GLRX2

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Glutaredoxin 2
PDB rendering based on 2cq9.
Available structures
PDB Ortholog search: Template:Homologene2PDBe PDBe, Template:Homologene2uniprot RCSB
Identifiers
Symbols GLRX2 ; GRX2; bA101E13.1
External IDs Template:OMIM5 Template:MGI HomoloGene41098
RNA expression pattern
More reference expression data
Orthologs
Template:GNF Ortholog box
Species Human Mouse
Entrez n/a n/a
Ensembl n/a n/a
UniProt n/a n/a
RefSeq (mRNA) n/a n/a
RefSeq (protein) n/a n/a
Location (UCSC) n/a n/a
PubMed search n/a n/a

Glutaredoxin 2, also known as GLRX2, is a human gene.[1]

Glutaredoxins (e.g., GLRX; MIM 600443) are a family of glutathione-dependent hydrogen donors that participate in a variety of cellular redox reactions.[supplied by OMIM][1]

References

  1. 1.0 1.1 "Entrez Gene: GLRX2 glutaredoxin 2".

Further reading

  • Davis DA, Newcomb FM, Starke DW; et al. (1997). "Thioltransferase (glutaredoxin) is detected within HIV-1 and can regulate the activity of glutathionylated HIV-1 protease in vitro". J. Biol. Chem. 272 (41): 25935–40. PMID 9325327.
  • Lai CH, Chou CY, Ch'ang LY; et al. (2000). "Identification of novel human genes evolutionarily conserved in Caenorhabditis elegans by comparative proteomics". Genome Res. 10 (5): 703–13. PMID 10810093.
  • Lundberg M, Johansson C, Chandra J; et al. (2001). "Cloning and expression of a novel human glutaredoxin (Grx2) with mitochondrial and nuclear isoforms". J. Biol. Chem. 276 (28): 26269–75. doi:10.1074/jbc.M011605200. PMID 11297543.
  • Gladyshev VN, Liu A, Novoselov SV; et al. (2001). "Identification and characterization of a new mammalian glutaredoxin (thioltransferase), Grx2". J. Biol. Chem. 276 (32): 30374–80. doi:10.1074/jbc.M100020200. PMID 11397793.
  • 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. doi:10.1073/pnas.242603899. PMID 12477932.
  • Johansson C, Lillig CH, Holmgren A (2004). "Human mitochondrial glutaredoxin reduces S-glutathionylated proteins with high affinity accepting electrons from either glutathione or thioredoxin reductase". J. Biol. Chem. 279 (9): 7537–43. doi:10.1074/jbc.M312719200. PMID 14676218.
  • Lundberg M, Fernandes AP, Kumar S, Holmgren A (2004). "Cellular and plasma levels of human glutaredoxin 1 and 2 detected by sensitive ELISA systems". Biochem. Biophys. Res. Commun. 319 (3): 801–9. doi:10.1016/j.bbrc.2004.04.199. PMID 15184054.
  • Peltoniemi M, Kaarteenaho-Wiik R, Säily M; et al. (2004). "Expression of glutaredoxin is highly cell specific in human lung and is decreased by transforming growth factor-beta in vitro and in interstitial lung diseases in vivo". Hum. Pathol. 35 (8): 1000–7. PMID 15297967.
  • Lillig CH, Lönn ME, Enoksson M; et al. (2004). "Short interfering RNA-mediated silencing of glutaredoxin 2 increases the sensitivity of HeLa cells toward doxorubicin and phenylarsine oxide". Proc. Natl. Acad. Sci. U.S.A. 101 (36): 13227–32. doi:10.1073/pnas.0401896101. PMID 15328416.
  • 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. PMID 15489334.
  • Enoksson M, Fernandes AP, Prast S; et al. (2005). "Overexpression of glutaredoxin 2 attenuates apoptosis by preventing cytochrome c release". Biochem. Biophys. Res. Commun. 327 (3): 774–9. doi:10.1016/j.bbrc.2004.12.067. PMID 15649413.
  • Lillig CH, Berndt C, Vergnolle O; et al. (2005). "Characterization of human glutaredoxin 2 as iron-sulfur protein: a possible role as redox sensor". Proc. Natl. Acad. Sci. U.S.A. 102 (23): 8168–73. doi:10.1073/pnas.0500735102. PMID 15917333.
  • Gregory SG, Barlow KF, McLay KE; et al. (2006). "The DNA sequence and biological annotation of human chromosome 1". Nature. 441 (7091): 315–21. doi:10.1038/nature04727. PMID 16710414.
  • Fernando MR, Lechner JM, Löfgren S; et al. (2007). "Mitochondrial thioltransferase (glutaredoxin 2) has GSH-dependent and thioredoxin reductase-dependent peroxidase activities in vitro and in lens epithelial cells". FASEB J. 20 (14): 2645–7. doi:10.1096/fj.06-5919fje. PMID 17065220.
  • Berndt C, Hudemann C, Hanschmann EM; et al. (2007). "How does iron-sulfur cluster coordination regulate the activity of human glutaredoxin 2?". Antioxid. Redox Signal. 9 (1): 151–7. doi:10.1089/ars.2007.9.151. PMID 17115894.
  • Johansson C, Kavanagh KL, Gileadi O, Oppermann U (2007). "Reversible sequestration of active site cysteines in a 2Fe-2S-bridged dimer provides a mechanism for glutaredoxin 2 regulation in human mitochondria". J. Biol. Chem. 282 (5): 3077–82. doi:10.1074/jbc.M608179200. PMID 17121859.
  • Sagemark J, Elgán TH, Bürglin TR; et al. (2007). "Redox properties and evolution of human glutaredoxins". Proteins. 68 (4): 879–92. doi:10.1002/prot.21416. PMID 17546662.

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