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Characterization of tBid‐induced cytochrome c release from mitochondria and liposomes
Author(s) -
Zhai Dayong,
Huang Xingxu,
Han Xuehai,
Yang Fuyu
Publication year - 2000
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(00)01471-x
Subject(s) - cytochrome c , mitochondrion , chemistry , liposome , mitochondrial permeability transition pore , biochemistry , cytochrome , biophysics , microbiology and biotechnology , apoptosis , biology , enzyme , programmed cell death
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.