Premium
The mitochondrial permeability transition pore may comprise VDAC molecules
Author(s) -
Szabó Ildikó,
Pinto Vito De,
Zoratti Mario
Publication year - 1993
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 - 10.1016/0014-5793(93)80274-x
Subject(s) - voltage dependent anion channel , porin , mitochondrial permeability transition pore , biophysics , dimer , chemistry , permeability (electromagnetism) , nucleotide , mitochondrion , gating , adenine nucleotide , bacterial outer membrane , biochemistry , membrane , biology , programmed cell death , apoptosis , organic chemistry , escherichia coli , gene
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.