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Glrx  -  glutaredoxin (thioltransferase)

Rattus norvegicus

Synonyms: Glrx1, Glutaredoxin-1, Grx, TTase-1, Thioltransferase-1
 
 
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Disease relevance of Glrx1

 

High impact information on Glrx1

 

Biological context of Glrx1

  • Here we demonstrated that overexpression of GRX protected cells from hydrogen peroxide (H2O2)-induced apoptosis by regulating the redox state of Akt [6].
  • Overexpression of GRX protected Akt from H2O2-induced oxidation and suppressed recruitment of protein phosphatase 2A to Akt, resulting in a sustained phosphorylation of Akt and inhibition of apoptosis [6].
  • Grx immunostaining in the CL was strong in infiltrating macrophages and in a population of steroidogenic cells that survived the apoptotic burst in regressing CL and in CL remnants, but was faint or absent in young CL of the current cycle and in CL during pseudopregnancy [7].
  • Thioltransferase in human red blood cells: kinetics and equilibrium [8].
  • Glutaredoxin is an important enzyme in thiol homeostasis [9].
 

Anatomical context of Glrx1

  • Grx was absent from the oocytes in the first days of postnatal life when marked oocyte degeneration takes place, but its presence was very conspicuous in the cytoplasm of oocytes in healthy and attretic follicles in rats from 10 days of age onward, independently of the day of oestrous cycle [7].
  • We have found a prominent presence of Grx in the oocytes and in corpora lutea (CL) during developmental and oestrous cycle changes [7].
  • These results support a role of Grx in the maintenance of functional oocytes and in luteal cells surviving the regression process, probably as a consequence of the demonstrated deglutathionylating function of this protein in an antioxidant and antiapoptotic context [7].
  • Grx has been identified in brain cytosol, but the presence of activity in subcellular organelles has not been reported [10].
  • The data presented demonstrate that mitochondria contain functional Grx-like activity [10].
 

Associations of Glrx1 with chemical compounds

 

Other interactions of Glrx1

 

Analytical, diagnostic and therapeutic context of Glrx1

References

  1. Ascorbic acid and cell survival of adriamycin resistant and sensitive MCF-7 breast tumor cells. Wells, W.W., Rocque, P.A., Xu, D.P., Meyer, E.B., Charamella, L.J., Dimitrov, N.V. Free Radic. Biol. Med. (1995) [Pubmed]
  2. Glutaredoxins catalyze the reduction of glutathione by dihydrolipoamide with high efficiency. Porras, P., Pedrajas, J.R., Martínez-Galisteo, E., Padilla, C.A., Johansson, C., Holmgren, A., Bárcena, J.A. Biochem. Biophys. Res. Commun. (2002) [Pubmed]
  3. Localization of glutaredoxin (thioltransferase) in the rat brain and possible functional implications during focal ischemia. Takagi, Y., Nakamura, T., Nishiyama, A., Nozaki, K., Tanaka, T., Hashimoto, N., Yodoi, J. Biochem. Biophys. Res. Commun. (1999) [Pubmed]
  4. Redox control of exocytosis: regulatory role of NADPH, thioredoxin, and glutaredoxin. Ivarsson, R., Quintens, R., Dejonghe, S., Tsukamoto, K., in 't Veld, P., Renström, E., Schuit, F.C. Diabetes (2005) [Pubmed]
  5. S-glutathiolation of Ras mediates redox-sensitive signaling by angiotensin II in vascular smooth muscle cells. Adachi, T., Pimentel, D.R., Heibeck, T., Hou, X., Lee, Y.J., Jiang, B., Ido, Y., Cohen, R.A. J. Biol. Chem. (2004) [Pubmed]
  6. Glutaredoxin exerts an antiapoptotic effect by regulating the redox state of Akt. Murata, H., Ihara, Y., Nakamura, H., Yodoi, J., Sumikawa, K., Kondo, T. J. Biol. Chem. (2003) [Pubmed]
  7. Expression of glutaredoxin (thioltransferase) in the rat ovary during the oestrous cycle and postnatal development. González-Fernández, R., Gaytán, F., Martínez-Galisteo, E., Porras, P., Padilla, C.A., Sánchez Criado, J.E., Bárcena, J.A. J. Mol. Endocrinol. (2005) [Pubmed]
  8. Thioltransferase in human red blood cells: kinetics and equilibrium. Mieyal, J.J., Starke, D.W., Gravina, S.A., Hocevar, B.A. Biochemistry (1991) [Pubmed]
  9. Effect of peroxynitrite on glutaredoxin. Aykaç-Toker, G., Bulgurcuoğlu, S., Koçak-Toker, N. Human & experimental toxicology. (2001) [Pubmed]
  10. Functional glutaredoxin (thioltransferase) activity in rat brain and liver mitochondria. Ehrhart, J., Gluck, M., Mieyal, J., Zeevalk, G.D. Parkinsonism Relat. Disord. (2002) [Pubmed]
  11. Regulation of hydroxylations in biosynthesis of bile acids. Isolation of a protein from rat liver cytosol stimulating reconstituted cholesterol 7 alpha-hydroxylase activity. Danielsson, H., Kalles, I., Wikvall, K. J. Biol. Chem. (1984) [Pubmed]
  12. Identification of an abundant S-thiolated rat liver protein as carbonic anhydrase III; characterization of S-thiolation and dethiolation reactions. Chai, Y.C., Jung, C.H., Lii, C.K., Ashraf, S.S., Hendrich, S., Wolf, B., Sies, H., Thomas, J.A. Arch. Biochem. Biophys. (1991) [Pubmed]
  13. Thiol-disulfide exchange systems in the liver of aging Fischer 344 rats. Rikans, L.E., Hornbrook, K.R. Gerontology. (1998) [Pubmed]
  14. Purification and properties of thioltransferase. Gan, Z.R., Wells, W.W. J. Biol. Chem. (1986) [Pubmed]
  15. Purification and characterization of glutathione-dependent dehydroascorbate reductase from rat liver. Maellaro, E., Del Bello, B., Sugherini, L., Santucci, A., Comporti, M., Casini, A.F. Biochem. J. (1994) [Pubmed]
  16. Modulation of class Pi glutathione transferase activity by sulfhydryl group modification. Shen, H.X., Tamai, K., Satoh, K., Hatayama, I., Tsuchida, S., Sato, K. Arch. Biochem. Biophys. (1991) [Pubmed]
 
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