The antioxidant responsive element. Activation by oxidative stress and identification of the DNA consensus sequence required for functional activity
Open accessAbstract
We have characterized further the antioxidant responsive element (ARE) identified in the 5'-flanking region of the rat glutathione S-transferase Ya subunit gene and the NAD(P)H:quinone reductase gene by mutational and deletion analyses. Our data suggest that the sequence, 5'-puGTGACNNNGC-3' 3'-pyCACTGNNNCG-5' where N is any nucleotide, represents the core sequence of the ARE required for transcriptional activation by phenolic antioxidants and metabolizable planar aromatic compounds (e.g. beta-naphthoflavone and 3-methylcholanthrene). We also have found that the ARE is responsive to hydrogen peroxide and phenolic antioxidants that undergo redox cycling. These latter data suggest that the ARE is responsive to reactive oxygen species and thus may represent part of a signal transduction pathway that allow eukaryotic cells to sense and respond to oxidative stress.
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The antioxidant response element (ARE) is a cis-acting enhancer sequence found within the promoter region of many cytoprotective antioxidant and phase II enzyme genes, with a core sequence of 5′-TGACnnnGC-3′.
“The antioxidant response element (ARE) [42], also referred to as the electrophile response element (EpRE), is a cis-acting enhancer sequence found within the promoter region of many cytoprotective antioxidant and phase II enzyme genes. It has a core sequence of 5′-TGACnnnGC-3′ and participates in inducible gene expression in response to oxidative stress [42].”
From Nrf2 and Oxidative Stress: A General Overview of Mechanisms and Implications in Human Disease (2022) · cites this paper as [42]
H2O2-induced oxidative stress and PMA modulate the activity of IRP1 and IRP2.
“H2O2-induced oxidative stress and phorbol 12-myristate 13-acetate (PMA) have been shown to modulate the activity of IRP1 and IRP2 (269).”
From Intracellular iron transport and storage: from molecular mechanisms to health implications (2008) · cites this paper as [269]
PMA induces IRP1 and IRP2 phosphorylation and enhances binding to ferritin IRE, resulting in decreased ferritin expression during PMA-induced HL-60 differentiation.
“PMA induces IRP1 and IRP2 phosphorylation and enhances this binding to ferritin IRE, resulting in decreased ferritin expression during PMA induced HL-60 differentiation (269).”
From Intracellular iron transport and storage: from molecular mechanisms to health implications (2008) · cites this paper as [269]
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- Authors
- Rushmore, T. H., Morton, M. R., & Pickett, C. B.
- Affiliations
- Merck Canada Inc. (Canada) (CA)
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1991-06
- Volume
- 266
- Issue
- 18
- Pages
- 11632-11639
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1561096292
- Cited by
- 1,464
- References
- 29
- Citations by year
- 2026: 21 · 2025: 17 · 2024: 30 · 2023: 31 · 2022: 31 · 2021: 32 · 2020: 36 · 2019: 44 · 2018: 49 · 2017: 53 · 2016: 47 · 2015: 45 · 2014: 60 · 2013: 51 · 2012: 58
- FWCI
- 13.35
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics, phytochemicals, and oxidative stress
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glutathione Transferases and Polymorphisms
- Keywords
- antioxidant response element, oxidative stress, glutathione S-transferase Ya, NAD(P)H:quinone reductase, transcriptional activation, hydrogen peroxide, phenolic antioxidants, redox cycling, reactive oxygen species, signal transduction, gene expression regulation
- MeSH terms
- Animals, Antioxidants, Base Sequence, beta-Galactosidase, Chromosome Deletion, DNA, Neoplasm, Glutathione Transferase, Carcinoma, Hepatocellular, Humans, Liver Neoplasms, Molecular Sequence Data, Mutation, Oxidation-Reduction, Promoter Regions, Genetic, Quinone Reductases, Transcription, Genetic, Transfection, Tumor Cells, Cultured, Chloramphenicol O-Acetyltransferase, Polymerase Chain Reaction, Consensus Sequence, Rats
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