Allergy and Immunology, 10355 Science Park Drive, San Diego, CA 92121, USA.

抄録

<jats:p>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.</jats:p>

収録刊行物

  • Science

    Science 275 (5303), 1132-1136, 1997-02-21

    American Association for the Advancement of Science (AAAS)

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