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Copper induces permeability transition through its interaction with the adenine nucleotide translocase
Author(s) -
García Noemí,
MartínezAbundis Eduardo,
Pavón Natalia,
Correa Francisco,
Chávez Edmundo
Publication year - 2007
Publication title -
cell biology international
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.932
H-Index - 77
eISSN - 1095-8355
pISSN - 1065-6995
DOI - 10.1016/j.cellbi.2007.02.003
Subject(s) - translocase , chemistry , mitochondrial permeability transition pore , biophysics , mitochondrion , efflux , inner mitochondrial membrane , permeability (electromagnetism) , swelling , copper , mitochondrial matrix , membrane , nucleotide , membrane potential , titration , biochemistry , biology , inorganic chemistry , cytosol , enzyme , chemical engineering , organic chemistry , apoptosis , chromosomal translocation , engineering , gene , programmed cell death
In this work we examined the effect of low concentrations of Cu 2+ on the opening of the mitochondrial non‐specific pore. The purpose was addressed to further contribute to the knowledge of the mechanisms that regulate the open/closed cycles of the permeability transition pore. Membrane leakage was established by measuring matrix Ca 2+ efflux and mitochondrial swelling. The experimental results indicate that Cu 2+ at very low concentrations promoted the release of accumulated Ca 2+ , as well as mitochondrial swelling, provided 1,10‐phenanthroline has been added. Carboxyatractyloside and Cu 2+ exhibited additive effects on these parameters. After Cu 2+ titration of membrane thiols, it might be assumed that the blockage of 5.9 nmol of SH/mg protein suffices to open the non‐specific pore. Taking into account the reinforcing effect of carboxyatractyloside, the increasing ADP concentrations, and that N ‐ethylmaleimide inhibited the Cu 2+ ‐induced Ca 2+ efflux, it is proposed that the target site for Cu 2+ is located in the ADP/ATP carrier.