Biology:GPX2 (gene)
 Generic protein structure example |
Glutathione peroxidase 2 is an enzyme that in humans is encoded by the GPX2 gene.[1][2][3]
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.[3]
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.
References
- ↑ "Expression, characterization, and tissue distribution of a new cellular selenium-dependent glutathione peroxidase, GSHPx-GI". J Biol Chem 268 (4): 2571–6. Mar 1993. doi:10.1016/S0021-9258(18)53812-6. PMID 8428933.
- ↑ Chu FF (Feb 1994). "The human glutathione peroxidase genes GPX2, GPX3, and GPX4 map to chromosomes 14, 5, and 19, respectively". Cytogenet Cell Genet 66 (2): 96–8. doi:10.1159/000133675. PMID 8287691.
- ↑ 3.0 3.1 "Entrez Gene: GPX2 glutathione peroxidase 2 (gastrointestinal)". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2877.
Further reading
- "A human cDNA sequence of a novel glutathione peroxidase-related protein.". Nucleic Acids Res. 18 (15): 4619. 1990. doi:10.1093/nar/18.15.4619. PMID 2388849.
- "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides.". Gene 138 (1–2): 171–4. 1994. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
- "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. 1997. doi:10.1006/geno.1996.0115. PMID 8833155.
- "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library.". Gene 200 (1–2): 149–56. 1997. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
- "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. 1998. doi:10.1006/abbi.1997.0566. PMID 9501919.
- "Molecular mechanism of decreased glutathione content in human immunodeficiency virus type 1 Tat-transgenic mice.". J. Biol. Chem. 275 (5): 3693–8. 2000. doi:10.1074/jbc.275.5.3693. PMID 10652368.
- "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. 2000. doi:10.1016/S0378-1119(00)00137-2. PMID 10806356.
- "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. 2001. doi:10.1006/abbi.2000.2197. PMID 11368344.
- "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. 2001. doi:10.1177/002215540104900609. PMID 11373322.
- "Cellular and subcellular localization of gastrointestinal glutathione peroxidase in normal and malignant human intestinal tissue.". Free Radic. Res. 35 (6): 655–63. 2002. doi:10.1080/10715760100301181. PMID 11811519.
- "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. 2003. doi:10.1073/pnas.242603899. PMID 12477932. Bibcode: 2002PNAS...9916899M.
- "3'UTRs of glutathione peroxidases differentially affect selenium-dependent mRNA stability and selenocysteine incorporation efficiency.". Biol. Chem. 384 (1): 11–8. 2003. doi:10.1515/BC.2003.002. PMID 12674495.
- "Microflora trigger colitis in mice deficient in selenium-dependent glutathione peroxidase and induce Gpx2 gene expression.". Biol. Chem. 384 (4): 597–607. 2003. doi:10.1515/BC.2003.067. PMID 12751789.
- "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. 2004. doi:10.1101/gr.2596504. PMID 15489334.
- "HIV-1 viral proteins gp120 and Tat induce oxidative stress in brain endothelial cells.". Brain Res. 1045 (1–2): 57–63. 2005. doi:10.1016/j.brainres.2005.03.031. PMID 15910762.
- "The GI-GPx gene is a target for Nrf2.". Mol. Cell. Biol. 25 (12): 4914–23. 2005. doi:10.1128/MCB.25.12.4914-4923.2005. PMID 15923610.
- "GPX2, a direct target of p63, inhibits oxidative stress-induced apoptosis in a p53-dependent manner.". J. Biol. Chem. 281 (12): 7856–62. 2006. doi:10.1074/jbc.M512655200. PMID 16446369.
- "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. 2007. doi:10.1165/rcmb.2005-0325OC. PMID 16794261.
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