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Recently, γglutamyl transpeptidase, which initiatescleavage of extracellular glutathione, has been shown to promote oxidativedamage to cells. Here we examined a murine disease model of glomerulosclerosis,involving loss of the Mpv17 gene coding for a peroxisomal protein. In Mpv17[/]cells, enzyme activity and mRNA expression (examined by quantitative RTPCR) ofmembranebound γglutamyl transpeptidase were increased, while plasma glutathioneperoxidase and superoxide dismutase levels were lowered. Superoxide anionproduction in these cells was increased as documented by electron spinresonance spectroscopy. In the presence of Mn(III)tetrakis(4- benzoicacid)porphyrin, the activities of γglutamyl transpeptidase and plasmaglutathione peroxidase were unchanged, suggesting a relationship between enzymeexpression and the amount of reactive oxygen species. Inhibition of γglutamyltranspeptidase by acivicin reverted the lowered plasma glutathione peroxidaseand superoxide dismutase activities, indicating reciprocal control of geneexpression for these enzymes.

Enhanced Gamma-Glutamyl Transpeptidase Expression and Superoxide Production in Mpv17-/-Glomerulosclerosis Mice