Induction of oxalate binding by lipid peroxidation in rat kidney mitochondria.
Enhanced oxalate binding (150-180% of control) was observed in kidney, liver, brain and heart, after subjecting them to lipid peroxidation in presence of iron. Kidney mitochondrial oxalate binding was stimulated by different promoters, and the order of stimulation was Fe2+ greater than t-BH greater than ascorbic acid greater than Fe3+ greater than H2O2. Oxalate binding was maximum when iron concentration was between 1-2 mM. The iron-induced oxalate binding was inhibited by reduced glutathione, beta-mercaptoethanol, alpha-tocopherol and hydroxyl ion scavengers, histidine and mannitol. Catalase inhibited both Fe(2+)-H2O2 induced oxalate binding and lipid peroxidation reactions, suggesting that the induced oxalate binding in mitochondria was mediated through the hydroxyl radical reaction mechanism.
Selvam
R
R
Department of Medical Biochemistry, Dr. Alm Post-Graduate Institute of Basic Medical Sciences, University of Madras, Taramani, India.
Devaraj
S
S
D000818:Animals; D001205:Ascorbic Acid / Q000494:pharmacology; D005978:Glutathione / Q000494:pharmacology; D006639:Histidine / Q000494:pharmacology; D006861:Hydrogen Peroxide / Q000494:pharmacology; D006878:Hydroxides / Q000378:metabolism; D017665:Hydroxyl Radical; D007501:Iron / Q000494:pharmacology; D007668:Kidney / Q000378:metabolism*; D015227:Lipid Peroxidation; D008297:Male; D008353:Mannitol / Q000494:pharmacology; D008623:Mercaptoethanol / Q000494:pharmacology; D008928:Mitochondria / Q000378:metabolism*; D010070:Oxalates / Q000378:metabolism*; D010545:Peroxides / Q000494:pharmacology; D051381:Rats; D011919:Rats, Inbred Strains; D020122:tert-Butylhydroperoxide
D006878:Hydroxides; D010070:Oxalates; D010545:Peroxides; D017665:Hydroxyl Radical; D008353:Mannitol; D006639:Histidine; D008623:Mercaptoethanol; D020122:tert-Butylhydroperoxide; D006861:Hydrogen Peroxide; D007501:Iron; D005978:Glutathione; D001205:Ascorbic Acid