title: Oxalate binding to rat kidney mitochondria: induction by oxidized glutathione.
abstract: Increased oxalate binding with negative correlation with reduced glutathione content was observed during lipid peroxidation in rat kidney mitochondria. In presence of oxidized glutathione (GSSG), peroxidized mitochondria lost 48% of protein-SH with concomitant 3-fold increase in oxalate binding activity while control mitochondria lost only 20% protein-SH with only 0.8 fold increase in oxalate binding activity. The GSSG-induced oxalate binding was apparently due to two-fold increased affinity of oxalate to the protein. Reduced glutathione (GSH) inhibited oxalate binding competitively with Ki, 1.4 x 10(-3) M. Urolithic rat kidney mitochondria showed 30-50% increase in oxalate binding activity along with depletion of GSH and protein-SH. These studies suggest that oxalate binding is regulated by thiol status of mitochondria.
authors: Department of Medical Biochemistry, University of Madras.
authors: R
authors: R
authors: Selvam
authors: S
authors: S
authors: Devaraj
mesh_terms: D000818:Animals; D005978:Glutathione / Q000031:analogs & derivatives* / Q000378:metabolism / Q000494:pharmacology; D019803:Glutathione Disulfide; D007668:Kidney / Q000378:metabolism*; D008297:Male; D008928:Mitochondria / Q000187:drug effects / Q000378:metabolism*; D010070:Oxalates / Q000378:metabolism*; D051381:Rats; D017208:Rats, Wistar; D014545:Urinary Calculi / Q000378:metabolism*
chemical_list: D010070:Oxalates; D005978:Glutathione; D019803:Glutathione Disulfide