메뉴 건너뛰기




Volumn 39, Issue 6, 2005, Pages 573-580

Regulation of protein function by glutathionylation

Author keywords

Cysteines; Dethiolating agent; Glutathione; Thiol disulfide exchange

Indexed keywords

CYSTEINE; GLUTAREDOXIN; GLUTATHIONE; GLUTATHIONE DISULFIDE; ISOMERASE; OXIDOREDUCTASE; PHOSPHATASE; PROTEIN DISULFIDE REDUCTASE (GLUTATHIONE); PROTEIN KINASE; REACTIVE OXYGEN METABOLITE; SULFENIC ACID DERIVATIVE; THIOREDOXIN; THIOREDOXIN REDUCTASE;

EID: 20544472348     PISSN: 10715762     EISSN: None     Source Type: Journal    
DOI: 10.1080/10715760500072172     Document Type: Review
Times cited : (246)

References (53)
  • 1
    • 0017747006 scopus 로고
    • On the cysteine and cystine content of proteins. Differences between intracellular and extracellular proteins
    • Fahey RC, Hunt JS, Windham GC. On the cysteine and cystine content of proteins. Differences between intracellular and extracellular proteins. J Mol Evol 1977;10: 155-160.
    • (1977) J. Mol. Evol. , vol.10 , pp. 155-160
    • Fahey, R.C.1    Hunt, J.S.2    Windham, G.C.3
  • 2
    • 0019881763 scopus 로고
    • Disulphide bridges in globular proteins
    • Thornton JM. Disulphide bridges in globular proteins. J Mol Biol 1981;151:261-287.
    • (1981) J. Mol. Biol. , vol.151 , pp. 261-287
    • Thornton, J.M.1
  • 3
    • 0026698060 scopus 로고
    • Oxidized redox state of glutathione in the endoplasmic reticulum
    • Hwang C, Sinskey AJ, Lodish HF. Oxidized redox state of glutathione in the endoplasmic reticulum. Science 1992;257:1496-1502.
    • (1992) Science , vol.257 , pp. 1496-1502
    • Hwang, C.1    Sinskey, A.J.2    Lodish, H.F.3
  • 4
    • 0025739254 scopus 로고
    • Reactive oxygen intermediates as apparently widely used messengers in the activation of the NF-kappa B transcription factor and HIV-1
    • Schreck R, Rieber P, Baeuerle PA. Reactive oxygen intermediates as apparently widely used messengers in the activation of the NF-kappa B transcription factor and HIV-1. Embo J 1991;10:2247-2258.
    • (1991) Embo J. , vol.10 , pp. 2247-2258
    • Schreck, R.1    Rieber, P.2    Baeuerle, P.A.3
  • 5
    • 0025677250 scopus 로고
    • Intracellular thiols regulate activation of nuclear factor kappa B and transcription of human immunodeficiency virus
    • Staal FJ, Roederer M, Herzenberg LA. Intracellular thiols regulate activation of nuclear factor kappa B and transcription of human immunodeficiency virus. Proc Natl Acad Sci USA 1990;87:9943-9947.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 9943-9947
    • Staal, F.J.1    Roederer, M.2    Herzenberg, L.A.3
  • 6
    • 0020624295 scopus 로고
    • Identification and quantitation of glutathione in hepatic protein mixed disulfides and its relationship to glutathione disulfide
    • Brigelius R, Muckel C, Akerboom TP, Sies H. Identification and quantitation of glutathione in hepatic protein mixed disulfides and its relationship to glutathione disulfide. Biochem Pharmacol 1983;32:2529-2534.
    • (1983) Biochem. Pharmacol. , vol.32 , pp. 2529-2534
    • Brigelius, R.1    Muckel, C.2    Akerboom, T.P.3    Sies, H.4
  • 7
    • 0020025906 scopus 로고
    • Increase in hepatic mixed disulphide and glutathione disulphide levels elicited by paraquat
    • Brigelius R, Lenzen R, Sies H. Increase in hepatic mixed disulphide and glutathione disulphide levels elicited by paraquat. Biochem Pharmacol 1982;31:1637-1641.
    • (1982) Biochem. Pharmacol. , vol.31 , pp. 1637-1641
    • Brigelius, R.1    Lenzen, R.2    Sies, H.3
  • 8
    • 0021284165 scopus 로고
    • Redox control of enzyme activities by thiol/disulfide exchange
    • Gilbert HF. Redox control of enzyme activities by thiol/disulfide exchange. Methods Enzymol 1984;107:330-351.
    • (1984) Methods Enzymol. , vol.107 , pp. 330-351
    • Gilbert, H.F.1
  • 9
    • 0023084124 scopus 로고
    • Formation of disulfides with diamide
    • Kosower NS, Kosower EM. Formation of disulfides with diamide. Methods Enzymol 1987;143:264-270.
    • (1987) Methods Enzymol. , vol.143 , pp. 264-270
    • Kosower, N.S.1    Kosower, E.M.2
  • 10
    • 0033521019 scopus 로고    scopus 로고
    • Roles of superoxide radical anion in signal transduction mediated by reversible regulation of protein-tyrosine phosphatase 1B
    • Barrett WC, DeGnore JP, Keng YF, Zhang ZY, Yim MB, Chock PB. Roles of superoxide radical anion in signal transduction mediated by reversible regulation of protein-tyrosine phosphatase 1B. J Biol Chem 1999;274:34543-34546.
    • (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
  • 11
    • 0347966073 scopus 로고    scopus 로고
    • Signal transduction by reactive oxygen and nitrogen species
    • Dordrecht, The Netherlands: Kluwer
    • Forman HJ, Fukuto J, Torres M, Signal transduction by reactive oxygen and nitrogen species. Dordrecht, The Netherlands: Kluwer; 2003.
    • (2003)
    • Forman, H.J.1    Fukuto, J.2    Torres, M.3
  • 12
    • 0028298361 scopus 로고
    • S-thiolation of individual human neutrophil proteins including actin by stimulation of the respiratory burst: Evidence against a role for glutathione disulfide
    • Chai YC, Ashraf SS, Rokutan K, Johnston Jr., RB, Thomas JA. S-thiolation of individual human neutrophil proteins including actin by stimulation of the respiratory burst: Evidence against a role for glutathione disulfide. Arch Biochem Biophys 1994;310:273-281.
    • (1994) Arch. Biochem. Biophys. , vol.310 , pp. 273-281
    • Chai, Y.C.1    Ashraf, S.S.2    Rokutan, K.3    Johnston Jr., R.B.4    Thomas, J.A.5
  • 14
    • 0038015010 scopus 로고    scopus 로고
    • Glutathione-thiyl radical scavenging and transferase properties of human glutaredoxin (thioltransferase). Potential role in redox signal transduction
    • Starke DW, Chock PB, Mieyal JJ. Glutathione-thiyl radical scavenging and transferase properties of human glutaredoxin (thioltransferase). Potential role in redox signal transduction. J Biol Chem 2003;278:14607-14613.
    • (2003) J. Biol. Chem. , vol.278 , pp. 14607-14613
    • Starke, D.W.1    Chock, P.B.2    Mieyal, J.J.3
  • 16
    • 0003674626 scopus 로고
    • Chemistry and biochemistry of the sulfhydryl group in amino acids, peptides, and proteins
    • Oxford: Pergamon Press Ltd
    • Friedman M. Chemistry and biochemistry of the sulfhydryl group in amino acids, peptides, and proteins. Oxford: Pergamon Press Ltd. 1973.
    • (1973)
    • Friedman, M.1
  • 18
    • 0024393963 scopus 로고
    • Thioredoxin and glutaredoxin systems
    • Holmgren A. Thioredoxin and glutaredoxin systems. J Biol Chem 1989;264:13963-13966.
    • (1989) J. Biol. Chem. , vol.264 , pp. 13963-13966
    • Holmgren, A.1
  • 22
    • 0025887464 scopus 로고
    • Thioltransferase in human red blood cells: Kinetics and equilibrium
    • Mieyal JJ, Starke DW, Gravina SA, Hocevar BA. Thioltransferase in human red blood cells: Kinetics and equilibrium. Biochemistry 1991;30:8883-8891.
    • (1991) Biochemistry , vol.30 , pp. 8883-8891
    • Mieyal, J.J.1    Starke, D.W.2    Gravina, S.A.3    Hocevar, B.A.4
  • 23
    • 0028037601 scopus 로고
    • Possible differences in the regenerative roles played by thioltransferase and thioredoxin for oxidatively damaged proteins
    • Yoshitake S, Nanri H, Fernando MR, Minakami S. Possible differences in the regenerative roles played by thioltransferase and thioredoxin for oxidatively damaged proteins. J Biochem (Tokyo) 1994;116:42-46.
    • (1994) J. Biochem. (Tokyo) , vol.116 , pp. 42-46
    • Yoshitake, S.1    Nanri, H.2    Fernando, M.R.3    Minakami, S.4
  • 25
    • 0038303229 scopus 로고    scopus 로고
    • Stable and controllable RNA interference: Investigating the physiological function of glutathionylated actin
    • Wang J, Tekle E, Oubrahim H, Mieyal JJ, Stadtman ER, Chock PB. Stable and controllable RNA interference: Investigating the physiological function of glutathionylated actin. Proc Natl Acad Sci USA 2003;100:5103-5106.
    • (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
  • 26
    • 0020804830 scopus 로고
    • Relative contributions of thioltransferase-and thioredoxin-dependent systems in reduction of low-molecular-mass and protein disulphides
    • Mannervik B, Axelsson K, Sundewall AC, Holmgren A. Relative contributions of thioltransferase-and thioredoxin-dependent systems in reduction of low-molecular-mass and protein disulphides. Biochem J 1983;213:519-523.
    • (1983) Biochem. J. , vol.213 , pp. 519-523
    • Mannervik, B.1    Axelsson, K.2    Sundewall, A.C.3    Holmgren, A.4
  • 27
    • 0029015864 scopus 로고
    • Protein sulfhydryls and their role in the antioxidant function of protein S-thiolation
    • Thomas JA, Poland B, Honzatko R. Protein sulfhydryls and their role in the antioxidant function of protein S-thiolation. Arch Biochem Biophys 1995;319:1-9.
    • (1995) Arch. Biochem. Biophys. , vol.319 , pp. 1-9
    • Thomas, J.A.1    Poland, B.2    Honzatko, R.3
  • 28
    • 0033972054 scopus 로고    scopus 로고
    • On the functional interchangeability, oxidant versus reductant, of members of the thioredoxin superfamily
    • Debarbieux L, Beckwith J. On the functional interchangeability, oxidant versus reductant, of members of the thioredoxin superfamily. J Bacteriol 2000;182:723-727.
    • (2000) J. Bacteriol. , vol.182 , pp. 723-727
    • Debarbieux, L.1    Beckwith, J.2
  • 29
    • 0032167852 scopus 로고    scopus 로고
    • The reductive enzyme thioredoxin 1 acts as an oxidant when it is exported to the Escherichia coli periplasm
    • Debarbieux L, Beckwith J. The reductive enzyme thioredoxin 1 acts as an oxidant when it is exported to the Escherichia coli periplasm. Proc Natl Acad Sci USA 1998;95:10751-10756.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 10751-10756
    • Debarbieux, L.1    Beckwith, J.2
  • 30
    • 0032587961 scopus 로고    scopus 로고
    • 17 beta-estradiol induces protein thiol/disulfide oxidoreductases and protects cultured bovine aortic endothelial cells from oxidative stress
    • Ejima K, Nanri H, Araki M, Uchida K, Kashimura M, Ikeda M. 17 beta-estradiol induces protein thiol/disulfide oxidoreductases and protects cultured bovine aortic endothelial cells from oxidative stress. Eur J Endocrinol 1999; 140:608-613.
    • (1999) Eur. J. Endocrinol. , vol.140 , pp. 608-613
    • Ejima, K.1    Nanri, H.2    Araki, M.3    Uchida, K.4    Kashimura, M.5    Ikeda, M.6
  • 32
    • 0032983979 scopus 로고    scopus 로고
    • Nitric oxide inhibits c-Jun DNA binding by specifically targeted S-glutathionylation
    • Klatt P, Molina EP, Lamas S. Nitric oxide inhibits c-Jun DNA binding by specifically targeted S-glutathionylation. J Biol Chem 1999;274:15857-15864.
    • (1999) J. Biol. Chem. , vol.274 , pp. 15857-15864
    • Klatt, P.1    Molina, E.P.2    Lamas, S.3
  • 34
    • 0034903753 scopus 로고    scopus 로고
    • Potent inactivation of representative members of each PKC isozyme subfamily and PKD via S-thiolation by the tumor-promotion/progression antagonist glutathione but not by its precursor cysteine
    • Chu F, Ward NE, O'Brian CA. Potent inactivation of representative members of each PKC isozyme subfamily and PKD via S-thiolation by the tumor-promotion/progression antagonist glutathione but not by its precursor cysteine. Carcinogenesis 2001;22:1221-1229.
    • (2001) Carcinogenesis , vol.22 , pp. 1221-1229
    • Chu, F.1    Ward, N.E.2    O'Brian, C.A.3
  • 37
    • 0021288857 scopus 로고
    • Glutathione disulfide (GSSG) efflux from cells and tissues
    • Sies H, Akerboom TP. Glutathione disulfide (GSSG) efflux from cells and tissues. Methods Enzymol 1984;105:445-451.
    • (1984) Methods Enzymol. , vol.105 , pp. 445-451
    • Sies, H.1    Akerboom, T.P.2
  • 38
    • 0042761742 scopus 로고    scopus 로고
    • Evolution of the coordinate regulation of glycolytic enzyme genes by hypoxia
    • Webster KA. Evolution of the coordinate regulation of glycolytic enzyme genes by hypoxia. J Exp Biol 2003;206: 2911-2922.
    • (2003) J. Exp. Biol. , vol.206 , pp. 2911-2922
    • Webster, K.A.1
  • 39
    • 0042261992 scopus 로고    scopus 로고
    • Protein S-thiolation targets glycolysis and protein synthesis in response to oxidative stress in the yeast Saccharomyces cerevisiae
    • Shenton D, Grant CM. Protein S-thiolation targets glycolysis and protein synthesis in response to oxidative stress in the yeast Saccharomyces cerevisiae. Biochem J 2003;374:513-519.
    • (2003) Biochem. J. , vol.374 , pp. 513-519
    • Shenton, D.1    Grant, C.M.2
  • 42
    • 12644252321 scopus 로고    scopus 로고
    • ATP depletion affects the phosphorylation state, ligand binding, and nuclear transport of the 4 S polycyclic aromatic hydrocarbon-binding protein in rat hepatoma cells
    • Bhat R, Weaver JA, Wagner C, Bodwell JE, Bresnick E. ATP depletion affects the phosphorylation state, ligand binding, and nuclear transport of the 4 S polycyclic aromatic hydrocarbon-binding protein in rat hepatoma cells. J Biol Chem 1996;271:32551-32556.
    • (1996) J. Biol. Chem. , vol.271 , pp. 32551-32556
    • Bhat, R.1    Weaver, J.A.2    Wagner, C.3    Bodwell, J.E.4    Bresnick, E.5
  • 43
    • 0033524938 scopus 로고    scopus 로고
    • Chaperone activity with a redox switch
    • Jakob U, Muse W, Eser M, Bardwell JC. Chaperone activity with a redox switch. Cell 1999;96:341-352.
    • (1999) Cell , vol.96 , pp. 341-352
    • Jakob, U.1    Muse, W.2    Eser, M.3    Bardwell, J.C.4
  • 45
    • 1942423136 scopus 로고    scopus 로고
    • Protein s-glutathionylation in retinal pigment epithelium converts heat shock protein 70 to an active chaperone
    • Hoppe G, Chai YC, Crabb JW, Sears J. Protein s-glutathionylation in retinal pigment epithelium converts heat shock protein 70 to an active chaperone. Exp Eye Res 2004;78:1085-1092.
    • (2004) Exp. Eye Res. , vol.78 , pp. 1085-1092
    • Hoppe, G.1    Chai, Y.C.2    Crabb, J.W.3    Sears, J.4
  • 47
    • 0034662178 scopus 로고    scopus 로고
    • Novel application of S-nitrosoglutathione-Sepharose to identify proteins that are potential targets for S-nitrosoglutathione-induced mixed-disulphide formation
    • Klatt P, Pineda Molina E, Perez-Sala D, Lamas S. Novel application of S-nitrosoglutathione-Sepharose to identify proteins that are potential targets for S-nitrosoglutathione-induced mixed-disulphide formation. Biochem J 2000;349:567-578.
    • (2000) Biochem. J. , vol.349 , pp. 567-578
    • Klatt, P.1    Pineda Molina, E.2    Perez-Sala, D.3    Lamas, S.4
  • 48
    • 0034647933 scopus 로고    scopus 로고
    • Antioxidant/pro-oxidant equilibrium regulates HIF-1alpha and NF-kappa B redox sensitivity. Evidence for inhibition by glutathione oxidation in alveolar epithelial cells
    • Haddad JJ, Olver RE, Land SC. Antioxidant/pro-oxidant equilibrium regulates HIF-1alpha and NF-kappa B redox sensitivity. Evidence for inhibition by glutathione oxidation in alveolar epithelial cells. J Biol Chem 2000;275:21130-21139.
    • (2000) J. Biol. Chem. , vol.275 , pp. 21130-21139
    • Haddad, J.J.1    Olver, R.E.2    Land, S.C.3
  • 49
    • 0036401454 scopus 로고    scopus 로고
    • Identification of S-glutathionylated cellular proteins during oxidative stress and constitutive metabolism by affinity purification and proteomic analysis
    • Lind C, Gerdes R, Hamnell Y, Schuppe-Koistinen I, von Lowenhielm HB, Holmgren A, Cotgreave IA. Identification of S-glutathionylated cellular proteins during oxidative stress and constitutive metabolism by affinity purification and proteomic analysis. Arch Biochem Biophys 2002;406: 229-240.
    • (2002) Arch. Biochem. Biophys. , vol.406 , pp. 229-240
    • Lind, C.1    Gerdes, R.2    Hamnell, Y.3    Schuppe-Koistinen, I.4    von Lowenhielm, H.B.5    Holmgren, A.6    Cotgreave, I.A.7
  • 52
    • 0034646457 scopus 로고    scopus 로고
    • Mammalian thioredoxin reductase: Oxidation of the C-terminal cysteine/selenocysteine active site forms a thioselenide, and replacement of selenium with sulfur markedly reduces catalytic activity
    • Lee SR, Bar-Noy S, Kwon J, Levine RL, Stadtman TC, Rhee SG. Mammalian thioredoxin reductase: Oxidation of the C-terminal cysteine/selenocysteine active site forms a thioselenide, and replacement of selenium with sulfur markedly reduces catalytic activity. Proc Natl Acad Sci USA 2000;97:2521-2526.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 2521-2526
    • Lee, S.R.1    Bar-Noy, S.2    Kwon, J.3    Levine, R.L.4    Stadtman, T.C.5    Rhee, S.G.6
  • 53
    • 0034674566 scopus 로고    scopus 로고
    • Essential role of selenium in the catalytic activities of mammalian thioredoxin reductase revealed by characterization of recombinant enzymes with selenocysteine mutations
    • Zhong L, Holmgren A. Essential role of selenium in the catalytic activities of mammalian thioredoxin reductase revealed by characterization of recombinant enzymes with selenocysteine mutations. J Biol Chem 2000;275: 18121-18128.
    • (2000) J. Biol. Chem. , vol.275 , pp. 18121-18128
    • Zhong, L.1    Holmgren, A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.