Gamma-Glutamyltranspeptidase-Dependent Glutathione Catabolism Results in Activation of NF-kB

γ-glutamyltranspeptidase (GGT) is a key enzyme implicated in the homeostasis of intracellular reduced glutathione (GSH) and hence in the regulation of the cellular redox state. Besides, the extracellular cleavage of GSH by GGT leads to reactive oxygen species (ROS) production, depending on the gener...

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Bibliographic Details
Published in:Biochemical and biophysical research communications 2000-10, Vol.276 (3), p.1062-1067
Main Authors: Accaoui, Marie-José, Enoiu, Milica, Mergny, Mojgan, Masson, Christine, Dominici, Sylvia, Wellman, Maria, Visvikis, Athanase
Format: Article
Language:English
Subjects:
Animals
antioxidants
Catalase - metabolism
Catalase - pharmacology
Cell Line
Cricetinae
Dipeptides - metabolism
Fibroblasts
g-glutamyltranspeptidase
gamma-Glutamyltransferase - genetics
gamma-Glutamyltransferase - metabolism
gamma-glutamyltranspeptidase
Genes, Reporter - genetics
glutathione
Glutathione - metabolism
Humans
Hydrogen Peroxide - metabolism
Hydrogen Peroxide - pharmacology
Kinetics
NF-^KB protein
NF-kappa B - metabolism
nuclear factor kB
Oxidation-Reduction - drug effects
Oxidative Stress - drug effects
reactive oxygen species
Reactive Oxygen Species - metabolism
reduced glutathione
Signal Transduction
Transcriptional Activation - drug effects
Transfection
Transgenes - genetics
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Summary:γ-glutamyltranspeptidase (GGT) is a key enzyme implicated in the homeostasis of intracellular reduced glutathione (GSH) and hence in the regulation of the cellular redox state. Besides, the extracellular cleavage of GSH by GGT leads to reactive oxygen species (ROS) production, depending on the generation and enhanced reactivity of cysteinylglycine (CysGly). Using a model cell line, the V79 GGT, which highly expresses a human GGT transgene, we examined whether the GGT induced oxidant stress could modulate intracellular transcription factors. For the first time, we show that GGT-dependent ROS production induces the NF-kB-binding and transactivation activities. This induction mimicked the one observed by H2O2 and was inhibited by catalase, suggesting the involvement of H2O2 in the NF-kB activation.
ISSN:0006-291X
1090-2104
DOI:10.1006/bbrc.2000.3585