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Gamma-glutamyltranspeptidase-dependent glutathione catabolism results in activation of NF-kB.

Abstract：

:gamma-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 H(2)O(2) and was inhibited by catalase, suggesting the involvement of H(2)O(2) in the NF-kB activation.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Accaoui MJ,Enoiu M,Mergny M,Masson C,Dominici S,Wellman M,Visvikis A

doi

10.1006/bbrc.2000.3585

subject

Has Abstract

pub_date

2000-10-05 00:00:00

pages

1062-7

issue

3

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(00)93585-X

journal_volume

276

pub_type

杂志文章

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