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J Cell Biol 2000 Sep 04;1505:1027-36. doi: 10.1083/jcb.150.5.1027.
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Preservation of mitochondrial structure and function after Bid- or Bax-mediated cytochrome c release.

von Ahsen O , Renken C , Perkins G , Kluck RM , Bossy-Wetzel E , Newmeyer DD .

Proapoptotic members of the Bcl-2 protein family, including Bid and Bax, can activate apoptosis by directly interacting with mitochondria to cause cytochrome c translocation from the intermembrane space into the cytoplasm, thereby triggering Apaf-1-mediated caspase activation. Under some circumstances, when caspase activation is blocked, cells can recover from cytochrome c translocation; this suggests that apoptotic mitochondria may not always suffer catastrophic damage arising from the process of cytochrome c release. We now show that recombinant Bid and Bax cause complete cytochrome c loss from isolated mitochondria in vitro, but preserve the ultrastructure and protein import function of mitochondria, which depend on inner membrane polarization. We also demonstrate that, if caspases are inhibited, mitochondrial protein import function is retained in UV-irradiated or staurosporine-treated cells, despite the complete translocation of cytochrome c. Thus, Bid and Bax act only on the outer membrane, and lesions in the inner membrane occurring during apoptosis are shown to be secondary caspase-dependent events.

PubMed ID: 10973993
PMC ID: PMC2175243
Article link: J Cell Biol
Grant support: [+]

Species referenced: Xenopus laevis
Genes referenced: actl6a apaf1 bax bcl2 bid mib1

Article Images: [+] show captions
References [+] :
Bossy-Wetzel, Mitochondrial cytochrome c release in apoptosis occurs upstream of DEVD-specific caspase activation and independently of mitochondrial transmembrane depolarization. 1998, Pubmed