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Enhanced Gamma-Glutamyl Transpeptidase Expression and Superoxide Production in Mpv17-/- Glomerulosclerosis Mice.
Biol. Chem. 382, 1019-1025 (2001)
Recently, gamma-glutamyl transpeptidase, which initiates cleavage of extracellular glutathione, has been shown to promote oxidative damage 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 RT-PCR) of membrane-bound gamma-glutamyl transpeptidase were increased, while plasma glutathione peroxidase and superoxide dismutase levels were lowered. Superoxide anion production in these cells was increased as documented by electron spin resonance spectroscopy. In the presence of Mn(III)tetrakis(4-benzoic acid)porphyrin, the activities of gamma-glutamyl transpeptidase and plasma glutathione peroxidase were unchanged, suggesting a relationship between enzyme expression and the amount of reactive oxygen species. Inhibition of gamma-glutamyl transpeptidase by acivicin reverted the lowered plasma glutathione peroxidase and superoxide dismutase activities, indicating reciprocal control of gene expression for these enzymes.
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Publikationstyp
Artikel: Journalartikel
Dokumenttyp
Wissenschaftlicher Artikel
Schlagwörter
Gene expression Glomerulopathy Glutathione cycle Reactive oxygen Transgenic mice
ISSN (print) / ISBN
1431-6730
e-ISSN
1437-4315
Zeitschrift
Biological Chemistry
Quellenangaben
Band: 382,
Heft: 7,
Seiten: 1019-1025
Verlag
de Gruyter
Nichtpatentliteratur
Publikationen
Begutachtungsstatus
Peer reviewed
Institut(e)
Institute of Radiation Biology (ISB)