Journal
JOURNAL OF BIOENERGETICS AND BIOMEMBRANES
Volume 32, Issue 2, Pages 193-198Publisher
SPRINGER/PLENUM PUBLISHERS
DOI: 10.1023/A:1005516115189
Keywords
mitochondria; octylguanidine; octylamine; carboxyatractyloside; permeability transition, kidney mitochondria; nonspecific pore; calcium; mitochondrial calcium; mitochondrial membrane
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Mitochondrial permeability transition occurs through a Ca2+-dependent opening of a transmembrane pore, whose identity has been attributed to that of the adenine nucleotide translocase (ANT). In this work, we induced permeability transition by adding 0.5 mu M carboxyatractyloside. The process was evaluated analyzing Ca2+ efflux, a drop in transmembrane electric gradient, and swelling. We found that the amphiphyllic cations octylguanidine and octylamine, at the concentration of 100 mu M, inhibited, almost completely, nonspecific membrane permeability. Hexylguanidine, hexylamine, as well as guanidine chloride and hydroxylamine failed to do so. The inhibition was reversed after the addition of 40 mM Li+, Na+ K+, Rb+, or Cs+; K+ was the most effective. We propose that the positive charge of the amines interact with negative charges of membrane proteins, more likely the ADP/ATP carrier, while the alkyl chain penetrates into the hydrophobic milieu of the inner membrane, fixing the reagent.
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