Closure of Ca2+-dependent pores by cyclosporin A: the role of magnesium ions, adenine nucleotides, and conformation status of the ADP/ATP antiporter | Zakrytie CA2+-zavisimoǐ pory tsiklosporinom A: rol' ionov magniia, adeninovykh nukleotidov i konformatsionnogo sostoianiia ADP/ATP-antiportera. Academic Article uri icon

Overview

MeSH Major

  • Adenine Nucleotides
  • Calcium
  • Cyclosporine
  • Magnesium
  • Mitochondrial ADP, ATP Translocases

abstract

  • Effects of ADP and Mg2+ on the ability of cyclosporin A to "reseal" mitochondria permeabilized by Ca2+ and P(i) have been studied. Cyclosporin A was completely ineffective, when ADP and Mg2+ were not included into the incubation medium. Both ADP and Mg2+ used at high concentrations potentiated the effect of cyclosporin A and prevented it reversal by carboxyatractylate. Data on the influence of different concentrations of ADP and Mg2+ on the resealing efficiency of cyclosporin A suggest that the true effector modulating the state of the Ca(2+)-dependent pore is the ADP-Mg2+ complex, but not ADP or Mg2+ used separately. The ability of non-hydrolyzable analogs of adenine nucleotides, ADP-S and ATP-S, to potentiate the resealing action of cyclosporin on mitochondria permeabilized by loading of different Ca2+ concentrations to that of ADP was compared. ATP-S was ineffective when the pore was induced by high concentrations of Ca2+. The results obtained are discussed in terms of hypothesis on the direct involvement of the ADP/ATP antiporter in regulation of the inner mitochondrial membrane Ca(2+)-dependent pore state.

publication date

  • October 1994

Research

keywords

  • Academic Article

Identity

Language

  • rus

PubMed ID

  • 7819399

Additional Document Info

start page

  • 1589

end page

  • 97

volume

  • 59

number

  • 10