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Gene Review

Glrx2  -  glutaredoxin 2 (thioltransferase)

Mus musculus

Synonyms: 1700010P22Rik, AI645710, Glutaredoxin-2, mitochondrial, Grx2
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Disease relevance of Glrx2


High impact information on Glrx2

  • Our findings indicate that Grx2 plays a central role in the response of mitochondria to both redox signals and oxidative stress by facilitating the interplay between the mitochondrial glutathione pool and protein thiols [2].
  • Quantitations reported establish differences among adult organs and embryonic stages, compare mRNA decay rates, explore the significance of alternative mRNA isoforms derived from TrxR1 and Grx2 genes, and examine the time-course expression upon superoxide stress promoted by paraquat [3].
  • The gene for human Grx2 consisted of four exons and three introns, spanned 10 kilobase pairs, and localized to chromosome 1q31.2-31 [1].
  • Western blot analysis of subcellular fractions from Jurkat cells with a specific anti-Grx2 antibody showed that human Grx2 was predominantly located in the nucleus but also present in the mitochondria [4].
  • These results demonstrate that dual activation of Ras/phosphoinositide 3-kinase and AP-1 cascades, which are mediated by Ref-1, is an essential component of the Grx2 mechanism of action [5].

Biological context of Glrx2

  • Most significantly, Grx2 catalyzed reversible protein glutathionylation/deglutathionylation over a wide range of GSH/GSSG ratios, from the reduced levels accessible under redox signaling to oxidized ratios only found under severe oxidative stress [2].
  • Grx2 over-expression protected cells against H2O2-mediated disruption of mitochondrial transmembrane potential [6].

Anatomical context of Glrx2

  • In this study we investigate Grx2 function by examining its potential peroxidase activity using lens epithelial cells (LEC). cDNA for human and mouse Grx2 was cloned into pET21d(+) vector and used to produce respective recombinant Grx2 for kinetic studies. cDNA for human Grx2 was transfected into human LEC and used for in vivo studies [6].

Analytical, diagnostic and therapeutic context of Glrx2


  1. Identification and characterization of a new mammalian glutaredoxin (thioltransferase), Grx2. Gladyshev, V.N., Liu, A., Novoselov, S.V., Krysan, K., Sun, Q.A., Kryukov, V.M., Kryukov, G.V., Lou, M.F. J. Biol. Chem. (2001) [Pubmed]
  2. Glutaredoxin 2 catalyzes the reversible oxidation and glutathionylation of mitochondrial membrane thiol proteins: implications for mitochondrial redox regulation and antioxidant DEFENSE. Beer, S.M., Taylor, E.R., Brown, S.E., Dahm, C.C., Costa, N.J., Runswick, M.J., Murphy, M.P. J. Biol. Chem. (2004) [Pubmed]
  3. Absolute gene expression patterns of thioredoxin and glutaredoxin redox systems in mouse. Jurado, J., Prieto-Alamo, M.J., Madrid-Rísquez, J., Pueyo, C. J. Biol. Chem. (2003) [Pubmed]
  4. Cloning and expression of a novel human glutaredoxin (Grx2) with mitochondrial and nuclear isoforms. Lundberg, M., Johansson, C., Chandra, J., Enoksson, M., Jacobsson, G., Ljung, J., Johansson, M., Holmgren, A. J. Biol. Chem. (2001) [Pubmed]
  5. Glutaredoxin protects cerebellar granule neurons from dopamine-induced apoptosis by dual activation of the ras-phosphoinositide 3-kinase and jun n-terminal kinase pathways. Daily, D., Vlamis-Gardikas, A., Offen, D., Mittelman, L., Melamed, E., Holmgren, A., Barzilai, A. J. Biol. Chem. (2001) [Pubmed]
  6. Mitochondrial thioltransferase (glutaredoxin 2) has GSH-dependent and thioredoxin reductase-dependent peroxidase activities in vitro and in lens epithelial cells. Fernando, M.R., Lechner, J.M., L??fgren, S., Gladyshev, V.N., Lou, M.F. FASEB J. (2006) [Pubmed]
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