Effect of ADP/ATP antiporter conformational state on the suppression of the nonspecific permeability of the inner mitochondrial membrane by cyclosporine A

FEBS Letters

Zorov, Dmitry B.¹  Kushnareva, Yulia E.¹  Novgorodov, Sergey A.¹  Kudrjashov, Yury B.²  Gudz, Tatjana I.² 

[1] A.N. Belozersky Laboratory, M.V. Lomonosov Moscow State University, Department of Biophysics, Moscow, USSR;Biological Faculty, M.V. Lomonosov Moscow State University, Department of Biophysics, Moscow, USSR

关键词: Mitochondria;    Nonspecific permeability;    Cyclosporine A;    ADP/ATP antiporter;    ΔΨ;    mitochondrial inner-membrane potential;    TPP +;    tetraphenylphosphonium;    RLM;    rat liver mitochondria;    CATR;    Carboxyatractiloside;    CSA;    cyclosporine A;    PhAsO;    phenylarsine oxide;   

DOI  :  10.1016/0014-5793(90)80824-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The influence of the conformational state of ADP/ATP antiporter on the efficiency of the inhibitory effect of cyclosporine A on the Ca²⁺-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.

【 授权许可】

Unknown