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PMID: 10751553 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Nrf2 and c-Jun regulation of antioxidant response element (ARE)-mediated expression and induction of gamma-glutamylcysteine synthetase heavy subunit gene.

Biochemical pharmacology ·Vol. 59 ·No. 11 ·2000-06-01 ·Pages 1433-9

Jeyapaul J, Jaiswal AK

Abstract

gamma-Glutamylcysteine synthetase (gamma-GCS) is a rate-limiting enzyme in the de novo synthesis of glutathione, a known scavenger of electrophiles and reactive oxygen species (ROS). The gamma-GCS gene is expressed ubiquitously and induced coordinately with NAD(P)H:quinone oxidoreductase(1) (NQO1) and glutathione S-transferase Ya (GST Ya) in response to xenobiotics and antioxidants. The antioxidant response element (ARE) is required for expression and induction of these genes. In the current report, we demonstrated that ARE-mediated gamma-GCS gene expression and induction is regulated by similar Nrf and Jun factors as reported earlier for the NQO1 and GST Ya genes. The gamma-GCS gene ARE competed with the binding of nuclear proteins (Nrf + Jun) to the NQO1 gene ARE (hARE). In addition, the overexpression of Nrf2 and Nrf1 with c-Jun significantly up-regulated gamma-GCS ARE-mediated basal expression and beta-naphthoflavone induction of the chloramphenicol acetyltransferase gene in transfected HepG2 cells. Interestingly, Nrf2 + c-Jun was more effective than Nrf1 + c-Jun in the regulation of ARE-mediated gamma-GCS gene expression. Further experiments demonstrated that the c-Jun level within the cells is an important determinant of the level of ARE-mediated gamma-GCS gene expression. Therefore, at higher concentrations of c-Jun, gamma-GCS gene expression is repressed, presumably due to generation of a sufficient amount of c-Jun + c-Fos complex that interferes with the binding of Nrf2 + c-Jun complex to the ARE.

MeSH Terms
Animals Antioxidants/metabolism Base Sequence DNA/genetics,physiology DNA-Binding Proteins/physiology Enzyme Induction Glutamate-Cysteine Ligase/biosynthesis,genetics Glutathione Transferase/genetics Humans Molecular Sequence Data NF-E2-Related Factor 2 Proto-Oncogene Proteins c-jun/physiology Quinone Reductases/genetics Rats Trans-Activators/physiology Tumor Cells, Cultured
Chemicals
Antioxidants DNA-Binding Proteins NF-E2-Related Factor 2 NFE2L2 protein, human Nfe2l2 protein, rat Proto-Oncogene Proteins c-jun Trans-Activators DNA NADH dehydrogenase (quinone) Quinone Reductases Glutathione Transferase Glutamate-Cysteine Ligase
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Jeyapaul J
Department of Pharmacology, Baylor College of Medicine, Houston, TX 77030, USA.
Jaiswal A K
Article Info
Journal
Biochemical pharmacology
Abbr.
Biochem Pharmacol
ISSN
0006-2952
Published
2000-06-01
Pages
1433-9
Language
English
Region
England
NLM ID
0101032
Subset
IM
Grants
NIGMS NIH HHS · GM47466 · United States
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