Characterization of tBid‐induced cytochrome c release from mitochondria and liposomes

FEBS Letters

Zhai, Dayong¹  Han, Xuehai¹  Huang, Xingxu¹  Yang, Fuyu¹ 

[1] National Laboratory of Biomacromolecules, Institute of Biophysics, Academia Sinica, 15 Datun Road, Beijing 100101, China

关键词: Apoptosis;    Bid;    Cytochrome c release;    Mitochondrion;    Permeability transition pore;    Liposome;    Cyt. c;    cytochrome c;    PTP;    permeability transition pore;    CsA;    cyclosporin A;    ΔΨ;    transmembrane electric potential difference;    CCCP;    carbonyl-cyanide m-chlorophenyl-hydrazone;    AA;    antimycin A;    BAEE;    Nα-benzoyl-l-arginine ethyl ester;    LUV;    large unilamellar vesicle;    VDAC;    voltage-dependent anion channel;   

DOI  :  10.1016/S0014-5793(00)01471-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown