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Volumn 7, Issue 4, 2007, Pages 381-391

Mechanisms of reversible protein glutathionylation in redox signaling and oxidative stress

Author keywords

[No Author keywords available]

Indexed keywords

CYSTEINE; DISULFIDE; FLAVOPROTEIN; GLUTAREDOXIN; GLUTATHIONE; GLUTATHIONE PEROXIDASE; GLUTATHIONE TRANSFERASE; GLUTATHIONE TRANSFERASE P1; GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE; METHIONINE SULFOXIDE REDUCTASE; OXIDOREDUCTASE; PEROXIREDOXIN; PHOSPHATASE; PROTEIN TYROSINE PHOSPHATASE 1B; REACTIVE NITROGEN SPECIES; REACTIVE OXYGEN METABOLITE; SELENOCYSTEINE; SULFENIC ACID DERIVATIVE; THIOL; THIOL OXIDASE;

EID: 34548163922     PISSN: 14714892     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.coph.2007.06.003     Document Type: Review
Times cited : (404)

References (106)
  • 1
    • 1842832392 scopus 로고    scopus 로고
    • Glyceraldehyde phosphate dehydrogenase oxidation during cardiac ischemia and reperfusion
    • Eaton P., Wright N., Hearse D.J., and Shattock M.J. Glyceraldehyde phosphate dehydrogenase oxidation during cardiac ischemia and reperfusion. J Mol Cell Cardiol 34 (2002) 1549-1560
    • (2002) J Mol Cell Cardiol , vol.34 , pp. 1549-1560
    • Eaton, P.1    Wright, N.2    Hearse, D.J.3    Shattock, M.J.4
  • 2
    • 3142663363 scopus 로고    scopus 로고
    • S-Glutathiolation of Ras mediates redox-sensitive signaling by angiotensin II in vascular smooth muscle cells
    • This manuscript provides strong support for physiological regulation of Ras by reversible S-glutathionylation and links activation of Ras via glutathionylation to regulation of protein synthesis and subsequent cellular hypertrophy.
    • Adachi T., Pimentel D.R., Heibeck T., Hou X., Lee Y.J., Jiang B., Ido Y., and Cohen R.A. S-Glutathiolation of Ras mediates redox-sensitive signaling by angiotensin II in vascular smooth muscle cells. J Biol Chem 279 (2004) 29857-29862. This manuscript provides strong support for physiological regulation of Ras by reversible S-glutathionylation and links activation of Ras via glutathionylation to regulation of protein synthesis and subsequent cellular hypertrophy.
    • (2004) J Biol Chem , vol.279 , pp. 29857-29862
    • Adachi, T.1    Pimentel, D.R.2    Heibeck, T.3    Hou, X.4    Lee, Y.J.5    Jiang, B.6    Ido, Y.7    Cohen, R.A.8
  • 4
    • 14044257843 scopus 로고    scopus 로고
    • Glutaredoxin: role in reversible protein S-glutathionylation and regulation of redox signal transduction and protein translocation
    • This review is the first to offer criteria for evaluating S-glutathionylation as a signaling mechanism, and it discusses evidence for reversible glutathionylation in the regulation of kinases, transcription factors, cell death mediators, and cytoskeletal protein. Methods for detecting protein-SSG are also discussed and evaluated.
    • Shelton M.D., Chock P.B., and Mieyal J.J. Glutaredoxin: role in reversible protein S-glutathionylation and regulation of redox signal transduction and protein translocation. Antioxid Redox Signal 7 (2005) 348-366. This review is the first to offer criteria for evaluating S-glutathionylation as a signaling mechanism, and it discusses evidence for reversible glutathionylation in the regulation of kinases, transcription factors, cell death mediators, and cytoskeletal protein. Methods for detecting protein-SSG are also discussed and evaluated.
    • (2005) Antioxid Redox Signal , vol.7 , pp. 348-366
    • Shelton, M.D.1    Chock, P.B.2    Mieyal, J.J.3
  • 5
    • 34250328361 scopus 로고    scopus 로고
    • Glutaredoxin regulates nuclear factor kappa-B and intercellular adhesion molecule in Muller cells: model of diabetic retinopathy
    • This work implicates GRx in the regulation of the NFκB pathway and transcription of ICAM in retinal glial cells under conditions of simulated hyperglycemia, thereby associating induction of GRx with the development of diabetic retinopathy, and identifying the enzyme as a potential therapeutic target.
    • Shelton M.D., Kern T.S., and Mieyal J.J. Glutaredoxin regulates nuclear factor kappa-B and intercellular adhesion molecule in Muller cells: model of diabetic retinopathy. J Biol Chem (2007). This work implicates GRx in the regulation of the NFκB pathway and transcription of ICAM in retinal glial cells under conditions of simulated hyperglycemia, thereby associating induction of GRx with the development of diabetic retinopathy, and identifying the enzyme as a potential therapeutic target.
    • (2007) J Biol Chem
    • Shelton, M.D.1    Kern, T.S.2    Mieyal, J.J.3
  • 6
    • 0038303229 scopus 로고    scopus 로고
    • Stable and controllable RNA interference: investigating the physiological function of glutathionylated actin
    • Wang J., Tekle E., Oubrahim H., Mieyal J.J., Stadtman E.R., and Chock P.B. Stable and controllable RNA interference: investigating the physiological function of glutathionylated actin. Proc Natl Acad Sci USA 100 (2003) 5103-5106
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 5103-5106
    • Wang, J.1    Tekle, E.2    Oubrahim, H.3    Mieyal, J.J.4    Stadtman, E.R.5    Chock, P.B.6
  • 7
    • 9144266981 scopus 로고    scopus 로고
    • S-Glutathiolation by peroxynitrite activates SERCA during arterial relaxation by nitric oxide
    • This manuscript provides support for regulation of SERCA via S-glutathionylation, and it is the first to link regulation by glutathionylation to vascular homeostasis.
    • Adachi T., Weisbrod R.M., Pimentel D.R., Ying J., Sharov V.S., Schoneich C., and Cohen R.A. S-Glutathiolation by peroxynitrite activates SERCA during arterial relaxation by nitric oxide. Nat Med 10 (2004) 1200-1207. This manuscript provides support for regulation of SERCA via S-glutathionylation, and it is the first to link regulation by glutathionylation to vascular homeostasis.
    • (2004) Nat Med , vol.10 , pp. 1200-1207
    • Adachi, T.1    Weisbrod, R.M.2    Pimentel, D.R.3    Ying, J.4    Sharov, V.S.5    Schoneich, C.6    Cohen, R.A.7
  • 8
    • 33749391618 scopus 로고    scopus 로고
    • Glutaredoxin modulates platelet-derived growth factor-dependent cell signaling by regulating the redox status of low molecular weight protein-tyrosine phosphatase
    • This paper supports the role of GRx1 in regulation of growth factor signaling in a cellular context by demonstrating that GRx knockdown results in increased phosphorylation of PTPs and concomitant activation of the PDGF receptor. By analogy to previous studies of PTP1B (Barrett et al.), increased receptor activation when GRx1 is decreased is probably due to decreased deglutathionylation of low molecular weight PTP-SSG, resulting in greater deactivation of PTP.
    • Kanda M., Ihara Y., Murata H., Urata Y., Kono T., Yodoi J., Seto S., Yano K., and Kondo T. Glutaredoxin modulates platelet-derived growth factor-dependent cell signaling by regulating the redox status of low molecular weight protein-tyrosine phosphatase. J Biol Chem 281 (2006) 28518-28528. This paper supports the role of GRx1 in regulation of growth factor signaling in a cellular context by demonstrating that GRx knockdown results in increased phosphorylation of PTPs and concomitant activation of the PDGF receptor. By analogy to previous studies of PTP1B (Barrett et al.), increased receptor activation when GRx1 is decreased is probably due to decreased deglutathionylation of low molecular weight PTP-SSG, resulting in greater deactivation of PTP.
    • (2006) J Biol Chem , vol.281 , pp. 28518-28528
    • Kanda, M.1    Ihara, Y.2    Murata, H.3    Urata, Y.4    Kono, T.5    Yodoi, J.6    Seto, S.7    Yano, K.8    Kondo, T.9
  • 10
    • 0033521019 scopus 로고    scopus 로고
    • Roles of superoxide radical anion in signal transduction mediated by reversible regulation of protein-tyrosine phosphatase 1B
    • Barrett W.C., DeGnore J.P., Keng Y.F., Zhang Z.Y., Yim M.B., and Chock P.B. Roles of superoxide radical anion in signal transduction mediated by reversible regulation of protein-tyrosine phosphatase 1B. J Biol Chem 274 (1999) 34543-34546
    • (1999) J Biol Chem , vol.274 , pp. 34543-34546
    • Barrett, W.C.1    DeGnore, J.P.2    Keng, Y.F.3    Zhang, Z.Y.4    Yim, M.B.5    Chock, P.B.6
  • 12
    • 0034714319 scopus 로고    scopus 로고
    • Acute cadmium exposure inactivates thioltransferase (Glutaredoxin), inhibits intracellular reduction of protein-glutathionyl-mixed disulfides, and initiates apoptosis
    • Chrestensen C.A., Starke D.W., and Mieyal J.J. Acute cadmium exposure inactivates thioltransferase (Glutaredoxin), inhibits intracellular reduction of protein-glutathionyl-mixed disulfides, and initiates apoptosis. J Biol Chem 275 (2000) 26556-26565
    • (2000) J Biol Chem , vol.275 , pp. 26556-26565
    • Chrestensen, C.A.1    Starke, D.W.2    Mieyal, J.J.3
  • 13
    • 0030296409 scopus 로고    scopus 로고
    • S-Glutathiolated hepatocyte proteins and insulin disulfides as substrates for reduction by glutaredoxin, thioredoxin, protein disulfide isomerase, and glutathione
    • Jung C.H., and Thomas J.A. S-Glutathiolated hepatocyte proteins and insulin disulfides as substrates for reduction by glutaredoxin, thioredoxin, protein disulfide isomerase, and glutathione. Arch Biochem Biophys 335 (1996) 61-72
    • (1996) Arch Biochem Biophys , vol.335 , pp. 61-72
    • Jung, C.H.1    Thomas, J.A.2
  • 14
    • 0029065402 scopus 로고
    • Thiol/disulfide exchange equilibria and disulfide bond stability
    • Gilbert H.F. Thiol/disulfide exchange equilibria and disulfide bond stability. Meth Enzymol 251 (1995) 8-28
    • (1995) Meth Enzymol , vol.251 , pp. 8-28
    • Gilbert, H.F.1
  • 15
    • 0025118967 scopus 로고
    • Molecular and cellular aspects of thiol-disulfide exchange
    • Gilbert H.F. Molecular and cellular aspects of thiol-disulfide exchange. Adv Enzymol Relat Areas Mol Biol 63 (1990) 69-172
    • (1990) Adv Enzymol Relat Areas Mol Biol , vol.63 , pp. 69-172
    • Gilbert, H.F.1
  • 17
    • 0035960648 scopus 로고    scopus 로고
    • Glutathionylation of the p50 subunit of NF-kappaB: a mechanism for redox-induced inhibition of DNA binding
    • Pineda-Molina E., Klatt P., Vazquez J., Marina A., Garcia d.L., Perez-Sala D., and Lamas S. Glutathionylation of the p50 subunit of NF-kappaB: a mechanism for redox-induced inhibition of DNA binding. Biochemistry 40 (2001) 14134-14142
    • (2001) Biochemistry , vol.40 , pp. 14134-14142
    • Pineda-Molina, E.1    Klatt, P.2    Vazquez, J.3    Marina, A.4    Garcia, d.L.5    Perez-Sala, D.6    Lamas, S.7
  • 18
    • 9144249116 scopus 로고    scopus 로고
    • Glutaredoxin 2 catalyzes the reversible oxidation and glutathionylation of mitochondrial membrane thiol proteins: implications for mitochondrial redox regulation and antioxidant DEFENSE
    • This was the first demonstration of the capacity of GRx2 to act as a glutathionylating and deglutathionylating enzyme toward a mitochondrial protein substrate, Complex I, although the kinetic analysis was limited and artificial GSH:GSSG ratios were used.
    • Beer S.M., Taylor E.R., Brown S.E., Dahm C.C., Costa N.J., Runswick M.J., and Murphy M.P. Glutaredoxin 2 catalyzes the reversible oxidation and glutathionylation of mitochondrial membrane thiol proteins: implications for mitochondrial redox regulation and antioxidant DEFENSE. J Biol Chem 279 (2004) 47939-47951. This was the first demonstration of the capacity of GRx2 to act as a glutathionylating and deglutathionylating enzyme toward a mitochondrial protein substrate, Complex I, although the kinetic analysis was limited and artificial GSH:GSSG ratios were used.
    • (2004) J Biol Chem , vol.279 , pp. 47939-47951
    • Beer, S.M.1    Taylor, E.R.2    Brown, S.E.3    Dahm, C.C.4    Costa, N.J.5    Runswick, M.J.6    Murphy, M.P.7
  • 19
    • 20544472348 scopus 로고    scopus 로고
    • Regulation of protein function by glutathionylation
    • This valuable review considers mechanisms of protein glutathionylation and deglutathionylation, and their potential roles in the regulation of cellular metabolism. The discussion of protein deglutathionylation, however, may be misleading in some aspects regarding non-enzymic and enzymic mechanisms.
    • Ghezzi P. Regulation of protein function by glutathionylation. Free Radic Res 39 (2005) 573-580. This valuable review considers mechanisms of protein glutathionylation and deglutathionylation, and their potential roles in the regulation of cellular metabolism. The discussion of protein deglutathionylation, however, may be misleading in some aspects regarding non-enzymic and enzymic mechanisms.
    • (2005) Free Radic Res , vol.39 , pp. 573-580
    • Ghezzi, P.1
  • 20
    • 27944504099 scopus 로고    scopus 로고
    • Oxidoreduction of protein thiols in redox regulation
    • Ghezzi P. Oxidoreduction of protein thiols in redox regulation. Biochem Soc Trans 33 (2005) 1378-1381
    • (2005) Biochem Soc Trans , vol.33 , pp. 1378-1381
    • Ghezzi, P.1
  • 21
    • 0021891877 scopus 로고
    • Role of reversible oxidation-reduction of enzyme thiols-disulfides in metabolic regulation
    • Ziegler D.M. Role of reversible oxidation-reduction of enzyme thiols-disulfides in metabolic regulation. Annu Rev Biochem 54 (1985) 305-329
    • (1985) Annu Rev Biochem , vol.54 , pp. 305-329
    • Ziegler, D.M.1
  • 22
    • 14044272119 scopus 로고    scopus 로고
    • S-Glutathionylation: from redox regulation of protein functions to human diseases
    • Giustarini D., Rossi R., Milzani A., Colombo R., and Dalle-Donne I. S-Glutathionylation: from redox regulation of protein functions to human diseases. J Cell Mol Med 8 (2004) 201-212
    • (2004) J Cell Mol Med , vol.8 , pp. 201-212
    • Giustarini, D.1    Rossi, R.2    Milzani, A.3    Colombo, R.4    Dalle-Donne, I.5
  • 24
    • 0033869092 scopus 로고    scopus 로고
    • Regulation of protein function by S-glutathiolation in response to oxidative and nitrosative stress
    • Klatt P., and Lamas S. Regulation of protein function by S-glutathiolation in response to oxidative and nitrosative stress. Eur J Biochem 267 (2000) 4928-4944
    • (2000) Eur J Biochem , vol.267 , pp. 4928-4944
    • Klatt, P.1    Lamas, S.2
  • 25
    • 33846849238 scopus 로고    scopus 로고
    • Reversible glutathiolation of caspase-3 by glutaredoxin as a novel redox signaling mechanism in tumor necrosis factor-alpha-induced cell death
    • Sykes M.C., Mowbray A.L., and Jo H. Reversible glutathiolation of caspase-3 by glutaredoxin as a novel redox signaling mechanism in tumor necrosis factor-alpha-induced cell death. Circ Res 100 (2007) 152-154
    • (2007) Circ Res , vol.100 , pp. 152-154
    • Sykes, M.C.1    Mowbray, A.L.2    Jo, H.3
  • 26
    • 0036709885 scopus 로고    scopus 로고
    • Glutathionylation of proteins by glutathione disulfide S-oxide
    • Huang K.P., and Huang F.L. Glutathionylation of proteins by glutathione disulfide S-oxide. Biochem Pharmacol 64 (2002) 1049-1056
    • (2002) Biochem Pharmacol , vol.64 , pp. 1049-1056
    • Huang, K.P.1    Huang, F.L.2
  • 28
    • 0029015864 scopus 로고
    • Protein sulfhydryls and their role in the antioxidant function of protein S-thiolation
    • Thomas J.A., Poland B., and Honzatko R. Protein sulfhydryls and their role in the antioxidant function of protein S-thiolation. Arch Biochem Biophys 319 (1995) 1-9
    • (1995) Arch Biochem Biophys , vol.319 , pp. 1-9
    • Thomas, J.A.1    Poland, B.2    Honzatko, R.3
  • 29
    • 33644976378 scopus 로고    scopus 로고
    • GSH depletion, protein S-glutathionylation and mitochondrial transmembrane potential hyperpolarization are early events in initiation of cell death induced by a mixture of isothiazolinones in HL60 cells
    • Di Stefano A., Frosali S., Leonini A., Ettorre A., Priora R., Di Simplicio F.C., and Di Simplicio P. GSH depletion, protein S-glutathionylation and mitochondrial transmembrane potential hyperpolarization are early events in initiation of cell death induced by a mixture of isothiazolinones in HL60 cells. Biochim Biophys Acta 1763 (2006) 214-225
    • (2006) Biochim Biophys Acta , vol.1763 , pp. 214-225
    • Di Stefano, A.1    Frosali, S.2    Leonini, A.3    Ettorre, A.4    Priora, R.5    Di Simplicio, F.C.6    Di Simplicio, P.7
  • 30
    • 24644469955 scopus 로고    scopus 로고
    • Sites and mechanisms of aconitase inactivation by peroxynitrite: modulation by citrate and glutathione
    • Han D., Canali R., Garcia J., Aguilera R., Gallaher T.K., and Cadenas E. Sites and mechanisms of aconitase inactivation by peroxynitrite: modulation by citrate and glutathione. Biochemistry 44 (2005) 11986-11996
    • (2005) Biochemistry , vol.44 , pp. 11986-11996
    • Han, D.1    Canali, R.2    Garcia, J.3    Aguilera, R.4    Gallaher, T.K.5    Cadenas, E.6
  • 31
    • 33746752638 scopus 로고    scopus 로고
    • Protein S-glutathionylation and platelet anti-aggregating activity of disulfiram
    • Rossi R., Giustarini D., Dalle-Donne I., and Milzani A. Protein S-glutathionylation and platelet anti-aggregating activity of disulfiram. Biochem Pharmacol 72 (2006) 608-615
    • (2006) Biochem Pharmacol , vol.72 , pp. 608-615
    • Rossi, R.1    Giustarini, D.2    Dalle-Donne, I.3    Milzani, A.4
  • 32
    • 0030918451 scopus 로고    scopus 로고
    • Targeting nitric oxide (NO) delivery in vivo. Design of a liver-selective NO donor prodrug that blocks tumor necrosis factor-alpha-induced apoptosis and toxicity in the liver
    • Saavedra J.E., Billiar T.R., Williams D.L., Kim Y.M., Watkins S.C., and Keefer L.K. Targeting nitric oxide (NO) delivery in vivo. Design of a liver-selective NO donor prodrug that blocks tumor necrosis factor-alpha-induced apoptosis and toxicity in the liver. J Med Chem 40 (1997) 1947-1954
    • (1997) J Med Chem , vol.40 , pp. 1947-1954
    • Saavedra, J.E.1    Billiar, T.R.2    Williams, D.L.3    Kim, Y.M.4    Watkins, S.C.5    Keefer, L.K.6
  • 33
    • 0032983979 scopus 로고    scopus 로고
    • Nitric oxide inhibits c-Jun DNA binding by specifically targeted S-glutathionylation
    • Klatt P., Molina E.P., and Lamas S. Nitric oxide inhibits c-Jun DNA binding by specifically targeted S-glutathionylation. J Biol Chem 274 (1999) 15857-15864
    • (1999) J Biol Chem , vol.274 , pp. 15857-15864
    • Klatt, P.1    Molina, E.P.2    Lamas, S.3
  • 34
    • 0035793599 scopus 로고    scopus 로고
    • Glutathiolation of proteins by glutathione disulfide S-oxide derived from S-nitrosoglutathione. Modifications of rat brain neurogranin/RC3 and neuromodulin/GAP-43
    • Li J., Huang F.L., and Huang K.P. Glutathiolation of proteins by glutathione disulfide S-oxide derived from S-nitrosoglutathione. Modifications of rat brain neurogranin/RC3 and neuromodulin/GAP-43. J Biol Chem 276 (2001) 3098-3105
    • (2001) J Biol Chem , vol.276 , pp. 3098-3105
    • Li, J.1    Huang, F.L.2    Huang, K.P.3
  • 35
    • 0033515479 scopus 로고    scopus 로고
    • Nitric oxide-induced S-glutathionylation and inactivation of glyceraldehyde-3-phosphate dehydrogenase
    • Mohr S., Hallak H., de Boitte A., Lapetina E.G., and Brune B. Nitric oxide-induced S-glutathionylation and inactivation of glyceraldehyde-3-phosphate dehydrogenase. J Biol Chem 274 (1999) 9427-9430
    • (1999) J Biol Chem , vol.274 , pp. 9427-9430
    • Mohr, S.1    Hallak, H.2    de Boitte, A.3    Lapetina, E.G.4    Brune, B.5
  • 36
    • 1342281240 scopus 로고    scopus 로고
    • Protein sulfenic acids in redox signaling
    • This comprehensive review discusses protein-SOH chemistry and its potential role in enzyme catalysis and cellular signaling, particularly in prokaryotic systems.
    • Poole L.B., Karplus P.A., and Claiborne A. Protein sulfenic acids in redox signaling. Annu Rev Pharmacol Toxicol 44 (2004) 325-347. This comprehensive review discusses protein-SOH chemistry and its potential role in enzyme catalysis and cellular signaling, particularly in prokaryotic systems.
    • (2004) Annu Rev Pharmacol Toxicol , vol.44 , pp. 325-347
    • Poole, L.B.1    Karplus, P.A.2    Claiborne, A.3
  • 37
    • 0027131771 scopus 로고
    • Protein-sulfenic acid stabilization and function in enzyme catalysis and gene regulation
    • Claiborne A., Miller H., Parsonage D., and Ross R.P. Protein-sulfenic acid stabilization and function in enzyme catalysis and gene regulation. FASEB J 7 (1993) 1483-1490
    • (1993) FASEB J , vol.7 , pp. 1483-1490
    • Claiborne, A.1    Miller, H.2    Parsonage, D.3    Ross, R.P.4
  • 38
    • 0033598677 scopus 로고    scopus 로고
    • Protein-sulfenic acids: diverse roles for an unlikely player in enzyme catalysis and redox regulation
    • Claiborne A., Yeh J.I., Mallett T.C., Luba J., Crane III E.J., Charrier V., and Parsonage D. Protein-sulfenic acids: diverse roles for an unlikely player in enzyme catalysis and redox regulation. Biochemistry 38 (1999) 15407-15416
    • (1999) Biochemistry , vol.38 , pp. 15407-15416
    • Claiborne, A.1    Yeh, J.I.2    Mallett, T.C.3    Luba, J.4    Crane III, E.J.5    Charrier, V.6    Parsonage, D.7
  • 39
    • 0022334391 scopus 로고
    • The glutathione peroxidase reaction: molecular basis of the antioxidant function of selenium in mammals
    • Flohe L. The glutathione peroxidase reaction: molecular basis of the antioxidant function of selenium in mammals. Curr Top Cell Regul 27 (1985) 473-478
    • (1985) Curr Top Cell Regul , vol.27 , pp. 473-478
    • Flohe, L.1
  • 40
    • 19444375216 scopus 로고    scopus 로고
    • Peroxiredoxins: a historical overview and speculative preview of novel mechanisms and emerging concepts in cell signaling
    • Rhee S.G., Chae H.Z., and Kim K. Peroxiredoxins: a historical overview and speculative preview of novel mechanisms and emerging concepts in cell signaling. Free Radic Biol Med 38 (2005) 1543-1552
    • (2005) Free Radic Biol Med , vol.38 , pp. 1543-1552
    • Rhee, S.G.1    Chae, H.Z.2    Kim, K.3
  • 41
    • 0028037601 scopus 로고
    • Possible differences in the regenerative roles played by thioltransferase and thioredoxin for oxidatively damaged proteins
    • Yoshitake S., Nanri H., Fernando M.R., and Minakami S. Possible differences in the regenerative roles played by thioltransferase and thioredoxin for oxidatively damaged proteins. J Biochem (Tokyo) 116 (1994) 42-46
    • (1994) J Biochem (Tokyo) , vol.116 , pp. 42-46
    • Yoshitake, S.1    Nanri, H.2    Fernando, M.R.3    Minakami, S.4
  • 42
    • 0032546955 scopus 로고    scopus 로고
    • Reversible inactivation of protein-tyrosine phosphatase 1B in A431 cells stimulated with epidermal growth factor
    • Lee S.R., Kwon K.S., Kim S.R., and Rhee S.G. Reversible inactivation of protein-tyrosine phosphatase 1B in A431 cells stimulated with epidermal growth factor. J Biol Chem 273 (1998) 15366-15372
    • (1998) J Biol Chem , vol.273 , pp. 15366-15372
    • Lee, S.R.1    Kwon, K.S.2    Kim, S.R.3    Rhee, S.G.4
  • 43
    • 0032554611 scopus 로고    scopus 로고
    • Specific and reversible inactivation of protein tyrosine phosphatases by hydrogen peroxide: evidence for a sulfenic acid intermediate and implications for redox regulation
    • Denu J.M., and Tanner K.G. Specific and reversible inactivation of protein tyrosine phosphatases by hydrogen peroxide: evidence for a sulfenic acid intermediate and implications for redox regulation. Biochemistry 37 (1998) 5633-5642
    • (1998) Biochemistry , vol.37 , pp. 5633-5642
    • Denu, J.M.1    Tanner, K.G.2
  • 45
    • 0032464635 scopus 로고    scopus 로고
    • Pathophysiology of nitric oxide and related species: free radical reactions and modification of biomolecules
    • Eiserich J.P., Patel R.P., and O'Donnell V.B. Pathophysiology of nitric oxide and related species: free radical reactions and modification of biomolecules. Mol Aspects Med 19 (1998) 221-357
    • (1998) Mol Aspects Med , vol.19 , pp. 221-357
    • Eiserich, J.P.1    Patel, R.P.2    O'Donnell, V.B.3
  • 46
    • 0036174890 scopus 로고    scopus 로고
    • The biochemistry and physiology of S-nitrosothiols
    • Hogg N. The biochemistry and physiology of S-nitrosothiols. Annu Rev Pharmacol Toxicol 42 (2002) 585-600
    • (2002) Annu Rev Pharmacol Toxicol , vol.42 , pp. 585-600
    • Hogg, N.1
  • 48
    • 0028987969 scopus 로고
    • NO+, NO, and NO- donation by S-nitrosothiols: implications for regulation of physiological functions by S-nitrosylation and acceleration of disulfide formation
    • Arnelle D.R., and Stamler J.S. NO+, NO, and NO- donation by S-nitrosothiols: implications for regulation of physiological functions by S-nitrosylation and acceleration of disulfide formation. Arch Biochem Biophys 318 (1995) 279-285
    • (1995) Arch Biochem Biophys , vol.318 , pp. 279-285
    • Arnelle, D.R.1    Stamler, J.S.2
  • 49
    • 0024299403 scopus 로고
    • Reaction of S-nitrosoglutathione with sulfhydryl groups in protein
    • Park J.W. Reaction of S-nitrosoglutathione with sulfhydryl groups in protein. Biochem Biophys Res Commun 152 (1988) 916-920
    • (1988) Biochem Biophys Res Commun , vol.152 , pp. 916-920
    • Park, J.W.1
  • 51
    • 0032921250 scopus 로고    scopus 로고
    • Nitric oxide and thiol groups
    • Gaston B. Nitric oxide and thiol groups. Biochim Biophys Acta 1411 (1999) 323-333
    • (1999) Biochim Biophys Acta , vol.1411 , pp. 323-333
    • Gaston, B.1
  • 53
    • 0033080394 scopus 로고    scopus 로고
    • S-Nitrosylation and S-glutathiolation of protein sulfhydryls by S-nitrosoglutathione
    • Ji Y., Akerboom T.P., Sies H., and Thomas J.A. S-Nitrosylation and S-glutathiolation of protein sulfhydryls by S-nitrosoglutathione. Arch Biochem Biophys 362 (1999) 67-78
    • (1999) Arch Biochem Biophys , vol.362 , pp. 67-78
    • Ji, Y.1    Akerboom, T.P.2    Sies, H.3    Thomas, J.A.4
  • 54
    • 18844410338 scopus 로고    scopus 로고
    • S-nitrosation versus S-glutathionylation of protein sulfhydryl groups by S-nitrosoglutathione
    • This study demonstrated that some proteins are both glutathionylated and nitrosylated by reaction with GSNO, whereas others are mostly nitrosylated, suggesting neighboring group effects on the outcome of cysteine modification.
    • Giustarini D., Milzani A., Aldini G., Carini M., Rossi R., and Dalle-Donne I. S-nitrosation versus S-glutathionylation of protein sulfhydryl groups by S-nitrosoglutathione. Antioxid Redox Signal 7 (2005) 930-939. This study demonstrated that some proteins are both glutathionylated and nitrosylated by reaction with GSNO, whereas others are mostly nitrosylated, suggesting neighboring group effects on the outcome of cysteine modification.
    • (2005) Antioxid Redox Signal , vol.7 , pp. 930-939
    • Giustarini, D.1    Milzani, A.2    Aldini, G.3    Carini, M.4    Rossi, R.5    Dalle-Donne, I.6
  • 55
    • 0029002385 scopus 로고
    • Kinetic factors that control the fate of thiyl radicals in cells
    • Wardman P., and von Sonntag C. Kinetic factors that control the fate of thiyl radicals in cells. Meth Enzymol 251 (1995) 31-45
    • (1995) Meth Enzymol , vol.251 , pp. 31-45
    • Wardman, P.1    von Sonntag, C.2
  • 57
    • 0034468846 scopus 로고    scopus 로고
    • Hypochlorite-induced oxidation of thiols: formation of thiyl radicals and the role of sulfenyl chlorides as intermediates
    • Davies M.J., and Hawkins C.L. Hypochlorite-induced oxidation of thiols: formation of thiyl radicals and the role of sulfenyl chlorides as intermediates. Free Radic Res 33 (2000) 719-729
    • (2000) Free Radic Res , vol.33 , pp. 719-729
    • Davies, M.J.1    Hawkins, C.L.2
  • 58
    • 0029939154 scopus 로고    scopus 로고
    • Characterization of sulfur-centered radical intermediates formed during the oxidation of thiols and sulfite by peroxynitrite. ESR-spin trapping and oxygen uptake studies
    • Karoui H., Hogg N., Frejaville C., Tordo P., and Kalyanaraman B. Characterization of sulfur-centered radical intermediates formed during the oxidation of thiols and sulfite by peroxynitrite. ESR-spin trapping and oxygen uptake studies. J Biol Chem 271 (1996) 6000-6009
    • (1996) J Biol Chem , vol.271 , pp. 6000-6009
    • Karoui, H.1    Hogg, N.2    Frejaville, C.3    Tordo, P.4    Kalyanaraman, B.5
  • 59
    • 0029047078 scopus 로고
    • Endogenous intracellular glutathionyl radicals are generated in neuroblastoma cells under hydrogen peroxide oxidative stress
    • Kwak H.S., Yim H.S., Chock P.B., and Yim M.B. Endogenous intracellular glutathionyl radicals are generated in neuroblastoma cells under hydrogen peroxide oxidative stress. Proc Natl Acad Sci USA 92 (1995) 4582-4586
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 4582-4586
    • Kwak, H.S.1    Yim, H.S.2    Chock, P.B.3    Yim, M.B.4
  • 60
    • 0025259891 scopus 로고
    • In vivo thiyl free radical formation from hemoglobin following administration of hydroperoxides
    • Maples K.R., Kennedy C.H., Jordan S.J., and Mason R.P. In vivo thiyl free radical formation from hemoglobin following administration of hydroperoxides. Arch Biochem Biophys 277 (1990) 402-409
    • (1990) Arch Biochem Biophys , vol.277 , pp. 402-409
    • Maples, K.R.1    Kennedy, C.H.2    Jordan, S.J.3    Mason, R.P.4
  • 61
    • 0028847601 scopus 로고
    • Identification of free radicals produced in rat erythrocytes exposed to hemolytic concentrations of phenylhydroxylamine
    • Bradshaw T.P., McMillan D.C., Crouch R.K., and Jollow D.J. Identification of free radicals produced in rat erythrocytes exposed to hemolytic concentrations of phenylhydroxylamine. Free Radic Biol Med 18 (1995) 279-285
    • (1995) Free Radic Biol Med , vol.18 , pp. 279-285
    • Bradshaw, T.P.1    McMillan, D.C.2    Crouch, R.K.3    Jollow, D.J.4
  • 62
    • 0038015010 scopus 로고    scopus 로고
    • Glutathione-thiyl radical scavenging and transferase properties of human glutaredoxin (thioltransferase). Potential role in redox signal transduction
    • Starke D.W., Chock P.B., and Mieyal J.J. Glutathione-thiyl radical scavenging and transferase properties of human glutaredoxin (thioltransferase). Potential role in redox signal transduction. J Biol Chem 278 (2003) 14607-14613
    • (2003) J Biol Chem , vol.278 , pp. 14607-14613
    • Starke, D.W.1    Chock, P.B.2    Mieyal, J.J.3
  • 63
    • 22044436241 scopus 로고    scopus 로고
    • S-thiolation of tyrosine hydroxylase by reactive nitrogen species in the presence of cysteine or glutathione
    • Sadidi M., Geddes T.J., and Kuhn D.M. S-thiolation of tyrosine hydroxylase by reactive nitrogen species in the presence of cysteine or glutathione. Antioxid Redox Signal 7 (2005) 863-869
    • (2005) Antioxid Redox Signal , vol.7 , pp. 863-869
    • Sadidi, M.1    Geddes, T.J.2    Kuhn, D.M.3
  • 64
    • 0035800858 scopus 로고    scopus 로고
    • Activation of matrix metalloproteinases by peroxynitrite-induced protein S-glutathiolation via disulfide S-oxide formation
    • Okamoto T., Akaike T., Sawa T., Miyamoto Y., van d V., and Maeda H. Activation of matrix metalloproteinases by peroxynitrite-induced protein S-glutathiolation via disulfide S-oxide formation. J Biol Chem 276 (2001) 29596-29602
    • (2001) J Biol Chem , vol.276 , pp. 29596-29602
    • Okamoto, T.1    Akaike, T.2    Sawa, T.3    Miyamoto, Y.4    van d, V.5    Maeda, H.6
  • 66
    • 0038749600 scopus 로고    scopus 로고
    • Oxidation state of the active-site cysteine in protein tyrosine phosphatase 1B
    • van Montfort R.L., Congreve M., Tisi D., Carr R., and Jhoti H. Oxidation state of the active-site cysteine in protein tyrosine phosphatase 1B. Nature 423 (2003) 773-777
    • (2003) Nature , vol.423 , pp. 773-777
    • van Montfort, R.L.1    Congreve, M.2    Tisi, D.3    Carr, R.4    Jhoti, H.5
  • 67
    • 0038411479 scopus 로고    scopus 로고
    • Redox regulation of protein tyrosine phosphatase 1B involves a sulphenyl-amide intermediate
    • Salmeen A., Andersen J.N., Myers M.P., Meng T.C., Hinks J.A., Tonks N.K., and Barford D. Redox regulation of protein tyrosine phosphatase 1B involves a sulphenyl-amide intermediate. Nature 423 (2003) 769-773
    • (2003) Nature , vol.423 , pp. 769-773
    • Salmeen, A.1    Andersen, J.N.2    Myers, M.P.3    Meng, T.C.4    Hinks, J.A.5    Tonks, N.K.6    Barford, D.7
  • 68
    • 0000326249 scopus 로고
    • Glutathionyl specificity of the thioltransferases: mechanistic and physiological implications
    • Packer L., and Cadenas E. (Eds), Marcel Dekker, Inc.
    • Mieyal J.J., Srinivasan U., Starke D.W., Gravina S.A., and Mieyal P.A. Glutathionyl specificity of the thioltransferases: mechanistic and physiological implications. In: Packer L., and Cadenas E. (Eds). Biothiols in Health and Disease (1995), Marcel Dekker, Inc. 305-372
    • (1995) Biothiols in Health and Disease , pp. 305-372
    • Mieyal, J.J.1    Srinivasan, U.2    Starke, D.W.3    Gravina, S.A.4    Mieyal, P.A.5
  • 69
    • 0031000775 scopus 로고    scopus 로고
    • pH profiles indicative of rate-limiting nucleophilic displacement in thioltransferase catalysis
    • Srinivasan U., Mieyal P.A., and Mieyal J.J. pH profiles indicative of rate-limiting nucleophilic displacement in thioltransferase catalysis. Biochemistry 36 (1997) 3199-3206
    • (1997) Biochemistry , vol.36 , pp. 3199-3206
    • Srinivasan, U.1    Mieyal, P.A.2    Mieyal, J.J.3
  • 70
    • 0027238801 scopus 로고
    • Thioltransferase is a specific glutathionyl mixed disulfide oxidoreductase
    • Gravina S.A., and Mieyal J.J. Thioltransferase is a specific glutathionyl mixed disulfide oxidoreductase. Biochemistry 32 (1993) 3368-3376
    • (1993) Biochemistry , vol.32 , pp. 3368-3376
    • Gravina, S.A.1    Mieyal, J.J.2
  • 71
    • 0030851732 scopus 로고    scopus 로고
    • Thioltransferase (glutaredoxin) is detected within HIV-1 and can regulate the activity of glutathionylated HIV-1 protease in vitro
    • Davis D.A., Newcomb F.M., Starke D.W., Ott D.E., Mieyal J.J., and Yarchoan R. Thioltransferase (glutaredoxin) is detected within HIV-1 and can regulate the activity of glutathionylated HIV-1 protease in vitro. J Biol Chem 272 (1997) 25935-25940
    • (1997) J Biol Chem , vol.272 , pp. 25935-25940
    • Davis, D.A.1    Newcomb, F.M.2    Starke, D.W.3    Ott, D.E.4    Mieyal, J.J.5    Yarchoan, R.6
  • 74
    • 1542320094 scopus 로고    scopus 로고
    • Human mitochondrial glutaredoxin reduces S-glutathionylated proteins with high affinity accepting electrons from either glutathione or thioredoxin reductase
    • Johansson C., Lillig C.H., and Holmgren A. Human mitochondrial glutaredoxin reduces S-glutathionylated proteins with high affinity accepting electrons from either glutathione or thioredoxin reductase. J Biol Chem 279 (2004) 7537-7543
    • (2004) J Biol Chem , vol.279 , pp. 7537-7543
    • Johansson, C.1    Lillig, C.H.2    Holmgren, A.3
  • 75
    • 33845443999 scopus 로고    scopus 로고
    • How does iron-sulfur cluster coordination regulate the activity of human glutaredoxin 2?
    • This study considers factors influencing the regulation and stability of GRx2-FeS clusters, including active-site sequence, stabilizing residues, and GSH concentration. Contrary to previous reports, data here suggest that monomeric GRx2 does not exhibit high affinity for GSH.
    • Berndt C., Hudemann C., Hanschmann E.M., Axelsson R., Holmgren A., and Lillig C.H. How does iron-sulfur cluster coordination regulate the activity of human glutaredoxin 2?. Antioxid Redox Signal 9 (2007) 151-157. This study considers factors influencing the regulation and stability of GRx2-FeS clusters, including active-site sequence, stabilizing residues, and GSH concentration. Contrary to previous reports, data here suggest that monomeric GRx2 does not exhibit high affinity for GSH.
    • (2007) Antioxid Redox Signal , vol.9 , pp. 151-157
    • Berndt, C.1    Hudemann, C.2    Hanschmann, E.M.3    Axelsson, R.4    Holmgren, A.5    Lillig, C.H.6
  • 76
    • 34548168156 scopus 로고    scopus 로고
    • Pai HV, Starke DW, Lesnefsky EJ, Hoppel, CL, Mieyal JJ: unpublished, submitted manuscript under review, 2007.
  • 78
    • 34347204123 scopus 로고    scopus 로고
    • Oxidation and S-nitrosylation of cysteines in human cytosolic and mitochondrial glutaredoxins: effects on structure and activity
    • Hashemy S.I., Johansson C., Berndt C., Lillig C.H., and Holmgren A. Oxidation and S-nitrosylation of cysteines in human cytosolic and mitochondrial glutaredoxins: effects on structure and activity. J Biol Chem 282 (2007) 14428-14436
    • (2007) J Biol Chem , vol.282 , pp. 14428-14436
    • Hashemy, S.I.1    Johansson, C.2    Berndt, C.3    Lillig, C.H.4    Holmgren, A.5
  • 80
    • 33845667283 scopus 로고    scopus 로고
    • 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., Lofgren S., Gladyshev V.N., and Lou M.F. Mitochondrial thioltransferase (glutaredoxin 2) has GSH-dependent and thioredoxin reductase-dependent peroxidase activities in vitro and in lens epithelial cells. FASEB J 20 (2006) 2645-2647
    • (2006) FASEB J , vol.20 , pp. 2645-2647
    • Fernando, M.R.1    Lechner, J.M.2    Lofgren, S.3    Gladyshev, V.N.4    Lou, M.F.5
  • 81
    • 4444337091 scopus 로고    scopus 로고
    • Short interfering RNA-mediated silencing of glutaredoxin 2 increases the sensitivity of HeLa cells toward doxorubicin and phenylarsine oxide
    • This study of GRx2 knockdown in HeLa implicates GRx2 in mitochondrial oxidative stress defense. However, the mechanism of GRx2-mediated protection was not explored.
    • Lillig C.H., Lonn M.E., Enoksson M., Fernandes A.P., and Holmgren A. Short interfering RNA-mediated silencing of glutaredoxin 2 increases the sensitivity of HeLa cells toward doxorubicin and phenylarsine oxide. Proc Natl Acad Sci USA 101 (2004) 13227-13232. This study of GRx2 knockdown in HeLa implicates GRx2 in mitochondrial oxidative stress defense. However, the mechanism of GRx2-mediated protection was not explored.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 13227-13232
    • Lillig, C.H.1    Lonn, M.E.2    Enoksson, M.3    Fernandes, A.P.4    Holmgren, A.5
  • 82
    • 0040932016 scopus 로고    scopus 로고
    • Grx5 glutaredoxin plays a central role in protection against protein oxidative damage in Saccharomyces cerevisiae
    • Rodriguez-Manzaneque M.T., Ros J., Cabiscol E., Sorribas A., and Herrero E. Grx5 glutaredoxin plays a central role in protection against protein oxidative damage in Saccharomyces cerevisiae. Mol Cell Biol 19 (1999) 8180-8190
    • (1999) Mol Cell Biol , vol.19 , pp. 8180-8190
    • Rodriguez-Manzaneque, M.T.1    Ros, J.2    Cabiscol, E.3    Sorribas, A.4    Herrero, E.5
  • 83
    • 0038491193 scopus 로고    scopus 로고
    • Biochemical characterization of yeast mitochondrial Grx5 monothiol glutaredoxin
    • Tamarit J., Belli G., Cabiscol E., Herrero E., and Ros J. Biochemical characterization of yeast mitochondrial Grx5 monothiol glutaredoxin. J Biol Chem 278 (2003) 25745-25751
    • (2003) J Biol Chem , vol.278 , pp. 25745-25751
    • Tamarit, J.1    Belli, G.2    Cabiscol, E.3    Herrero, E.4    Ros, J.5
  • 84
    • 0037053377 scopus 로고    scopus 로고
    • Regulation of protein S-thiolation by glutaredoxin 5 in the yeast Saccharomyces cerevisiae
    • Shenton D., Perrone G., Quinn K.A., Dawes I.W., and Grant C.M. Regulation of protein S-thiolation by glutaredoxin 5 in the yeast Saccharomyces cerevisiae. J Biol Chem 277 (2002) 16853-16859
    • (2002) J Biol Chem , vol.277 , pp. 16853-16859
    • Shenton, D.1    Perrone, G.2    Quinn, K.A.3    Dawes, I.W.4    Grant, C.M.5
  • 85
    • 0242416188 scopus 로고    scopus 로고
    • ATP-dependent reduction of cysteine-sulphinic acid by S. cerevisiae sulphiredoxin
    • Biteau B., Labarre J., and Toledano M.B. ATP-dependent reduction of cysteine-sulphinic acid by S. cerevisiae sulphiredoxin. Nature 425 (2003) 980-984
    • (2003) Nature , vol.425 , pp. 980-984
    • Biteau, B.1    Labarre, J.2    Toledano, M.B.3
  • 86
    • 33746111275 scopus 로고    scopus 로고
    • A novel role for human sulfiredoxin in the reversal of glutathionylation
    • This study uses HEK 293 cells overexpressing sulfiredoxin (SRx) to implicate SRx in reversing protein glutathionylation associated with PABA/NO treatment. However, alternative mechanisms by which SRx might interfere with protein glutathionylation are not distinguished.
    • Findlay V.J., Townsend D.M., Morris T.E., Fraser J.P., He L., and Tew K.D. A novel role for human sulfiredoxin in the reversal of glutathionylation. Cancer Res 66 (2006) 6800-6806. This study uses HEK 293 cells overexpressing sulfiredoxin (SRx) to implicate SRx in reversing protein glutathionylation associated with PABA/NO treatment. However, alternative mechanisms by which SRx might interfere with protein glutathionylation are not distinguished.
    • (2006) Cancer Res , vol.66 , pp. 6800-6806
    • Findlay, V.J.1    Townsend, D.M.2    Morris, T.E.3    Fraser, J.P.4    He, L.5    Tew, K.D.6
  • 87
    • 33748347924 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae cells have three omega class glutathione S-transferases acting as 1-Cys thiol transferases
    • Garcera A., Barreto L., Piedrafita L., Tamarit J., and Herrero E. Saccharomyces cerevisiae cells have three omega class glutathione S-transferases acting as 1-Cys thiol transferases. Biochem J 398 (2006) 187-196
    • (2006) Biochem J , vol.398 , pp. 187-196
    • Garcera, A.1    Barreto, L.2    Piedrafita, L.3    Tamarit, J.4    Herrero, E.5
  • 88
    • 0033067791 scopus 로고    scopus 로고
    • Does glutathione-S-transferase dethiolate lens protein-thiol mixed disulfides? A comparative study with thioltransferase
    • Raghavachari N., Qiao F., and Lou M.F. Does glutathione-S-transferase dethiolate lens protein-thiol mixed disulfides? A comparative study with thioltransferase. Exp Eye Res 68 (1999) 715-724
    • (1999) Exp Eye Res , vol.68 , pp. 715-724
    • Raghavachari, N.1    Qiao, F.2    Lou, M.F.3
  • 89
  • 90
    • 1642326559 scopus 로고    scopus 로고
    • Activation of the antioxidant enzyme 1-CYS peroxiredoxin requires glutathionylation mediated by heterodimerization with pi GST
    • This work provided evidence for a novel mechanism of catalysis for both 1CysPRx (i.e. turnover by GSTπ) and for GSTπ (i.e. glutathionylation of protein-SOH). At present it represents the best studied example of catalyzed protein S-glutathionylation, providing a prototype for potential discovery of other glutathionylating enzymes that may act analogously.
    • Manevich Y., Feinstein S.I., and Fisher A.B. Activation of the antioxidant enzyme 1-CYS peroxiredoxin requires glutathionylation mediated by heterodimerization with pi GST. Proc Natl Acad Sci USA 101 (2004) 3780-3785. This work provided evidence for a novel mechanism of catalysis for both 1CysPRx (i.e. turnover by GSTπ) and for GSTπ (i.e. glutathionylation of protein-SOH). At present it represents the best studied example of catalyzed protein S-glutathionylation, providing a prototype for potential discovery of other glutathionylating enzymes that may act analogously.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 3780-3785
    • Manevich, Y.1    Feinstein, S.I.2    Fisher, A.B.3
  • 91
    • 30744437425 scopus 로고    scopus 로고
    • Direct evidence for the formation of a complex between 1-cysteine peroxiredoxin and glutathione S-transferase pi with activity changes in both enzymes
    • Ralat L.A., Manevich Y., Fisher A.B., and Colman R.F. Direct evidence for the formation of a complex between 1-cysteine peroxiredoxin and glutathione S-transferase pi with activity changes in both enzymes. Biochemistry 45 (2006) 360-372
    • (2006) Biochemistry , vol.45 , pp. 360-372
    • Ralat, L.A.1    Manevich, Y.2    Fisher, A.B.3    Colman, R.F.4
  • 92
    • 33947381788 scopus 로고    scopus 로고
    • Redox in redux: emergent roles for glutathione S-transferase P (GSTP) in regulation of cell signaling and S-glutathionylation
    • This comprehensive review offers provocative speculation on the role of GSTP in mediating protein glutathionylation under normal redox signaling conditions and in response to pharmacological stimulation (e.g. PABA/NO) in vivo.
    • Tew K.D. Redox in redux: emergent roles for glutathione S-transferase P (GSTP) in regulation of cell signaling and S-glutathionylation. Biochem Pharmacol 73 (2007) 1257-1269. This comprehensive review offers provocative speculation on the role of GSTP in mediating protein glutathionylation under normal redox signaling conditions and in response to pharmacological stimulation (e.g. PABA/NO) in vivo.
    • (2007) Biochem Pharmacol , vol.73 , pp. 1257-1269
    • Tew, K.D.1
  • 94
    • 31044436627 scopus 로고    scopus 로고
    • A glutathione S-transferase pi-activated prodrug causes kinase activation concurrent with S-glutathionylation of proteins
    • This study is the first to relate treatment with a potential pharmacological agent (PABA/NO) and protein glutathionylation. Protein-SSG formation and phosphorylation of some stress kinases occurred coincidently, suggesting a link to cytotoxicity.
    • Townsend D.M., Findlay V.J., Fazilev F., Ogle M., Fraser J., Saavedra J.E., Ji X., Keefer L.K., and Tew K.D. A glutathione S-transferase pi-activated prodrug causes kinase activation concurrent with S-glutathionylation of proteins. Mol Pharmacol 69 (2006) 501-508. This study is the first to relate treatment with a potential pharmacological agent (PABA/NO) and protein glutathionylation. Protein-SSG formation and phosphorylation of some stress kinases occurred coincidently, suggesting a link to cytotoxicity.
    • (2006) Mol Pharmacol , vol.69 , pp. 501-508
    • Townsend, D.M.1    Findlay, V.J.2    Fazilev, F.3    Ogle, M.4    Fraser, J.5    Saavedra, J.E.6    Ji, X.7    Keefer, L.K.8    Tew, K.D.9
  • 95
    • 0029005196 scopus 로고
    • Kinetics of thiol reactions
    • Schoneich C. Kinetics of thiol reactions. Meth Enzymol 251 (1995) 45-55
    • (1995) Meth Enzymol , vol.251 , pp. 45-55
    • Schoneich, C.1
  • 96
    • 0003083421 scopus 로고
    • Thiyl radicals, perththiyl radicals, and oxidative reactions
    • Packer L., and Cadenas E. (Eds), Marcel Dekker, Inc.
    • Shoneich C. Thiyl radicals, perththiyl radicals, and oxidative reactions. In: Packer L., and Cadenas E. (Eds). Biothiols in Health and Disease (1995), Marcel Dekker, Inc. 21-47
    • (1995) Biothiols in Health and Disease , pp. 21-47
    • Shoneich, C.1
  • 97
    • 34548169188 scopus 로고    scopus 로고
    • Wardman P: Reactions of thiyl radicals. Edited by Packer L, Cadenas E. Marcel Dekker, Inc.; 1995:1-19.
  • 98
    • 34547128886 scopus 로고    scopus 로고
    • Glutathione supplementation potentiates hypoxic apoptosis by S-glutathionylation of p65-NFkappa B
    • This study implicates GRx1 as a catalyst of glutathionylation of NFκB in situ.
    • Qanungo S., Starke D.W., Pai H.V., Mieyal J.J., and Nieminen A.L. Glutathione supplementation potentiates hypoxic apoptosis by S-glutathionylation of p65-NFkappa B. J Biol Chem (2007). This study implicates GRx1 as a catalyst of glutathionylation of NFκB in situ.
    • (2007) J Biol Chem
    • Qanungo, S.1    Starke, D.W.2    Pai, H.V.3    Mieyal, J.J.4    Nieminen, A.L.5
  • 100
    • 33646688670 scopus 로고    scopus 로고
    • Multidomain flavin-dependent sulfhydryl oxidases
    • This comprehensive review addresses the evolution, structure, activity, and putative cellular roles of sulfhydryl oxidases from all species.
    • Coppock D.L., and Thorpe C. Multidomain flavin-dependent sulfhydryl oxidases. Antioxid Redox Signal 8 (2006) 300-311. This comprehensive review addresses the evolution, structure, activity, and putative cellular roles of sulfhydryl oxidases from all species.
    • (2006) Antioxid Redox Signal , vol.8 , pp. 300-311
    • Coppock, D.L.1    Thorpe, C.2
  • 101
    • 0019321282 scopus 로고
    • Properties of a flavoprotein sulfhydryl oxidase from rat seminal vesicle secretion
    • Ostrowski M.C., and Kistler W.S. Properties of a flavoprotein sulfhydryl oxidase from rat seminal vesicle secretion. Biochemistry 19 (1980) 2639-2645
    • (1980) Biochemistry , vol.19 , pp. 2639-2645
    • Ostrowski, M.C.1    Kistler, W.S.2
  • 102
    • 34047250626 scopus 로고    scopus 로고
    • Reversible sequestration of active site cysteines in a 2Fe-2S-bridged dimer provides a mechanism for glutaredoxin 2 regulation in human mitochondria
    • This paper reports that human GRx2, like poplar C1 glutaredoxin, exists in a dimeric FeS cluster coordinated by 2 active sites of Cys and 2 GSH molecules, and it proposes oxidative regulation of GRx2.
    • Johansson C., Kavanagh K.L., Gileadi O., and Oppermann U. 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 (2007) 3077-3082. This paper reports that human GRx2, like poplar C1 glutaredoxin, exists in a dimeric FeS cluster coordinated by 2 active sites of Cys and 2 GSH molecules, and it proposes oxidative regulation of GRx2.
    • (2007) J Biol Chem , vol.282 , pp. 3077-3082
    • Johansson, C.1    Kavanagh, K.L.2    Gileadi, O.3    Oppermann, U.4
  • 103
    • 0036226063 scopus 로고    scopus 로고
    • Grx5 is a mitochondrial glutaredoxin required for the activity of iron/sulfur enzymes
    • Rodriguez-Manzaneque M.T., Tamarit J., Belli G., Ros J., and Herrero E. Grx5 is a mitochondrial glutaredoxin required for the activity of iron/sulfur enzymes. Mol Biol Cell 13 (2002) 1109-1121
    • (2002) Mol Biol Cell , vol.13 , pp. 1109-1121
    • Rodriguez-Manzaneque, M.T.1    Tamarit, J.2    Belli, G.3    Ros, J.4    Herrero, E.5
  • 104
    • 33744919853 scopus 로고    scopus 로고
    • Molecular mechanism of the reduction of cysteine sulfinic acid of peroxiredoxin to cysteine by mammalian sulfiredoxin
    • Jeong W., Park S.J., Chang T.S., Lee D.Y., and Rhee S.G. Molecular mechanism of the reduction of cysteine sulfinic acid of peroxiredoxin to cysteine by mammalian sulfiredoxin. J Biol Chem 281 (2006) 14400-14407
    • (2006) J Biol Chem , vol.281 , pp. 14400-14407
    • Jeong, W.1    Park, S.J.2    Chang, T.S.3    Lee, D.Y.4    Rhee, S.G.5
  • 106
    • 0020627222 scopus 로고
    • Synthesis and pH-dependent stability of purine-6-sulfenic acid, a putative reactive metabolite of 6-thiopurine
    • Abraham R.T., Benson L.M., and Jardine I. Synthesis and pH-dependent stability of purine-6-sulfenic acid, a putative reactive metabolite of 6-thiopurine. J Med Chem 26 (1983) 1523-1526
    • (1983) J Med Chem , vol.26 , pp. 1523-1526
    • Abraham, R.T.1    Benson, L.M.2    Jardine, I.3


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