The mitochondrial permeability transition pore may comprise VDAC molecules

FEBS Letters

Pinto, Vito De¹  Zoratti, Mario²  Szabó, Ildikó² 

[1] Department of Pharmaco-Biology, CNR Unit for Mitochondria and Bioenergetics, Bari, Italy;CNR Unit for the Physiology of Mitochondria, Department of Exp. Biomedical Sciences, Via Trieste 75, 35121 Padova, Italy

关键词: Permeability transition;    Patch-clamp;    VDAC;    Porin;    Mitochondrial channel;    Rat liver mitochondria;    pS;    picoSiemens;    nS;    nanoSiemens;    MMC;    mitochon-drial megachannel;    PT;    permeability transition;    PTP;    permeability transition pore;    VDAC;    voltage-dependent anion channel (mitochon-drial porin);    ADC;    adenine nucleotide carrier;    mBzR;    mitochondrial benzodiazepine receptor;    HEPES;    4-(2-hydroxyethyl)-1-piperazi-neethanesulfonic acid;   

DOI  :  10.1016/0014-5793(93)80274-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The electrophysiological properties of isolated mitochondrial porin (VDAC), reconstituted in planar bilayers or proteoliposomes, resemble those of the mitochondrial megachannel believed to be the permeability transition pore. In particular, a correspondence was found with regard to the voltage dependence: VDAC was driven to closed states by potentials of either sign, but the effect was not symmetrical; voltages negative in the compartment to which VDAC was added were more effective. The results are consistent with the hypothesis that the FTP may consist of two cooperating VDAC channels, plus presumably an adenine nucleotide carrier dimer and a third component known to be part of the mitochondrial benzodiazepine receptor.

【 授权许可】

Unknown