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Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board: Buchner, Johannes / Lei, Ming / Ludwig, Stephan / Thomas, Douglas D. / Turk, Boris / Wittinghofer, Alfred


IMPACT FACTOR 2018: 3.014
5-year IMPACT FACTOR: 3.162

CiteScore 2018: 3.09

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1437-4315
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Glutathione peroxidases and redox-regulated transcription factors

Regina Brigelius-Flohé
  • German Institute of Human Nutrition, Potsdam-Rehbrücke, Arthur-Scheunert-Allee 114-116, D-14558 Nuthetal, Germany
  • Other articles by this author:
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Published Online: 2006-11-02 | DOI: https://doi.org/10.1515/BC.2006.166

Abstract

Analysis of the selenoproteome identified five glutathione peroxidases (GPxs) in mammals: cytosolic GPx (cGPx, GPx1), phospholipid hydroperoxide GPx (PHGPX, GPx4), plasma GPx (pGPX, GPx3), gastrointestinal GPx (GI-GPx, GPx2) and, in humans, GPx6, which is restricted to the olfactory system. GPxs reduce hydroperoxides to the corresponding alcohols by means of glutathione (GSH). They have long been considered to only act as antioxidant enzymes. Increasing evidence, however, suggests that nature has not created redundant GPxs just to detoxify hydroperoxides. cGPx clearly acts as an antioxidant, as convincingly demonstrated in GPx1-knockout mice. PHGPx specifically interferes with NF-κB activation by interleukin-1, reduces leukotriene and prostanoid biosynthesis, prevents COX-2 expression, and is indispensable for sperm maturation and embryogenesis. GI-GPx, which is not exclusively expressed in the gastrointestinal system, is upregulated in colon and skin cancers and in certain cultured cancer cells. GI-GPx is a target for Nrf2, and thus is part of the adaptive response by itself, while PHGPx might prevent cancer by interfering with inflammatory pathways. In conclusion, cGPx, PHGPx and GI-GPx have distinct roles, particularly in cellular defence mechanisms. Redox sensing and redox regulation of metabolic events have become attractive paradigms to unravel the specific and in part still enigmatic roles of GPxs.

Keywords: cancer; glutathione peroxidases; inflammation; NF-κB; Nrf2

About the article

Published Online: 2006-11-02

Published in Print: 2006-10-01


Citation Information: Biological Chemistry, Volume 387, Issue 10/11, Pages 1329–1335, ISSN (Online) 1437-4315, ISSN (Print) 1431-6730, DOI: https://doi.org/10.1515/BC.2006.166.

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Biological Chemistry, 2007, Volume 388, Number 10
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Psychopharmacology, 2011, Volume 213, Number 4, Page 757
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Vanja Radišić Biljak, Lada Rumora, Ivana Čepelak, Dolores Pancirov, Sanja Popović-Grle, Jasna Sorić, and Tihana Žanić Grubišić
Cell Biochemistry and Function, 2010, Volume 28, Number 6, Page 448
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Alison Sutherland, Dong-Hyun Kim, Caroline Relton, Yoon-Ok Ahn, and John Hesketh
Genes & Nutrition, 2010, Volume 5, Number 3, Page 215
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Biochemistry (Moscow) Supplement Series B: Biomedical Chemistry, 2010, Volume 4, Number 3, Page 224
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Biological Trace Element Research, 2010, Volume 134, Number 3, Page 235
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Sarah Elizabeth Jackson-Rosario and William Thomas Self
Metallomics, 2010, Volume 2, Number 2, Page 112
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Journal of Animal Physiology and Animal Nutrition, 2009, Volume 93, Number 6, Page 695
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Biochemistry (Moscow) Supplement Series B: Biomedical Chemistry, 2009, Volume 3, Number 2, Page 129
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International Journal of Cosmetic Science, 2009, Volume 31, Number 3, Page 201
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Chemical Senses, 2009, Volume 34, Number 4, Page 317
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Journal of Molecular Medicine, 2008, Volume 86, Number 11, Page 1279
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Harsharn GILL and Glen WALKER
Nutrition & Dietetics, 2008, Volume 65, Page S41
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British Journal of Nutrition, 2008, Volume 100, Number 02
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European Journal of Gastroenterology & Hepatology, 2008, Volume 20, Number 6, Page 496
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Albena T. Dinkova-Kostova and Paul Talalay
Molecular Nutrition & Food Research, 2008
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PROTEOMICS – CLINICAL APPLICATIONS, 2007, Volume 1, Number 12, Page 1613

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