GLRX2

From Wikipedia, the free encyclopedia

Glutaredoxin 2

PDB rendering based on 2cq9.

Available structures: 2cq9, 2fls, 2ht9

Identifiers

Symbol(s)

GLRX2; GRX2; bA101E13.1

External IDs

OMIM: 606820 MGI: 1916617 HomoloGene: 41098

Gene ontology
Molecular Function:	• iron ion binding • arsenate reductase (glutaredoxin) activity • electron donor activity • protein disulfide oxidoreductase activity • glutathione disulfide oxidoreductase activity • thiol-disulfide exchange intermediate activity • metal ion binding • 2 iron, 2 sulfur cluster binding
Cellular Component:	• nucleus • mitochondrion
Biological Process:	• electron transport • protein thiol-disulfide exchange • glutathione metabolic process • transport • apoptosis • redox signal response • response to temperature stimulus • response to pH • regulation of signal transduction • response to organic substance • cell differentiation • regulation of cell redox homeostasis • DNA protection • response to hydrogen peroxide • regulation of transcription

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_016066 (mRNA)
NP_057150 (protein)

NM_001038592 (mRNA)
NP_001033681 (protein)

Location

Chr 1: 191.33 - 191.34 Mb

Chr 1: 145.5 - 145.51 Mb

Pubmed search

[1]

[2]

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]

[edit] References

^ ^a ^b Entrez Gene: GLRX2 glutaredoxin 2.

[edit] 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.