Regulation of lipid peroxidation by ATP synthetase substrates in rat liver mitochondria.
The addition of cumene hydroperoxide to succinate-energized mitochondria has been shown to result only in an insignificant acceleration of lipid peroxidation. Phosphate accelerates this process, while ADP reverses the phosphate effect. The phosphate and ADP effects are revealed in the mitochondrial matrix. N-Ethylmaleimide, the phosphate transport inhibitor, taken at low concentrations, prevents the phosphate effects; accordingly, carboxyatractyloside, the nucleotide transport inhibitor, prevents the ADP effects. The addition of an uncoupler to the energized mitochondria has no effect on the induction of lipid peroxidation by cumene hydroperoxide in the presence of phosphate and does not reverse the ADP effect.
D025181:ATP Synthetase Complexes; D000244:Adenosine Diphosphate / Q000378:metabolism; D000818:Animals; D001555:Benzene Derivatives / Q000378:metabolism; D002259:Carbonyl Cyanide p-Trifluoromethoxyphenylhydrazone / Q000494:pharmacology; D002849:Chromatography, Gas; D008054:Lipid Peroxides / Q000378:metabolism*; D008315:Malondialdehyde / Q000378:metabolism; D008564:Membrane Potentials; D008930:Mitochondria, Liver / Q000201:enzymology*; D009097:Multienzyme Complexes / Q000378:metabolism*; D010710:Phosphates / Q000378:metabolism; D010770:Phosphotransferases / Q000378:metabolism*; D051381:Rats
D001555:Benzene Derivatives; D008054:Lipid Peroxides; D009097:Multienzyme Complexes; D010710:Phosphates; D002259:Carbonyl Cyanide p-Trifluoromethoxyphenylhydrazone; D008315:Malondialdehyde; D000244:Adenosine Diphosphate; D010770:Phosphotransferases; D025181:ATP Synthetase Complexes; C007164:cumene hydroperoxide