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• W2046757730 abstract "The rate-limiting step in the de novo synthesis of the cellular protectant glutathione is catalyzed by γ-glutamylcysteine synthetase (GCS; also known as glutamine-L-cysteine ligase, GLCL), a heterodimer consisting of catalytic (GCSh) and regulatory (GCSl) subunits. Regulation of expression of the human γ-glutamylcysteine synthetase regulatory subunit gene in response to β-NF is mediated by an Electrophile Responsive Element (EpRE) [Moinova, H., and Mulcahy, R. T. (1998) J. Biol. Chem. 273, 14683–14689]. Oligonucleotide probes corresponding to wild-type and mutant EpRE sequences were used in gel-shift and super-shift analyses to identify proteins binding. Four protein:DNA complexes (a–d) with distinct mobilities were detected when the wild-type EpRE probe was incubated with nuclear extracts from control or β-NF-treated HepG2 cells. Following β-NF treatment, there was an increase in the intensity of a single band, band b. This band was eliminated in gel shifts employing mutant EpRE probes which abolish β-NF inducibility, demonstrating a correlation between band b and transactivation. Super-shift analysis identified JunD, Nrf1, and Nrf2 in the EpRE-binding complexes. Antibodies to Nrf2 completely super-shifted the band b protein:DNA complex. These studies demonstrate that Nrf2 proteins recognize and bind the GCSl EpRE sequence to affect transactivation of the gene." @default.
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• W2046757730 date "1999-08-01" @default.
• W2046757730 modified "2023-09-26" @default.
• W2046757730 title "Up-Regulation of the Human γ-Glutamylcysteine Synthetase Regulatory Subunit Gene Involves Binding of Nrf-2 to an Electrophile Responsive Element" @default.
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• W2046757730 doi "https://doi.org/10.1006/bbrc.1999.1109" @default.
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