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词条 GPX2 (gene)
释义

  1. References

  2. Further reading

{{Infobox_gene}}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

1. ^{{cite journal |vauthors=Chu FF, Doroshow JH, Esworthy RS | title = Expression, characterization, and tissue distribution of a new cellular selenium-dependent glutathione peroxidase, GSHPx-GI | journal = J Biol Chem | volume = 268 | issue = 4 | pages = 2571–6 |date=Mar 1993 | pmid = 8428933 | pmc = | doi = }}
2. ^{{cite journal | author = Chu FF | title = The human glutathione peroxidase genes GPX2, GPX3, and GPX4 map to chromosomes 14, 5, and 19, respectively | journal = Cytogenet Cell Genet | volume = 66 | issue = 2 | pages = 96–8 |date=Feb 1994 | pmid = 8287691 | pmc = | doi =10.1159/000133675 }}
3. ^1 {{cite web | title = Entrez Gene: GPX2 glutathione peroxidase 2 (gastrointestinal)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2877| accessdate = }}

Further reading

{{refbegin | 2}}
  • {{cite journal |vauthors=Akasaka M, Mizoguchi J, Takahashi K |title=A human cDNA sequence of a novel glutathione peroxidase-related protein. |journal=Nucleic Acids Res. |volume=18 |issue= 15 |pages= 4619 |year= 1990 |pmid= 2388849 |doi= 10.1093/nar/18.15.4619| pmc=331311 }}
  • {{cite journal |vauthors=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1–2 |pages= 171–4 |year= 1994 |pmid= 8125298 |doi=10.1016/0378-1119(94)90802-8 }}
  • {{cite journal |vauthors=Chu FF, Rohan de Silva HA, Esworthy RS, etal |title=Polymorphism and chromosomal localization of the GI-form of human glutathione peroxidase (GPX2) on 14q24.1 by in situ hybridization. |journal=Genomics |volume=32 |issue= 2 |pages= 272–6 |year= 1997 |pmid= 8833155 |doi= 10.1006/geno.1996.0115 }}
  • {{cite journal |vauthors=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, etal |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1–2 |pages= 149–56 |year= 1997 |pmid= 9373149 |doi=10.1016/S0378-1119(97)00411-3 }}
  • {{cite journal |vauthors=Opalenik SR, Ding Q, Mallery SR, Thompson JA |title=Glutathione depletion associated with the HIV-1 TAT protein mediates the extracellular appearance of acidic fibroblast growth factor. |journal=Arch. Biochem. Biophys. |volume=351 |issue= 1 |pages= 17–26 |year= 1998 |pmid= 9501919 |doi= 10.1006/abbi.1997.0566 }}
  • {{cite journal |vauthors=Choi J, Liu RM, Kundu RK, etal |title=Molecular mechanism of decreased glutathione content in human immunodeficiency virus type 1 Tat-transgenic mice. |journal=J. Biol. Chem. |volume=275 |issue= 5 |pages= 3693–8 |year= 2000 |pmid= 10652368 |doi=10.1074/jbc.275.5.3693 }}
  • {{cite journal |vauthors=Kelner MJ, Bagnell RD, Montoya MA, Lanham KA |title=Structural organization of the human gastrointestinal glutathione peroxidase (GPX2) promoter and 3'-nontranscribed region: transcriptional response to exogenous redox agents. |journal=Gene |volume=248 |issue= 1–2 |pages= 109–16 |year= 2000 |pmid= 10806356 |doi=10.1016/S0378-1119(00)00137-2 }}
  • {{cite journal |vauthors=Richard MJ, Guiraud P, Didier C, etal |title=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. |journal=Arch. Biochem. Biophys. |volume=386 |issue= 2 |pages= 213–20 |year= 2001 |pmid= 11368344 |doi= 10.1006/abbi.2000.2197 }}
  • {{cite journal |vauthors=Komatsu H, Okayasu I, Mitomi H, etal |title=Immunohistochemical detection of human gastrointestinal glutathione peroxidase in normal tissues and cultured cells with novel mouse monoclonal antibodies. |journal=J. Histochem. Cytochem. |volume=49 |issue= 6 |pages= 759–66 |year= 2001 |pmid= 11373322 |doi= 10.1177/002215540104900609}}
  • {{cite journal |vauthors=Florian S, Wingler K, Schmehl K, etal |title=Cellular and subcellular localization of gastrointestinal glutathione peroxidase in normal and malignant human intestinal tissue. |journal=Free Radic. Res. |volume=35 |issue= 6 |pages= 655–63 |year= 2002 |pmid= 11811519 |doi=10.1080/10715760100301181 }}
  • {{cite journal |vauthors=Strausberg RL, Feingold EA, Grouse LH, etal |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 | pmc=139241 }}
  • {{cite journal |vauthors=Müller C, Wingler K, Brigelius-Flohé R |title=3'UTRs of glutathione peroxidases differentially affect selenium-dependent mRNA stability and selenocysteine incorporation efficiency. |journal=Biol. Chem. |volume=384 |issue= 1 |pages= 11–8 |year= 2003 |pmid= 12674495 |doi=10.1515/BC.2003.002 }}
  • {{cite journal |vauthors=Esworthy RS, Binder SW, Doroshow JH, Chu FF |title=Microflora trigger colitis in mice deficient in selenium-dependent glutathione peroxidase and induce Gpx2 gene expression. |journal=Biol. Chem. |volume=384 |issue= 4 |pages= 597–607 |year= 2003 |pmid= 12751789 |doi=10.1515/BC.2003.067 }}
  • {{cite journal |vauthors=Gerhard DS, Wagner L, Feingold EA, etal |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 | pmc=528928 }}
  • {{cite journal |vauthors=Price TO, Ercal N, Nakaoke R, Banks WA |title=HIV-1 viral proteins gp120 and Tat induce oxidative stress in brain endothelial cells. |journal=Brain Res. |volume=1045 |issue= 1–2 |pages= 57–63 |year= 2005 |pmid= 15910762 |doi= 10.1016/j.brainres.2005.03.031 }}
  • {{cite journal |vauthors=Banning A, Deubel S, Kluth D, etal |title=The GI-GPx gene is a target for Nrf2. |journal=Mol. Cell. Biol. |volume=25 |issue= 12 |pages= 4914–23 |year= 2005 |pmid= 15923610 |doi= 10.1128/MCB.25.12.4914-4923.2005 | pmc=1140597 }}
  • {{cite journal |vauthors=Yan W, Chen X |title=GPX2, a direct target of p63, inhibits oxidative stress-induced apoptosis in a p53-dependent manner. |journal=J. Biol. Chem. |volume=281 |issue= 12 |pages= 7856–62 |year= 2006 |pmid= 16446369 |doi= 10.1074/jbc.M512655200 }}
  • {{cite journal |vauthors=Singh A, Rangasamy T, Thimmulappa RK, etal |title=Glutathione peroxidase 2, the major cigarette smoke-inducible isoform of GPX in lungs, is regulated by Nrf2. |journal=Am. J. Respir. Cell Mol. Biol. |volume=35 |issue= 6 |pages= 639–50 |year= 2007 |pmid= 16794261 |doi= 10.1165/rcmb.2005-0325OC | pmc=2643293 }}
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2 : EC 1.11.1|Selenoproteins
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