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Volumn 17, Issue 2, 2012, Pages 63-71

Protein glutathionylation in cellular compartments: A constitutive redox signal

Author keywords

Cytoskeleton; Dermal fibroblasts; Glutathionylation; Nuclear lamina

Indexed keywords

GLUTATHIONE DERIVATIVE; PROTEIN BOUND GLUTATHIONE; UNCLASSIFIED DRUG;

EID: 84861158156     PISSN: 13510002     EISSN: 17432928     Source Type: Journal    
DOI: 10.1179/1351000212Y.0000000009     Document Type: Article
Times cited : (8)

References (42)
  • 1
    • 0036960604 scopus 로고    scopus 로고
    • Glutathione in defense and signaling: Lessons from a small thiol
    • Dickinson DA, Forman HJ. Glutathione in defense and signaling: lessons from a small thiol. Ann NY Acad Sci 2002;973: 488-504.
    • (2002) Ann NY Acad Sci , vol.973 , pp. 488-504
    • Dickinson, D.A.1    Forman, H.J.2
  • 2
    • 0142211205 scopus 로고    scopus 로고
    • Actin glutathionylation increases in fibroblasts of patients with Friedreich's ataxia: A potential role in the pathogenesis of the disease
    • Pastore A, Tozzi G, Gaeta LM, Bertini E, Serafini V, Di Cesare S, et al. Actin glutathionylation increases in fibroblasts of patients with Friedreich's ataxia: a potential role in the pathogenesis of the disease. J Biol Chem 2003;43:42588-95.
    • (2003) J Biol Chem , vol.43 , pp. 42588-42595
    • Pastore, A.1    Tozzi, G.2    Gaeta, L.M.3    Bertini, E.4    Serafini, V.5    di Cesare, S.6
  • 3
    • 0032488513 scopus 로고    scopus 로고
    • Recent trends in glutathione biochemistry. Glutathione-protein interactions: A molecular link between oxidative stress and cell proliferation?
    • Cotgreave IA, Gerdes RG. Recent trends in glutathione biochemistry. Glutathione-protein interactions: a molecular link between oxidative stress and cell proliferation? Biochem Biophys Res Commun 1998;242:1-9.
    • (1998) Biochem Biophys Res Commun , vol.242 , pp. 1-9
    • Cotgreave, I.A.1    Gerdes, R.G.2
  • 4
    • 0033869092 scopus 로고    scopus 로고
    • Regulation of protein function by S-glutathionylation in response to oxidative and nitrosative stress
    • Klatt P, Lamas S. Regulation of protein function by S-glutathionylation in response to oxidative and nitrosative stress. Eur J Biochem 2000;267:4928-44.
    • (2000) Eur J Biochem , vol.267 , pp. 4928-4944
    • Klatt, P.1    Lamas, S.2
  • 5
    • 18344390036 scopus 로고    scopus 로고
    • Identification by redox proteomics of glutathionylated proteins in oxidatively stressed human T lymphocytes
    • Fratelli M, Demol H, Puype M, Casagrande S, Eberini L, Salmona M, et al. Identification by redox proteomics of glutathionylated proteins in oxidatively stressed human T lymphocytes. Proc Natl Acad Sci USA 2002;99:3505-10.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 3505-3510
    • Fratelli, M.1    Demol, H.2    Puype, M.3    Casagrande, S.4    Eberini, L.5    Salmona, M.6
  • 6
    • 14044272119 scopus 로고    scopus 로고
    • S-glutathionylation: From redox regulation of protein functions to human diseases
    • Giustarini D, Rossi R, Milzani A, Colombo R, Dalle-Donne I. S-glutathionylation: from redox regulation of protein functions to human diseases. J Cell Mol Med 2004;8:201-12.
    • (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
  • 7
    • 0035960648 scopus 로고    scopus 로고
    • Glutathionylation of the p50 subunit of NF-kB: A mechanism for redox-induced inhibition of DNA binding
    • Pineda-Molina E, Klatt P, Vazquez J, Marina A, Garcia de Jacoba M, Perez-Sala D, et al. Glutathionylation of the p50 subunit of NF-kB: a mechanism for redox-induced inhibition of DNA binding. Biochemistry 2001;40:14134-42.
    • (2001) Biochemistry , vol.40 , pp. 14134-14142
    • Pineda-Molina, E.1    Klatt, P.2    Vazquez, J.3    Marina, A.4    de Garcia, J.M.5    Perez-Sala, D.6
  • 8
    • 31844438837 scopus 로고    scopus 로고
    • Protein glutathionylation in human central nervous system: Potential role in redox regulation of neuronal defense against free radicals
    • Sparaco M, Gaeta LM, Tozzi G, Bertini E, Pastore A, Simonati A, et al. Protein glutathionylation in human central nervous system: potential role in redox regulation of neuronal defense against free radicals. J Neurosci Res 2006;83:256-63.
    • (2006) J Neurosci Res , vol.83 , pp. 256-263
    • Sparaco, M.1    Gaeta, L.M.2    Tozzi, G.3    Bertini, E.4    Pastore, A.5    Simonati, A.6
  • 9
  • 11
    • 0028170673 scopus 로고
    • S-thiolation of glyceraldehyde-3-phosphate dehydrogenase induced by the phagocytosis-associated respiratory burst in blood monocytes
    • Ravichandran V, Seres T, Moriguchi T, Thomas JA, Johnston RB. S-thiolation of glyceraldehyde-3-phosphate dehydrogenase induced by the phagocytosis-associated respiratory burst in blood monocytes. J Biol Chem 1994;269:25010-5.
    • (1994) J Biol Chem , vol.269 , pp. 25010-25015
    • Ravichandran, V.1    Seres, T.2    Moriguchi, T.3    Thomas, J.A.4    Johnston, R.B.5
  • 12
    • 0028204459 scopus 로고
    • Sthiolation of human endothelial cell glyceraldehyde-3-phosphate dehydrogenase after hydrogen peroxide treatment
    • Schuppe-Koisinen I, Moldeus P, Bergmann T, Coatgreave IA. Sthiolation of human endothelial cell glyceraldehyde-3-phosphate dehydrogenase after hydrogen peroxide treatment. Eur J Biochem 1994;221:1033-7.
    • (1994) Eur J Biochem , vol.221 , pp. 1033-1037
    • Schuppe-Koisinen, I.1    Moldeus, P.2    Bergmann, T.3    Coatgreave, I.A.4
  • 13
    • 2542486403 scopus 로고    scopus 로고
    • Inactivation of creatine kinase by S-glutathionylation of the active-site cysteine residue
    • Reddy S, Jones AD, Cross CE, Wong PS, Van Der Vliet A. Inactivation of creatine kinase by S-glutathionylation of the active-site cysteine residue. Biochem J 2000;347(Pt 3):821-7.
    • (2000) Biochem J , vol.347 , Issue.3 PT. , pp. 821-827
    • Reddy, S.1    Jones, A.D.2    Cross, C.E.3    Wong, P.S.4    van der Vliet, A.5
  • 14
    • 0034662178 scopus 로고    scopus 로고
    • Novel application of S-nitrosoglutathione-Sepharose to identify proteins that are potential targets for S-nitrosoglutathione-induced mixeddisulphide formation
    • Klatt P, Pineda Molina E, Pérez-Sala D, Lamas S. Novel application of S-nitrosoglutathione-Sepharose to identify proteins that are potential targets for S-nitrosoglutathione-induced mixeddisulphide formation. Biochem J 2000;349(Pt 2):567-78.
    • (2000) Biochem J , vol.349 , Issue.2 PT. , pp. 567-578
    • Klatt, P.1    Pineda, M.E.2    Pérez-Sala, D.3    Lamas, S.4
  • 15
    • 18844427352 scopus 로고    scopus 로고
    • S-glutathionylation in human platelets by a thiol-disulfide exchange-independent mechanism
    • Dalle-Donne I, Giustarini D, Colombo R, Milzani A, Rossi R. S-glutathionylation in human platelets by a thiol-disulfide exchange-independent mechanism. Free Radic Biol Med 2005; 38:1501-10.
    • (2005) Free Radic Biol Med , vol.38 , pp. 1501-1510
    • Dalle-Donne, I.1    Giustarini, D.2    Colombo, R.3    Milzani, A.4    Rossi, R.5
  • 16
    • 0348109493 scopus 로고    scopus 로고
    • Different types of glutathionylation of hemoglobin can exist in intact erythrocytes
    • Mawatari S, Murakami K. Different types of glutathionylation of hemoglobin can exist in intact erythrocytes. Arch Biochem Biophys 2004;421:108-14.
    • (2004) Arch Biochem Biophys , vol.421 , pp. 108-114
    • Mawatari, S.1    Murakami, K.2
  • 17
    • 0042665896 scopus 로고    scopus 로고
    • Identification of proteins undergoing glutathionylation in oxidatively stressed hepatocytes and hepatoma cells
    • Fratelli M, Demol H, Puype M, Casagrande S, Villa P, Eberini L, et al. Identification of proteins undergoing glutathionylation in oxidatively stressed hepatocytes and hepatoma cells. Proteomics 2003;3:1154-61.
    • (2003) Proteomics , vol.3 , pp. 1154-1161
    • Fratelli, M.1    Demol, H.2    Puype, M.3    Casagrande, S.4    Villa, P.5    Eberini, L.6
  • 19
    • 12244311183 scopus 로고    scopus 로고
    • Reversible S-glutathionylation of Cys 374 regulates actin filament formation by inducing structural changes in the actin molecule
    • Dalle-Donne I, Giustarini D, Rossi R, Colombo R, Milzani A. Reversible S-glutathionylation of Cys 374 regulates actin filament formation by inducing structural changes in the actin molecule. Free Rad Biol Med 2003;34:23-32.
    • (2003) Free Rad Biol Med , vol.34 , pp. 23-32
    • Dalle-Donne, I.1    Giustarini, D.2    Rossi, R.3    Colombo, R.4    Milzani, A.5
  • 20
    • 0035930608 scopus 로고    scopus 로고
    • Reversible glutathionylation regulates actin polymerization in A431 cells
    • Wang J, Boja ES, Tan W, Tekle E, Fales HM, English S, et al. Reversible glutathionylation regulates actin polymerization in A431 cells. J Biol Chem 2001;276:47763-6.
    • (2001) J Biol Chem , vol.276 , pp. 47763-47766
    • Wang, J.1    Boja, E.S.2    Tan, W.3    Tekle, E.4    Fales, H.M.5    English, S.6
  • 21
    • 0038303229 scopus 로고    scopus 로고
    • Stable and controllable RNA interference: Investigating and physiological function of glutathionylated actin
    • Wang J, Tekle E, Oubrahim H, Mieyal JJ, Stadtman ER, Chock PB. Stable and controllable RNA interference: investigating and physiological function of glutathionylated actin. Proc Natl Acad Sci USA 2003;100:5103-6.
    • (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
  • 22
    • 0347635415 scopus 로고    scopus 로고
    • Modulation of the redox state of tubulin by the glutathione/glutaredoxin reductase system
    • Landino LM, Moynihan KL, Todd JV, Kennett KL. Modulation of the redox state of tubulin by the glutathione/glutaredoxin reductase system. Biochem Biophys Res Commun 2004a;314:555-60.
    • (2004) Biochem Biophys Res Commun , vol.314 , pp. 555-560
    • Landino, L.M.1    Moynihan, K.L.2    Todd, J.V.3    Kennett, K.L.4
  • 23
    • 4444330824 scopus 로고    scopus 로고
    • Redox modulation of tau and microtubule-associated protein-2 by the glutathione/glutaredoxin reductase system
    • Landino LM, Robinson SH, Skreslet TE, Cabral DM. Redox modulation of tau and microtubule-associated protein-2 by the glutathione/glutaredoxin reductase system. Biochem Biophys Res Commun 2004b;323:112-7.
    • (2004) Biochem Biophys Res Commun , vol.323 , pp. 112-117
    • Landino, L.M.1    Robinson, S.H.2    Skreslet, T.E.3    Cabral, D.M.4
  • 27
    • 34547110841 scopus 로고    scopus 로고
    • Glutathione is recruited into the nucleus in early phases of cell proliferation
    • Markovic J, Borrás C, Ortega A, Sastre J, Viña J, Pallardó FV. Glutathione is recruited into the nucleus in early phases of cell proliferation. J Biol Chem 2007;282(28):20416-24.
    • (2007) J Biol Chem , vol.282 , Issue.28 , pp. 20416-20424
    • Markovic, J.1    Borrás, C.2    Ortega, A.3    Sastre, J.4    Viña, J.5    Pallardó, F.V.6
  • 28
    • 65049087578 scopus 로고    scopus 로고
    • Role of nuclear glutathione as a key regulator of cell proliferation
    • Pallardó FV, Markovic J, García JL, Viña J. Role of nuclear glutathione as a key regulator of cell proliferation. Mol Aspects Med 2009;30:77-85.
    • (2009) Mol Aspects Med , vol.30 , pp. 77-85
    • Pallardó, F.V.1    Markovic, J.2    García, J.L.3    Viña, J.4
  • 30
    • 77957315403 scopus 로고    scopus 로고
    • Redox compartmentalization and cellular stress
    • Jones DP, Go YM. Redox compartmentalization and cellular stress. Diabetes Obes Metab 2010;12(2):116-25.
    • (2010) Diabetes Obes Metab , vol.12 , Issue.2 , pp. 116-125
    • Jones, D.P.1    Go, Y.M.2
  • 31
    • 0034911738 scopus 로고    scopus 로고
    • Determination of blood total, reduced and oxidized glutathione in pediatric subjects
    • Pastore A, Piemonte F, Locatelli M, Lo Russo A, Gaeta LM, Tozzi G, et al. Determination of blood total, reduced and oxidized glutathione in pediatric subjects. Clin Chem 2001;47: 1467-9.
    • (2001) Clin Chem , vol.47 , pp. 1467-1469
    • Pastore, A.1    Piemonte, F.2    Locatelli, M.3    Russo Lo, A.4    Gaeta, L.M.5    Tozzi, G.6
  • 33
    • 49349085256 scopus 로고    scopus 로고
    • Redox compartmentalization in eukaryotic cells
    • Go YM, Jones DP. Redox compartmentalization in eukaryotic cells. Biochim Biophys Acta 2008;1780:1273-90.
    • (2008) Biochim Biophys Acta , vol.1780 , pp. 1273-1290
    • Go, Y.M.1    Jones, D.P.2
  • 34
    • 71549117899 scopus 로고    scopus 로고
    • The nuclear envelope as a signaling node in development and disease
    • Dauer WT, Worman HJ. The nuclear envelope as a signaling node in development and disease. Dev Cell 2009;17:626-38.
    • (2009) Dev Cell , vol.17 , pp. 626-638
    • Dauer, W.T.1    Worman, H.J.2
  • 38
    • 48649100200 scopus 로고    scopus 로고
    • Protein glutathionylation increases in the liver of patients with non-alcoholic fatty liver disease
    • Piemonte F, Petrini S, Gaeta LM, Tozzi G, Bertini E, Devito R, et al. Protein glutathionylation increases in the liver of patients with non-alcoholic fatty liver disease. Hepatology 2007;23:457-64.
    • (2007) Hepatology , vol.23 , pp. 457-464
    • Piemonte, F.1    Petrini, S.2    Gaeta, L.M.3    Tozzi, G.4    Bertini, E.5    Devito, R.6
  • 39
    • 0022818865 scopus 로고
    • Methodologies for the application of monobromobimane to the simultaneous analysis of soluble and protein thiol components of biological systems
    • Cotgreave IA, Moldeus P. Methodologies for the application of monobromobimane to the simultaneous analysis of soluble and protein thiol components of biological systems. J Biochem Biophys Methods 1986;13:231-49.
    • (1986) J Biochem Biophys Methods , vol.13 , pp. 231-249
    • Cotgreave, I.A.1    Moldeus, P.2
  • 40
    • 77951722027 scopus 로고    scopus 로고
    • Determination of intracellular glutathione and cysteine using HPLC with a monolithic column after derivatization with monobromobimane
    • Conlan XA, Stupka N, McDermott GP, Francis PS, Barnett NW. Determination of intracellular glutathione and cysteine using HPLC with a monolithic column after derivatization with monobromobimane. Biomed Chromatogr 2010;24(5): 455-7.
    • (2010) Biomed Chromatogr , vol.24 , Issue.5 , pp. 455-457
    • Conlan, X.A.1    Stupka, N.2    McDermott, G.P.3    Francis, P.S.4    Barnett, N.W.5
  • 41
    • 33644669954 scopus 로고    scopus 로고
    • The utility of N,N-biotinyl glutathione disulfide in the study of protein S-glutathiolation
    • Brennan JP, Miller JIA, Fuller W, Wait R, Begum S, Dunn MJ, et al. The utility of N,N-biotinyl glutathione disulfide in the study of protein S-glutathiolation. Mol Cell Proteomics 2006;5: 215-25.
    • (2006) Mol Cell Proteomics , vol.5 , pp. 215-225
    • Brennan, J.P.1    Miller, J.I.A.2    Fuller, W.3    Wait, R.4    Begum, S.5    Dunn, M.J.6
  • 42
    • 77951979741 scopus 로고    scopus 로고
    • S-Glutathionylation regulates inflammatory activities of S100A9
    • Lim SY, Raftery MJ, Goyette J, Geczy CL. S-Glutathionylation regulates inflammatory activities of S100A9. J Biol Chem 2010; 285(19):14377-88.
    • (2010) J Biol Chem , vol.285 , Issue.19 , pp. 14377-14388
    • Lim, S.Y.1    Raftery, M.J.2    Goyette, J.3    Geczy, C.L.4


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