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Effect of ADP/ATP antiporter conformational state on the suppression of the nonspecific permeability of the inner mitochondrial membrane by cyclosporine A
Author(s) -
Novgorodov Sergey A.,
Gudz Tatjana I.,
Kushnareva Yulia E.,
Zorov Dmitry B.,
Kudrjashov Yury B.
Publication year - 1990
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(90)80824-3
Subject(s) - antiporter , phenylarsine oxide , chemistry , biophysics , mitochondrion , inner mitochondrial membrane , inner membrane , permeability (electromagnetism) , atp–adp translocase , nucleotide , biochemistry , reagent , membrane potential , membrane , biology , enzyme , gene
The influence of the conformational state of ADP/ATP antiporter on the efficiency of the inhibitory effect of cyclosporine A on the Ca 2+ ‐induced nonspecific permeability of the inner mitochondrial membrane has been studied. Carboxyatractiloside, the inhibitor of ADP/ATP‐antiporter, was shown to prevent the cyclosporine A‐induced suppression of the nonspecific permeability. The Carboxyatractiloside enect was displayed only in mitochondria depleted of adenine nucleotides. Bifunctional SH reagent, phenylarsine oxide, was also able to reverse the effect of cyclosporine A. The data are consistent with the suggestion that cyclosporine A causes suppression of the nonspecific permeability due to its effect on the ADP/ATP antiporter conformation.