Biology:Peroxiredoxin 2
From HandWiki
Short description: Protein-coding gene in the species Homo sapiens
Generic protein structure example |
Peroxiredoxin-2 is a protein that in humans is encoded by the PRDX2 gene.[1][2]
PRDX2 encodes a member of the peroxiredoxin family of antioxidant enzymes, which reduce hydrogen peroxide and alkyl hydroperoxides. The encoded protein may play an antioxidant protective role in cells, and may contribute to the antiviral activity of CD8(+) T-cells. This protein may have a proliferative effect and play a role in cancer development or progression. The crystal structure of this protein has been resolved to 0.27 nm (= 2.7 angstroms). Transcript variants encoding distinct isoforms have been identified for this gene.[2]
References
- ↑ "Localization of TDPX1, a human homologue of the yeast thioredoxin-dependent peroxide reductase gene (TPX), to chromosome 13q12". Genomics 26 (3): 602–6. Aug 1995. doi:10.1016/0888-7543(95)80183-M. PMID 7607688.
- ↑ 2.0 2.1 "Entrez Gene: PRDX2 peroxiredoxin 2". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7001.
Further reading
- Yao Y, Taylor M, Davey F, RenY, Aiton J , Coote P, Chen X, Yan SD & Gunn-Moore FJ. (2007). "Interaction of Amyloid binding Alcohol Dehydrogenase/Aβ mediates up-regulation of peroxiredoxin II in the brains of Alzheimer's disease patients and a transgenic Alzheimer's disease mouse model.". Molecular and Cellular Neuroscience 35 (2): 377–82. doi:10.1016/j.mcn.2007.03.013. PMID 17490890.
- "Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes.". Electrophoresis 13 (12): 960–9. 1993. doi:10.1002/elps.11501301199. PMID 1286667.
- "Cloning and sequence analysis of candidate human natural killer-enhancing factor genes.". Immunogenetics 40 (2): 129–34. 1994. doi:10.1007/BF00188176. PMID 8026862.
- "Cloning and sequencing of thiol-specific antioxidant from mammalian brain: alkyl hydroperoxide reductase and thiol-specific antioxidant define a large family of antioxidant enzymes.". Proc. Natl. Acad. Sci. U.S.A. 91 (15): 7017–21. 1994. doi:10.1073/pnas.91.15.7017. PMID 8041738.
- "Purification and characterization of thiol-specific antioxidant protein from human red blood cell: a new type of antioxidant protein.". Biochem. Biophys. Res. Commun. 199 (1): 199–206. 1994. doi:10.1006/bbrc.1994.1214. PMID 8123012.
- "The thiol-specific antioxidant protein from human brain: gene cloning and analysis of conserved cysteine regions.". Gene 140 (2): 279–84. 1994. doi:10.1016/0378-1119(94)90558-4. PMID 8144038.
- "Plasma and red blood cell protein maps: update 1993.". Electrophoresis 14 (11): 1223–31. 1994. doi:10.1002/elps.11501401183. PMID 8313871.
- "Glutathione-linked thiol peroxidase activity of human serum albumin: a possible antioxidant role of serum albumin in blood plasma.". Biochem. Biophys. Res. Commun. 222 (2): 619–25. 1996. doi:10.1006/bbrc.1996.0793. PMID 8670254.
- "A two-dimensional gel database of human colon carcinoma proteins.". Electrophoresis 18 (3–4): 605–13. 1997. doi:10.1002/elps.1150180344. PMID 9150948.
- "Chemokines are the main proinflammatory mediators in human monocytes activated by Staphylococcus aureus, peptidoglycan, and endotoxin.". J. Biol. Chem. 275 (27): 20260–7. 2000. doi:10.1074/jbc.M909168199. PMID 10751418.
- "Interaction of human thiol-specific antioxidant protein 1 with erythrocyte plasma membrane.". Biochemistry 39 (23): 6944–50. 2000. doi:10.1021/bi000034j. PMID 10841776.
- "Crystal structure of decameric 2-Cys peroxiredoxin from human erythrocytes at 1.7 A resolution.". Structure 8 (6): 605–15. 2000. doi:10.1016/S0969-2126(00)00147-7. PMID 10873855.
- "Comparison of the decameric structure of peroxiredoxin-II by transmission electron microscopy and X-ray crystallography.". Biochim. Biophys. Acta 1547 (2): 221–34. 2001. doi:10.1016/s0167-4838(01)00184-4. PMID 11410278.
- "Overexpression of peroxiredoxin in human breast cancer.". Anticancer Res. 21 (3B): 2085–90. 2001. PMID 11497302.
- "Protein levels of human peroxiredoxin subtypes in brains of patients with Alzheimer's disease and Down syndrome.". J. Neural Transm. Suppl. (61): 223–35. 2002. doi:10.1007/978-3-7091-6262-0_18. ISBN 978-3-211-83704-7. PMID 11771746.
- "Proteomics analysis of cellular response to oxidative stress. Evidence for in vivo overoxidation of peroxiredoxins at their active site.". J. Biol. Chem. 277 (22): 19396–401. 2002. doi:10.1074/jbc.M106585200. PMID 11904290.
- "Identification of new proteins in follicular fluid of mature human follicles.". Electrophoresis 23 (7–8): 1197–202. 2002. doi:10.1002/1522-2683(200204)23:7/8<1197::AID-ELPS1197>3.0.CO;2-2. PMID 11981869.
- "Nonredundant antioxidant defense by multiple two-cysteine peroxiredoxins in human prostate cancer cells.". Mol. Med. 8 (2): 95–102. 2002. doi:10.1007/BF03402079. PMID 12080185.
- "HIV-1 antiviral activity of recombinant natural killer cell enhancing factors, NKEF-A and NKEF-B, members of the peroxiredoxin family.". J. Biol. Chem. 278 (3): 1569–74. 2003. doi:10.1074/jbc.M209964200. PMID 12421812.
- "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.