Cited by 199Genomics, phytochemicals, and oxidative stressGlutathione Transferases and PolymorphismsRedox biology and oxidative stress

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A genomic screen for activators of the antioxidant response element

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Liu, Yanxia, Kern, Jonathan T., Walker, John R., Johnson, Jeffrey A., Schultz, Peter G., Luesch, Hendrik·2007·Proceedings of the National Academy of Sciences

DOI 10.1073/pnas.0700898104PMC PMC1829287

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Abstract

The antioxidant response element (ARE) is a cis-acting regulatory enhancer element found in the 5′ flanking region of many phase II detoxification enzymes. Up-regulation of ARE-dependent target genes is known to have neuroprotective effects; yet, the mechanism of activation is largely unknown. By screening an arrayed collection of ≈15,000 full-length expression cDNAs in the human neuroblastoma cell line IMR-32 with an ARE-luciferase reporter, we have identified several cDNAs not previously associated with ARE activation. A subset of cDNAs, encoding sequestosome 1 (SQSTM1) and dipeptidylpeptidase 3 (DPP3), activated the ARE in primary mouse-derived cortical neurons. Overexpression of SQSTM1 and DPP3 in IMR-32 cells stimulated NF-E2-related factor 2 (NRF2) nuclear translocation and led to increased levels of NAD(P)H:quinone oxidoreductase 1, a protein which is transcriptionally regulated by the ARE. When transfected into IMR-32 neuroblastoma cells that were depleted of transcription factor NRF2 by RNA interference, SQSTM1 and DPP3 were unable to activate the ARE or induce NAD(P)H:quinone oxidoreductase 1 expression, indicating that the ARE activation upon ectopic expression of these cDNAs is mediated by NRF2. Studies with pharmacological inhibitors indicated that 1-phosphatidylinositol 3-kinase and protein kinase C signaling are essential for activity. Overexpression of these cDNAs conferred partial resistance to hydrogen peroxide or rotenone-induced toxicity, consistent with the induction of antioxidant and phase II detoxification enzymes, which can protect from oxidative stress. This work and other such studies may provide mechanisms for activating the ARE in the absence of general oxidative stress and a yet-unexploited therapeutic approach to degenerative diseases and aging.

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Show all 53 references

Research works printed but not linked: 1

M McMahon, K Itoh, M Yamamoto, SA Chanas, CJ Henderson, LI McLellan, CR Wolf, C Cavin, JD Hayes Cancer Res 61, 3299–3307 (2001).

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Chen, C. (2024) · Springer eBooks · doi:10.1007/978-3-031-55287-8_14
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Srivastava, P., Verma, A. K., Singh, A. L., Kumar, R., & Rizvi, S. I. (2024) · Indian Journal of Clinical Biochemistry · doi:10.1007/s12291-024-01233-9
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Tsubota, K. (2024) · Springer eBooks · doi:10.1007/978-981-97-8514-8_11
Gene library deep sequencing for protein superfamily profiling
Sabapathy, R. T., Henry-Cocks, K., Feng, J., Marri, S., Granado, G. B., & Janovjak, H. (2026) · Cell Reports Methods · doi:10.1101/2025.10.20.682913
La voie de la dipeptidyl-peptidase 3 : une nouvelle voie thérapeutique de la défaillance cardiaque aiguë
Deniau, B. (2020) · theses.fr (ABES) · doi:10.70675/58e60e7bz58d0z4839zbce3z1aaf9556bd1e
Source and mechanism of Dipeptidyl peptidase 3 (DPP3) release in pathological situations
Assad, N. (2024) · theses.fr (ABES) · doi:10.70675/cb675ab6z1d3fz42a8z82a9zcafae80e8180
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Lang, T., Lipp, A.-M., Demmel, D., Pröll, J., & Wechselberger, C. (2026) · Environmental Toxicology and Pharmacology · doi:10.1016/j.etap.2026.105177
BindingDB Entry 7891: Validation of flavonoids as potential dipeptidyl peptidase III inhibitors: Experimental and computational approach.
BindingDB (2017) · UC San Diego · doi:10.7270/q2x34wbs
BindingDB Entry 50022224: NRF2 inhibitors: Recent progress, future design and therapeutic potential.
BindingDB (2025) · UC San Diego · doi:10.7270/q27h1q92
BindingDB Entry 50018472: p62 as a therapeutic target for tumor.
BindingDB (2024) · UC San Diego · doi:10.7270/q2q244g8
BindingDB Entry 50010943: p62/SQSTM1, a Central but Unexploited Target: Advances in Its Physiological/Pathogenic Functions and Small Molecular Modulators.
BindingDB (2021) · UC San Diego · doi:10.7270/q2s46wjb

Authors: Liu, Y., Kern, J. T., Walker, J. R., Johnson, J. A., Schultz, P. G., & Luesch, H.
Affiliations: University of Florida (US)
University of Wisconsin–Madison (US)
Genomics Institute of the Novartis Research Foundation (US)
Scripps Research Institute (US)
ORCID: Liu, Yanxia
Kern, Jonathan T.
Walker, John R.
Johnson, Jeffrey A.
Schultz, Peter G.
Luesch, Hendrik
Venue: Proceedings of the National Academy of Sciences
Publisher: National Academy of Sciences
Published: 2007-03-20
Volume: 104
Issue: 12
Pages: 5205-5210
ISSN: 0027-8424 (ISSN-L)
1091-6490
DOI: 10.1073/pnas.0700898104
PMC: PMC1829287
OpenAlex: W2147984935
Cited by: 196
References: 53
Citations by year: 2026: 2 · 2025: 6 · 2024: 8 · 2023: 6 · 2022: 11 · 2021: 15 · 2020: 15 · 2019: 5 · 2018: 7 · 2017: 13 · 2016: 12 · 2015: 14 · 2014: 11 · 2013: 12 · 2012: 12
FWCI: 4.91
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Locations: Proceedings of the National Academy of Sciences (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Funders: Ellison Medical Foundation
American Heart Association
McKnight Foundation
National Institute of Environmental Health Sciences (ES10042, R01ES010042, ES08089, R01ES008089, R29ES008089)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics, phytochemicals, and oxidative stress
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glutathione Transferases and Polymorphisms
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
Keywords: antioxidant response element, Nrf2, NAD(P)H:quinone oxidoreductase 1, p62, phase II enzymes, oxidative stress, neuroprotection, PI3K signaling, protein kinase C signaling, neuroblastoma cells, cortical neurons, neurodegenerative diseases
MeSH terms: Sequestosome-1 Protein, Animals, Antioxidants, Cell Nucleus, Cells, Cultured, Cerebral Cortex, Enzyme Induction, Heat-Shock Proteins, NADPH Dehydrogenase, Trans-Activators, Gene Library, Gene Expression, NAD(P)H Dehydrogenase (Quinone), Genome, DNA, Complementary, Oxidative Stress, Response Elements, Oligonucleotide Array Sequence Analysis, Protein Transport, Genomics, RNA, Small Interfering, Protein Kinase Inhibitors, Adaptor Proteins, Signal Transducing, NF-E2-Related Factor 2, Mice

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A genomic screen for activators of the antioxidant response element

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