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Gene Review

GPX2  -  glutathione peroxidase 2 (gastrointestinal)

Homo sapiens

Synonyms: GI-GPx, GPRP, GPRP-2, GPx-2, GPx-GI, ...
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Disease relevance of GPX2


High impact information on GPX2

  • Transport of 13-hydroperoxy octadecadienoic acid (13-HPODE) was investigated in a CaCo-2 cell monolayer modulated in GI-GPx and cGPx by selenium restriction or repletion [6].
  • GI-GPx may thus function as a barrier against hydroperoxide absorption. cGPx contributes to balance major oxidative challenge [6].
  • BACKGROUND & AIMS: Gastrointestinal glutathione peroxidase (GI-GPx), 1 of the 4 types of selenium-dependent glutathione peroxidases, is expressed exclusively in the gastrointestinal system and has therefore been suggested to function as a barrier against the absorption of dietary hydroperoxides [6].
  • Platelet activation by thrombin, generally regarded as the most physiologically important agonist, can be studied in whole blood in a clinical setting through the use of the peptide GPRP [7].
  • The peptide gly-pro-arg-pro (GPRP) was included in this assay to prevent fibrin polymerization and platelet aggregation, thus allowing the measurement of the reactivity to thrombin of individual platelets in the physiological milieu of whole blood [7].

Chemical compound and disease context of GPX2


Biological context of GPX2


Anatomical context of GPX2

  • The GPX2 gene codes for GSHPx-GI, a glutathione peroxidase whose mRNA is readily detectable in the gastrointestinal tract [14].
  • Surprisingly, the human GPX2 promoter could direct transcription and respond to oxidative stress in the murine NIH3T3 fibroblast cell line, which is devoid of the ability to bind to a variety of intestinal specific elements [13].
  • GSHPx-GI expressed in neo-D1 is a tetrameric protein localized in cytosol [1].
  • GSHPx-GI mRNA was readily detected in human liver and colon, and occasionally in human breast samples, but not other human tissues including kidney, heart, lung, placenta, or uterus [1].
  • Inverse mRNA expression of the selenocysteine-containing proteins GI-GPx and SeP in colorectal adenomas compared with adjacent normal mucosa [4].

Associations of GPX2 with chemical compounds


Regulatory relationships of GPX2

  • The anticarcinogenic role of GI-GPx is evident from enhanced gastrointestinal tumor formation in gpx2/gpx1 double KO mice [16].

Other interactions of GPX2


Analytical, diagnostic and therapeutic context of GPX2


  1. Expression, characterization, and tissue distribution of a new cellular selenium-dependent glutathione peroxidase, GSHPx-GI. Chu, F.F., Doroshow, J.H., Esworthy, R.S. J. Biol. Chem. (1993) [Pubmed]
  2. Expression of gastrointestinal glutathione peroxidase is inversely correlated to the presence of hepatitis C virus subgenomic RNA in human liver cells. Morbitzer, M., Herget, T. J. Biol. Chem. (2005) [Pubmed]
  3. Expression pattern of gastrointestinal selenoproteins--targets for selenium supplementation. Mörk, H., Lex, B., Scheurlen, M., Dreher, I., Schütze, N., Köhrle, J., Jakob, F. Nutrition and cancer. (1998) [Pubmed]
  4. Inverse mRNA expression of the selenocysteine-containing proteins GI-GPx and SeP in colorectal adenomas compared with adjacent normal mucosa. Mörk, H., al-Taie, O.H., Bähr, K., Zierer, A., Beck, C., Scheurlen, M., Jakob, F., Köhrle, J. Nutrition and cancer. (2000) [Pubmed]
  5. Cellular and subcellular localization of gastrointestinal glutathione peroxidase in normal and malignant human intestinal tissue. Florian, S., Wingler, K., Schmehl, K., Jacobasch, G., Kreuzer, O.J., Meyerhof, W., Brigelius-Flohé, R. Free Radic. Res. (2001) [Pubmed]
  6. Gastrointestinal glutathione peroxidase prevents transport of lipid hydroperoxides in CaCo-2 cells. Wingler, K., Müller, C., Schmehl, K., Florian, S., Brigelius-Flohé, R. Gastroenterology (2000) [Pubmed]
  7. Effect of strenuous exercise on platelet activation state and reactivity. Kestin, A.S., Ellis, P.A., Barnard, M.R., Errichetti, A., Rosner, B.A., Michelson, A.D. Circulation (1993) [Pubmed]
  8. Retinoic acid induces Gpx2 gene expression in MCF-7 human breast cancer cells. Chu, F.F., Esworthy, R.S., Lee, L., Wilczynski, S. J. Nutr. (1999) [Pubmed]
  9. Microflora trigger colitis in mice deficient in selenium-dependent glutathione peroxidase and induce Gpx2 gene expression. Esworthy, R.S., Binder, S.W., Doroshow, J.H., Chu, F.F. Biol. Chem. (2003) [Pubmed]
  10. Expression and chromosomal mapping of mouse Gpx2 gene encoding the gastrointestinal form of glutathione peroxidase, GPX-GI. Chu, F.F., Esworthy, R.S., Ho, Y.S., Bermeister, M., Swiderek, K., Elliott, R.W. Biomed. Environ. Sci. (1997) [Pubmed]
  11. GPX2, a direct target of p63, inhibits oxidative stress-induced apoptosis in a p53-dependent manner. Yan, W., Chen, X. J. Biol. Chem. (2006) [Pubmed]
  12. Glutathione Peroxidase 2, the Major Cigarette Smoke-Inducible Isoform of GPX in Lungs, Is Regulated by Nrf2. Singh, A., Rangasamy, T., Thimmulappa, R.K., Lee, H., Osburn, W.O., Brigelius-Floh??, R., Kensler, T.W., Yamamoto, M., Biswal, S. Am. J. Respir. Cell Mol. Biol. (2006) [Pubmed]
  13. Structural organization of the human gastrointestinal glutathione peroxidase (GPX2) promoter and 3'-nontranscribed region: transcriptional response to exogenous redox agents. Kelner, M.J., Bagnell, R.D., Montoya, M.A., Lanham, K.A. Gene (2000) [Pubmed]
  14. The mouse glutathione peroxidase Gpx2 gene maps to chromosome 12; its pseudogene Gpx2-ps maps to chromosome 7. Chu, F.F., Esworthy, R.S., Burmeister, M. Genomics (1996) [Pubmed]
  15. The GI-GPx gene is a target for Nrf2. Banning, A., Deubel, S., Kluth, D., Zhou, Z., Brigelius-Flohé, R. Mol. Cell. Biol. (2005) [Pubmed]
  16. Part of the Series: From dietary antioxidants to regulators in cellular signaling and gene regulation. Brigelius-Floh??, R., Banning, A. Free Radic. Res. (2006) [Pubmed]
  17. Mitochondrial GPx1 decreases induced but not basal oxidative damage to mtDNA in T47D cells. Legault, J., Carrier, C., Petrov, P., Renard, P., Remacle, J., Mirault, M.E. Biochem. Biophys. Res. Commun. (2000) [Pubmed]
  18. 3'UTRs of glutathione peroxidases differentially affect selenium-dependent mRNA stability and selenocysteine incorporation efficiency. Müller, C., Wingler, K., Brigelius-Flohé, R. Biol. Chem. (2003) [Pubmed]
  19. Smoking and cancer-related gene expression in bronchial epithelium and non-small-cell lung cancers. Woenckhaus, M., Klein-Hitpass, L., Grepmeier, U., Merk, J., Pfeifer, M., Wild, P., Bettstetter, M., Wuensch, P., Blaszyk, H., Hartmann, A., Hofstaedter, F., Dietmaier, W. J. Pathol. (2006) [Pubmed]
  20. Polymorphism and chromosomal localization of the GI-form of human glutathione peroxidase (GPX2) on 14q24.1 by in situ hybridization. Chu, F.F., Rohan de Silva, H.A., Esworthy, R.S., Boteva, K.K., Walters, C.E., Roses, A., Rao, P.N., Pettenati, M.J. Genomics (1996) [Pubmed]
  21. Glutathione peroxidase isoforms as part of the local antioxidative defense system in normal and Barrett's esophagus. Mörk, H., Scheurlen, M., Al-Taie, O., Zierer, A., Kraus, M., Schöttker, K., Jakob, F., Köhrle, J. Int. J. Cancer (2003) [Pubmed]
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