Evidence for different localization of glutathione oxidase and gamma-glutamyltransferase activities during extracellular glutathione metabolism in isolated perfused rat kidney.
The metabolism of extracellular glutathione was studied in the isolated, perfused rat kidney.  The results indicate different localization of glutathione oxidase and gamma -glutamyltransferase (5-glutamyl)-peptide: aminoacid 5-glutamyltransferase, EC 2.3.2.2) activities, since glutathione oxidase activity was observed only with glutathione present in the perfusate, whereas gamma -glutamyltransferase-mediated metabolism of glutathione was restricted to glutathione present to the localization of renal gamma -glutamyltransferase in the brush border membranes of the tubular epithelium, but suggest an opposite localization of renal glutathione oxidase activity, i.e., in the basal plasma membrane fraction of the tubular cells, facing the capillary bloodstream. Furthermore, the existence of the tubular glutathione extraction mechanism operating in addition to glomerular filtration is confirmed.
D000818:Animals; D005919:Glomerular Filtration Rate; D005978:Glutathione / Q000378:metabolism*; D007668:Kidney / Q000201:enzymology*; D007700:Kinetics; D008297:Male; D010084:Oxidation-Reduction; D010088:Oxidoreductases / Q000378:metabolism*; D010477:Perfusion; D051381:Rats; D011919:Rats, Inbred Strains; D005723:gamma-Glutamyltransferase / Q000378:metabolism*
D010088:Oxidoreductases; C020667:glutathione oxidase; D005723:gamma-Glutamyltransferase; D005978:Glutathione