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Gene Review

GLRX  -  glutaredoxin (thioltransferase)

Homo sapiens

Synonyms: GRX, GRX1, Glutaredoxin-1, TTase-1, Thioltransferase-1
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Disease relevance of GLRX


High impact information on GLRX


Chemical compound and disease context of GLRX


Biological context of GLRX


Anatomical context of GLRX

  • In this study 30-min exposure of H9 and Jurkat cells to cadmium inhibited intracellular protein-SSG reduction, and this correlated with inhibition of the thioltransferase system, consistent with thioltransferase being the primary intracellular catalyst of deglutathionylation [12].
  • Most importantly, it has been demonstrated that thioltransferase has a remarkable resistance to oxidation (H(2)O(2)) in cultured human and rabbit lens epithelial cells under oxidative stress conditions when other oxidation defense systems of GSH peroxidase and GSH reductase are severely inactivated [13].
  • The intense immunostaining concomitant with the presence of pinopodes suggests that Grx plays an important role during implantation, possibly by protecting the epithelial cells from apoptotic actions of the trophoblast cells [14].
  • Immunohistochemical localization of glutaredoxin and thioredoxin in human endometrium: a possible association with pinopodes [14].
  • Both Grx1 and Grx2 were present in placenta extracts and in cell lysates prepared from various tumor cell lines [15].

Associations of GLRX with chemical compounds


Physical interactions of GLRX


Enzymatic interactions of GLRX

  • To investigate the catalytic mechanism of the Grx-dependent reduction of hydroperoxides catalyzed by Prx, a series of cysteinic mutants was constructed [17].
  • Here we show that restoration of the DNA-binding activity of oxidized NFI-C can be catalyzed in vitro by the cellular enzyme thioltransferase (glutaredoxin) coupled to GSH and GSSG reductase [18].

Regulatory relationships of GLRX

  • GRX-overexpressing cells demonstrated resistance to glucose deprivation-induced cytotoxicity and decreased activation of c-Jun N-terminal kinase (JNK1) [11].
  • In A549 cells, Grx1 was down-regulated by TGF-beta, whereas TNF-alpha caused no clear effect [3].
  • Abeta toxicity was inhibited by insulin-like growth factor-I (IGF-I) and by overexpressing GRX1 or TRX1 [2].
  • Also to examine whether depleting the primary cellular antioxidant glutathione (GSH) in these cells has any influence on TTase expression under the same conditions [19].
  • It is also shown that the efficiency of S-glutathionylation of either native or oxidised GAPDH is enhanced by the presence of recombinant glutaredoxin (thiol transferase) of either bacterial or human origin [20].

Other interactions of GLRX


Analytical, diagnostic and therapeutic context of GLRX


  1. 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]
  2. Involvement of glutaredoxin-1 and thioredoxin-1 in beta-amyloid toxicity and Alzheimer's disease. Akterin, S., Cowburn, R.F., Miranda-Vizuete, A., Jiménez, A., Bogdanovic, N., Winblad, B., Cedazo-Minguez, A. Cell Death Differ. (2006) [Pubmed]
  3. 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]
  4. 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]
  5. Phloem sap proteins from cucurbita maxima and ricinus communis have the capacity to traffic cell to cell through plasmodesmata. Balachandran, S., Xiang, Y., Schobert, C., Thompson, G.A., Lucas, W.J. Proc. Natl. Acad. Sci. U.S.A. (1997) [Pubmed]
  6. Glutaredoxin homolog encoded by vaccinia virus is a virion-associated enzyme with thioltransferase and dehydroascorbate reductase activities. Ahn, B.Y., Moss, B. Proc. Natl. Acad. Sci. U.S.A. (1992) [Pubmed]
  7. Glutaredoxins: glutathione-dependent redox enzymes with functions far beyond a simple thioredoxin backup system. Fernandes, A.P., Holmgren, A. Antioxid. Redox Signal. (2004) [Pubmed]
  8. High-level expression of fully active human glutaredoxin (thioltransferase) in E. coli and characterization of Cys7 to Ser mutant protein. Padilla, C.A., Spyrou, G., Holmgren, A. FEBS Lett. (1996) [Pubmed]
  9. Thioltransferase overexpression increases resistance of MCF-7 cells to adriamycin. Meyer, E.B., Wells, W.W. Free Radic. Biol. Med. (1999) [Pubmed]
  10. Crystal Structures of a Poxviral Glutaredoxin in the Oxidized and Reduced States Show Redox-correlated Structural Changes. Bacik, J.P., Hazes, B. J. Mol. Biol. (2007) [Pubmed]
  11. Role of glutaredoxin in metabolic oxidative stress. Glutaredoxin as a sensor of oxidative stress mediated by H2O2. Song, J.J., Rhee, J.G., Suntharalingam, M., Walsh, S.A., Spitz, D.R., Lee, Y.J. J. Biol. Chem. (2002) [Pubmed]
  12. Acute cadmium exposure inactivates thioltransferase (Glutaredoxin), inhibits intracellular reduction of protein-glutathionyl-mixed disulfides, and initiates apoptosis. Chrestensen, C.A., Starke, D.W., Mieyal, J.J. J. Biol. Chem. (2000) [Pubmed]
  13. Redox regulation in the lens. Lou, M.F. Progress in retinal and eye research. (2003) [Pubmed]
  14. Immunohistochemical localization of glutaredoxin and thioredoxin in human endometrium: a possible association with pinopodes. Stavréus-Evers, A., Masironi, B., Landgren, B.M., Holmgren, A., Eriksson, H., Sahlin, L. Mol. Hum. Reprod. (2002) [Pubmed]
  15. Cellular and plasma levels of human glutaredoxin 1 and 2 detected by sensitive ELISA systems. Lundberg, M., Fernandes, A.P., Kumar, S., Holmgren, A. Biochem. Biophys. Res. Commun. (2004) [Pubmed]
  16. Regulation of human thioltransferase (hTTase) gene by AP-1 transcription factor under oxidative stress. Krysan, K., Lou, M.F. Invest. Ophthalmol. Vis. Sci. (2002) [Pubmed]
  17. Glutaredoxin-dependent peroxiredoxin from poplar: protein-protein interaction and catalytic mechanism. Rouhier, N., Gelhaye, E., Jacquot, J.P. J. Biol. Chem. (2002) [Pubmed]
  18. Thioltransferase (glutaredoxin) reactivates the DNA-binding activity of oxidation-inactivated nuclear factor I. Bandyopadhyay, S., Starke, D.W., Mieyal, J.J., Gronostajski, R.M. J. Biol. Chem. (1998) [Pubmed]
  19. Regulation of thioltransferase expression in human lens epithelial cells. Raghavachari, N., Krysan, K., Xing, K., Lou, M.F. Invest. Ophthalmol. Vis. Sci. (2001) [Pubmed]
  20. Studies on the mechanism of oxidative modification of human glyceraldehyde-3-phosphate dehydrogenase by glutathione: catalysis by glutaredoxin. Lind, C., Gerdes, R., Schuppe-Koistinen, I., Cotgreave, I.A. Biochem. Biophys. Res. Commun. (1998) [Pubmed]
  21. Differential role of glutaredoxin and thioredoxin in metabolic oxidative stress-induced activation of apoptosis signal-regulating kinase 1. Song, J.J., Lee, Y.J. Biochem. J. (2003) [Pubmed]
  22. Measurements of plasma glutaredoxin and thioredoxin in healthy volunteers and during open-heart surgery. Nakamura, H., Vaage, J., Valen, G., Padilla, C.A., Björnstedt, M., Holmgren, A. Free Radic. Biol. Med. (1998) [Pubmed]
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