Glutathione peroxidase 2

Glutathione peroxidase 2 is an enzyme that in humans is encoded by the GPX2 gene.

GPX2
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2HE3
Identifiers
Aliases	GPX2, GI-GPx, GPRP, GPRP-2, GPx-2, GPx-GI, GSHPX-GI, GSHPx-2, glutathione peroxidase 2
External IDs	OMIM: 138319; MGI: 106609; HomoloGene: 20479; GeneCards: GPX2; OMA:GPX2 - orthologs
Gene location (Human) Chr. Chromosome 14 (human) Band 14q23.3 Start 64,939,152 bp End 64,942,746 bp
Gene location (Mouse) Chr. Chromosome 12 (mouse) Band 12 C3|12 33.73 cM Start 76,839,107 bp End 76,842,273 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in gallbladder rectum mucosa of sigmoid colon mucosa of transverse colon pancreatic ductal cell islet of Langerhans mucosa of ileum nasal epithelium right lobe of liver olfactory zone of nasal mucosa Top expressed in crypt of lieberkuhn of small intestine esophagus large intestine colon duodenum jejunum left colon mucous cell of stomach epithelium of bronchus epithelium of stomach More reference expression data BioGPS More reference expression data
Gene ontology Molecular function electron transfer activity oxidoreductase activity glutathione peroxidase activity peroxidase activity Cellular component cytoplasm cytosol Biological process response to oxidative stress cellular oxidant detoxification cellular response to oxidative stress electron transport chain Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 2877 14776 Ensembl ENSG00000176153 ENSMUSG00000042808 UniProt P18283 Q9JHC0 RefSeq (mRNA) NM_002083 NM_030677 RefSeq (protein) NP_002074 NP_109602 Location (UCSC) Chr 14: 64.94 – 64.94 Mb Chr 12: 76.84 – 76.84 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

This gene is a member of the glutathione peroxidase family encoding a selenium-dependent glutathione peroxidase that is one of two isoenzymes responsible for the majority of the glutathione-dependent hydrogen peroxide-reducing activity in the epithelium of the gastrointestinal tract. Studies in knockout mice indicate that mRNA expression levels respond to luminal microflora, suggesting a role of the ileal glutathione peroxidases in preventing inflammation in the GI tract.

The antioxidant enzyme glutathione peroxidase 2 (Gpx2) is one out of eight known glutathione peroxidases (Gpx1-8) in humans. Mammalian Gpx1, GPx2 (this protein), Gpx3, and Gpx4 have been shown to be selenium-containing enzymes, whereas Gpx6 is a selenoprotein in humans with cysteine-containing homologues in rodents. In selenoproteins, the 21st amino acid selenocysteine is inserted in the nascent polypeptide chain during the process of translational recoding of the UGA stop codon.

Further reading

• Akasaka M, Mizoguchi J, Takahashi K (1990). "A human cDNA sequence of a novel glutathione peroxidase-related protein". Nucleic Acids Res. 18 (15): 4619. doi:10.1093/nar/18.15.4619. PMC 331311. PMID 2388849.
• Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
• Chu FF, Rohan de Silva HA, Esworthy RS, et al. (1997). "Polymorphism and chromosomal localization of the GI-form of human glutathione peroxidase (GPX2) on 14q24.1 by in situ hybridization". Genomics. 32 (2): 272–6. doi:10.1006/geno.1996.0115. PMID 8833155.
• Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
• Opalenik SR, Ding Q, Mallery SR, Thompson JA (1998). "Glutathione depletion associated with the HIV-1 TAT protein mediates the extracellular appearance of acidic fibroblast growth factor". Arch. Biochem. Biophys. 351 (1): 17–26. doi:10.1006/abbi.1997.0566. PMID 9501919.
• Choi J, Liu RM, Kundu RK, et al. (2000). "Molecular mechanism of decreased glutathione content in human immunodeficiency virus type 1 Tat-transgenic mice". J. Biol. Chem. 275 (5): 3693–8. doi:10.1074/jbc.275.5.3693. PMID 10652368.
• Kelner MJ, Bagnell RD, Montoya MA, Lanham KA (2000). "Structural organization of the human gastrointestinal glutathione peroxidase (GPX2) promoter and 3'-nontranscribed region: transcriptional response to exogenous redox agents". Gene. 248 (1–2): 109–16. doi:10.1016/S0378-1119(00)00137-2. PMID 10806356.
• Richard MJ, Guiraud P, Didier C, et al. (2001). "Human immunodeficiency virus type 1 Tat protein impairs selenoglutathione peroxidase expression and activity by a mechanism independent of cellular selenium uptake: consequences on cellular resistance to UV-A radiation". Arch. Biochem. Biophys. 386 (2): 213–20. doi:10.1006/abbi.2000.2197. PMID 11368344.
• Komatsu H, Okayasu I, Mitomi H, et al. (2001). "Immunohistochemical detection of human gastrointestinal glutathione peroxidase in normal tissues and cultured cells with novel mouse monoclonal antibodies". J. Histochem. Cytochem. 49 (6): 759–66. doi:10.1177/002215540104900609. PMID 11373322.
• Florian S, Wingler K, Schmehl K, et al. (2002). "Cellular and subcellular localization of gastrointestinal glutathione peroxidase in normal and malignant human intestinal tissue". Free Radic. Res. 35 (6): 655–63. doi:10.1080/10715760100301181. PMID 11811519. S2CID 22845933.
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Müller C, Wingler K, Brigelius-Flohé R (2003). "3'UTRs of glutathione peroxidases differentially affect selenium-dependent mRNA stability and selenocysteine incorporation efficiency". Biol. Chem. 384 (1): 11–8. doi:10.1515/BC.2003.002. PMID 12674495. S2CID 24693834.
• Esworthy RS, Binder SW, Doroshow JH, Chu FF (2003). "Microflora trigger colitis in mice deficient in selenium-dependent glutathione peroxidase and induce Gpx2 gene expression". Biol. Chem. 384 (4): 597–607. doi:10.1515/BC.2003.067. PMID 12751789. S2CID 25131807.
• Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
• Price TO, Ercal N, Nakaoke R, Banks WA (2005). "HIV-1 viral proteins gp120 and Tat induce oxidative stress in brain endothelial cells". Brain Res. 1045 (1–2): 57–63. doi:10.1016/j.brainres.2005.03.031. PMID 15910762. S2CID 7362454.
• Banning A, Deubel S, Kluth D, et al. (2005). "The GI-GPx gene is a target for Nrf2". Mol. Cell. Biol. 25 (12): 4914–23. doi:10.1128/MCB.25.12.4914-4923.2005. PMC 1140597. PMID 15923610.
• Yan W, Chen X (2006). "GPX2, a direct target of p63, inhibits oxidative stress-induced apoptosis in a p53-dependent manner". J. Biol. Chem. 281 (12): 7856–62. doi:10.1074/jbc.M512655200. PMID 16446369.
• Singh A, Rangasamy T, Thimmulappa RK, et al. (2007). "Glutathione peroxidase 2, the major cigarette smoke-inducible isoform of GPX in lungs, is regulated by Nrf2". Am. J. Respir. Cell Mol. Biol. 35 (6): 639–50. doi:10.1165/rcmb.2005-0325OC. PMC 2643293. PMID 16794261.