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Gene Review

GLRX2  -  glutaredoxin 2

Homo sapiens

Synonyms: CGI-133, GRX2, Glutaredoxin-2, mitochondrial, bA101E13.1
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High impact information on GLRX2


Biological context of GLRX2

  • The properties that permit GLRX2, and not other glutaredoxins, to form an iron-sulfur-containing dimer are likely due to the proline-to-serine substitution in the active site motif, allowing the main chain more flexibility in this area and providing polar interaction with the stabilizing glutathione [3].
  • Human mitochondrial glutaredoxin 2 (GLRX2), which controls intracellular redox balance and apoptosis, exists in a dynamic equilibrium of enzymatically active monomers and quiescent dimers [3].
  • These results indicate a crucial role of Grx2 in the regulation of the mitochondrial redox status and regulation of cell death at the mitochondrial checkpoint [2].
  • Alternative splicing forms of mammalian Grx2 mRNAs were identified that differed in sequences upstream of exon 2 [4].
  • Grx2 was encoded in the genomes of mammals and birds and expressed in a variety of cell types [4].
  • Alternative isoforms of Grx2, derived from alternative transcription initiation and splicing, have been demonstrated in human and mouse [5] [6].

Anatomical context of GLRX2

  • Here, we have successfully established a method to silence the expression of Grx2 in HeLa cells by using short interfering RNA to study its role in the cell [2].
  • The mitochondrial leader sequence was also present in mouse and rat Grx2 sequences and was shown to direct either Grx2 or green fluorescent protein to mitochondria [4].
  • 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 [7].
  • Coimmunoprecipitation of radiolabeled iron with Grx2 from human cell lines indicated the presence of the cluster in vivo [1].
  • Both Grx1 and Grx2 could be detected at the mRNA and protein level in cultured human lung cells, but only Grx1 was prominently expressed in lung homogenates and alveolar macrophages [8].

Associations of GLRX2 with chemical compounds


Other interactions of GLRX2


Analytical, diagnostic and therapeutic context of GLRX2


  1. Characterization of human glutaredoxin 2 as iron-sulfur protein: a possible role as redox sensor. Lillig, C.H., Berndt, C., Vergnolle, O., Lönn, M.E., Hudemann, C., Bill, E., Holmgren, A. Proc. Natl. Acad. Sci. U.S.A. (2005) [Pubmed]
  2. Short interfering RNA-mediated silencing of glutaredoxin 2 increases the sensitivity of HeLa cells toward doxorubicin and phenylarsine oxide. Lillig, C.H., Lönn, M.E., Enoksson, M., Fernandes, A.P., Holmgren, A. Proc. Natl. Acad. Sci. U. S. A. (2004) [Pubmed]
  3. Reversible Sequestration of Active Site Cysteines in a 2Fe-2S-bridged Dimer Provides a Mechanism for Glutaredoxin 2 Regulation in Human Mitochondria. Johansson, C., Kavanagh, K.L., Gileadi, O., Oppermann, U. J. Biol. Chem. (2007) [Pubmed]
  4. 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]
  5. Expression pattern of human glutaredoxin 2 isoforms: identification and characterization of two testis/cancer cell-specific isoforms. Lönn, M.E., Hudemann, C., Berndt, C., Cherkasov, V., Capani, F., Holmgren, A., Lillig, C.H. Antioxid. Redox. Signal. (2008) [Pubmed]
  6. Identification, expression pattern, and characterization of mouse glutaredoxin 2 isoforms. Hudemann, C., Lönn, M.E., Godoy, J.R., Zahedi Avval, F., Capani, F., Holmgren, A., Lillig, C.H. Antioxid. Redox. Signal. (2009) [Pubmed]
  7. 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]
  8. 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. Peltoniemi, M., Kaarteenaho-Wiik, R., Säily, M., Sormunen, R., Pääkkö, P., Holmgren, A., Soini, Y., Kinnula, V.L. Hum. Pathol. (2004) [Pubmed]
  9. 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]
  10. Human mitochondrial glutaredoxin reduces S-glutathionylated proteins with high affinity accepting electrons from either glutathione or thioredoxin reductase. Johansson, C., Lillig, C.H., Holmgren, A. J. Biol. Chem. (2004) [Pubmed]
  11. Solution structure of Escherichia coli glutaredoxin-2 shows similarity to mammalian glutathione-S-transferases. Xia, B., Vlamis-Gardikas, A., Holmgren, A., Wright, P.E., Dyson, H.J. J. Mol. Biol. (2001) [Pubmed]
  12. Human glutaredoxin 2 affinity tag for recombinant peptide and protein purification. Lundberg, M., Holmgren, A., Johansson, M. Protein Expr. Purif. (2006) [Pubmed]
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