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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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Source Normalized Impact per Paper (SNIP) 2018: 0.820

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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
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Published Online: 2006-11-02 | DOI: https://doi.org/10.1515/BC.2006.166


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

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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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Metallomics, 2010, Volume 2, Number 2, Page 112
I. Placha, R. Borutova, L. Gresakova, V. Petrovic, S. Faix, and L. Leng
Journal of Animal Physiology and Animal Nutrition, 2009, Volume 93, Number 6, Page 695
V. I. Kulinsky and L. S. Kolesnichenko
Biochemistry (Moscow) Supplement Series B: Biomedical Chemistry, 2009, Volume 3, Number 2, Page 129
A. T. Grazul-Bilska, J. J. Bilski, D. A. Redmer, L. P. Reynolds, K. M. Abdullah, and A. Abdullah
International Journal of Cosmetic Science, 2009, Volume 31, Number 3, Page 201
G. A. Behr, L. L. da Motta, M. R. de Oliveira, M. W. S. Oliveira, D. P. Gelain, and J. C. F. Moreira
Chemical Senses, 2009, Volume 34, Number 4, Page 317
Ioannis G. Habeos, Panos G. Ziros, Dionysios Chartoumpekis, Agathoklis Psyrogiannis, Venetsana Kyriazopoulou, and Athanasios G. Papavassiliou
Journal of Molecular Medicine, 2008, Volume 86, Number 11, Page 1279
Harsharn GILL and Glen WALKER
Nutrition & Dietetics, 2008, Volume 65, Page S41
Margaret P. Rayman
British Journal of Nutrition, 2008, Volume 100, Number 02
Philip Rosenstiel and Stefan Schreiber
European Journal of Gastroenterology & Hepatology, 2008, Volume 20, Number 6, Page 496
Albena T. Dinkova-Kostova and Paul Talalay
Molecular Nutrition & Food Research, 2008
Yue Ge, R. Julian Preston, and Russell D. Owen
PROTEOMICS – CLINICAL APPLICATIONS, 2007, Volume 1, Number 12, Page 1613

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