Characterization of tBid-induced cytochrome c release from mitochondria and liposomes.
tBid, the cleaved form of Bid, can induce cytochrome c (Cyt. c) release from rat heart mitochondria more efficiently and reproducibly than that from liver or brain mitochondria. Unlike Bax, such release was not prevented by cyclosphorin A, an inhibitor of the opening of permeability transition pore. Carbonyl-cyanide m-chlorophenyl-hydrazone or oligomycin also have no obvious effect on the release of Cyt. c. In contrast to ceramide, tBid-mediated Cyt. c release from mitochondria is independent of the redox state of Cyt. c. Furthermore, Bid or tBid can directly trigger the efflux of encapsulated Cyt. c or trypsin within liposomes without involvement of other protein factors.
Zhai
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National Laboratory of Biomacromolecules, Institute of Biophysics, Academia Sinica, 15 Datun Road, Beijing, China.
Huang
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Han
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Yang
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D000818:Animals; D051023:BH3 Interacting Domain Death Agonist Protein; D001921:Brain / Q000378:metabolism; D002352:Carrier Proteins / Q000378:metabolism*; D003574:Cytochrome c Group / Q000378:metabolism*; D005260:Female; D005615:Freezing; D006801:Humans; D008081:Liposomes / Q000378:metabolism; D008929:Mitochondria, Heart / Q000378:metabolism*; D008930:Mitochondria, Liver / Q000378:metabolism*; D010084:Oxidation-Reduction; D051381:Rats
D051023:BH3 Interacting Domain Death Agonist Protein; C494814:BID protein, human; C494816:Bid protein, rat; D002352:Carrier Proteins; D003574:Cytochrome c Group; D008081:Liposomes