The DOI matches its Crossref record; 5 of the 5 references it cites were found in a registry or an index.
The GI-GPx Gene Is a Target for Nrf2
Open accessAbstract
The gastrointestinal glutathione peroxidase (GI-GPx, GPx2) is a selenoprotein that was suggested to act as barrier against hydroperoxide absorption but has also been implicated in the control of inflammation and malignant growth. In CaCo-2 cells, GI-GPx was induced by t-butyl hydroquinone (tBHQ) and sulforaphane (SFN), i.e., "antioxidants" known to activate the "antioxidant response element" (ARE) via electrophilic thiol modification of Keap1 in the Nrf2/Keap1 system. The functional significance of a putative ARE in the GI-GPx promoter was validated by transcriptional activation of reporter gene constructs upon exposure to electrophiles (tBHQ, SFN, and curcumin) or overexpression of Nrf2 and by reversal of these effects by mutation of the ARE in the promoter and by overexpressed Keap1. Binding of Nrf2 to the ARE sequence in authentic gpx2 was corroborated by chromatin immunoprecipitation. Thus, the presumed natural antioxidants sulforaphane and curcumin may exert their anti-inflammatory and anticarcinogenic effects not only by induction of phase 2 enzymes but also by the up-regulation of the selenoprotein GI-GPx.
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Dinkova-Kostova, A. T., Holtzclaw, W. D., Cole, R. N., Itoh, K., Wakabayashi, N., Katoh, Y., Yamamoto, M., & Talalay, P. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.172398899 · Cited by 1,947
Tissue-specific functions of individual glutathione peroxidases
Brigelius-Flohé, R. (1999) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(99)00173-2 · Cited by 1,114
Self-citationWakabayashi, N., Dinkova-Kostova, A. T., Holtzclaw, W. D., Kang, M.-I., Kobayashi, A., Yamamoto, M., Kensler, T. W., & Talalay, P. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0307301101 · Cited by 986 · cited 1×
“Modification of specific SH groups in Keap1 by oxidation, alkylation, or arylation results in the dissociation of the Keap1/Nrf2 complex and translocation of Nrf2 to the nucleus, where it heterodimerizes with other basic leucine zipper proteins, such as small Maf, and then can bind to ARE (62).”
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Cited by
Brigelius-Flohé, R., & Maiorino, M. (2013) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2012.11.020 · Cited by 1,904
Self-citationLubos, E., Loscalzo, J., & Handy, D. E. (2011) · Antioxidants & Redox Signaling · doi:10.1089/ars.2010.3586 · Cited by 1,280
Tebay, L. E., Robertson, H., Durant, S. T., Vitale, S. R., Penning, T. M., Dinkova-Kostova, A. T., & Hayes, J. D. (2015) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2015.06.021 · Cited by 837
Role of antioxidants in the skin: Anti-aging effects
Masaki, H. (2010) · Journal of Dermatological Science · doi:10.1016/j.jdermsci.2010.03.003 · Cited by 788
Liu, G.-H., Qu, J., & Shen, X. (2008) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2008.01.002 · Cited by 697
Metadata
- Authors
- Banning, A., Deubel, S., Kluth, D., Zhou, Z., & Brigelius-Flohé, R.
- Venue
- Molecular and Cellular Biology
- Publisher
- Informa UK Limited
- Published
- 2005-06-01
- Volume
- 25
- Issue
- 12
- Pages
- 4914-4923
- ISSN
- 0270-7306 (ISSN-L)
- 1098-5549
- OpenAlex
- W2146962699
- Cited by
- 344
- References
- 5
- FWCI
- 6.80
- Type
- journal article
- Language
- en
- Open access
- green
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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