title: The mitochondrial permeability transition pore may comprise VDAC molecules. II. The electrophysiological properties of VDAC are compatible with those of the mitochondrial megachannel.
abstract: 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 PTP 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.
authors.affiliation: CNR Unit for the Physiology of Mitochondria, Department of Exp. Biomedical Sciences, Padova, Italy.
authors.forename: I
authors.initials: I
authors.lastname: Szabó
authors.forename: V
authors.initials: V
authors.lastname: De Pinto
authors.forename: M
authors.initials: M
authors.lastname: Zoratti
mesh_terms: D000818:Animals; D007425:Intracellular Membranes / Q000502:physiology; D007473:Ion Channels / Q000502:physiology*; D008564:Membrane Potentials; D008565:Membrane Proteins / Q000502:physiology*; D008930:Mitochondria, Liver / Q000502:physiology*; D018272:Porins; D011510:Proteolipids; D051381:Rats; D050994:Voltage-Dependent Anion Channels
chemical_list: D007473:Ion Channels; D008565:Membrane Proteins; D018272:Porins; D011510:Proteolipids; D050994:Voltage-Dependent Anion Channels; C020485:proteoliposomes