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Volumn 7, Issue 4, 2007, Pages 398-403

Glutathionylation pathways in drug response

Author keywords

[No Author keywords available]

Indexed keywords

AUROTHIOGLUCOSE; BACITRACIN; CARMUSTINE; GLUTATHIONE; HISTONE DEACETYLASE INHIBITOR; PROTEIN; PROTEIN KINASE INHIBITOR;

EID: 34548082849     PISSN: 14714892     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.coph.2007.04.006     Document Type: Review
Times cited : (48)

References (30)
  • 1
    • 0021284165 scopus 로고
    • Redox control of enzyme activities by thiol/disulfide exchange
    • Gilbert H.F. Redox control of enzyme activities by thiol/disulfide exchange. Methods Enzymol 107 (1984) 330-351
    • (1984) Methods Enzymol , vol.107 , pp. 330-351
    • Gilbert, H.F.1
  • 2
    • 0025677250 scopus 로고
    • Intracellular thiols regulate activation of nuclear factor kappa B and transcription of human immunodeficiency virus
    • Staal F.J., Roederer M., and Herzenberg L.A. Intracellular thiols regulate activation of nuclear factor kappa B and transcription of human immunodeficiency virus. Proc Natl Acad Sci USA 87 (1990) 9943-9947
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 9943-9947
    • Staal, F.J.1    Roederer, M.2    Herzenberg, L.A.3
  • 3
    • 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., and Baeuerle P.A. Reactive oxygen intermediates as apparently widely used messengers in the activation of the NF-kappa B transcription factor and HIV-1. EMBO J 10 (1991) 2247-2258
    • (1991) EMBO J , vol.10 , pp. 2247-2258
    • Schreck, R.1    Rieber, P.2    Baeuerle, P.A.3
  • 6
    • 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
  • 7
    • 31044436627 scopus 로고    scopus 로고
    • A glutathione S-transferase pi-activated prodrug causes kinase activation concurrent with S-glutathionylation of proteins
    • Three studies that identified glutathionylated proteins by redox proteomics using different techniques for their detection.
    • 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. Three studies that identified glutathionylated proteins by redox proteomics using different techniques for their detection.
    • (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
  • 8
    • 22044445670 scopus 로고    scopus 로고
    • Thiol-disulfide balance: from the concept of oxidative stress to that of redox regulation
    • Ghezzi P., Bonetto V., and Fratelli M. Thiol-disulfide balance: from the concept of oxidative stress to that of redox regulation. Antioxid Redox Signal 7 (2005) 964-972
    • (2005) Antioxid Redox Signal , vol.7 , pp. 964-972
    • Ghezzi, P.1    Bonetto, V.2    Fratelli, M.3
  • 10
    • 0000189906 scopus 로고
    • Relative nucleophilic reactivities of amino groups and mercaptide ions in addition reactions with α,β-unsaturated compounds
    • Friedman M., Cavins J.F., and Wall J.P. Relative nucleophilic reactivities of amino groups and mercaptide ions in addition reactions with α,β-unsaturated compounds. J Am Chem Soc 87 (1965) 3672-3682
    • (1965) J Am Chem Soc , vol.87 , pp. 3672-3682
    • Friedman, M.1    Cavins, J.F.2    Wall, J.P.3
  • 11
    • 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
  • 12
    • 0023084124 scopus 로고
    • Formation of disulfides with diamide
    • Kosower N.S., and Kosower E.M. Formation of disulfides with diamide. Methods Enzymol 143 (1987) 264-270
    • (1987) Methods Enzymol , vol.143 , pp. 264-270
    • Kosower, N.S.1    Kosower, E.M.2
  • 14
    • 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
  • 15
    • 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
  • 16
    • 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 Y.C., Ashraf S.S., Rokutan K., Johnston Jr. R.B., and Thomas J.A. 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 310 (1994) 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
  • 17
    • 0242352426 scopus 로고    scopus 로고
    • Actin S-glutathionylation: evidence against a thiol-disulphide exchange mechanism
    • Dalle-Donne I., Rossi R., Giustarini D., Colombo R., and Milzani A. Actin S-glutathionylation: evidence against a thiol-disulphide exchange mechanism. Free Radic Biol Med 35 (2003) 1185-1193
    • (2003) Free Radic Biol Med , vol.35 , pp. 1185-1193
    • Dalle-Donne, I.1    Rossi, R.2    Giustarini, D.3    Colombo, R.4    Milzani, A.5
  • 18
    • 0024393963 scopus 로고
    • Thioredoxin and glutaredoxin systems
    • Holmgren A. Thioredoxin and glutaredoxin systems. J Biol Chem 264 (1989) 13963-13966
    • (1989) J Biol Chem , vol.264 , pp. 13963-13966
    • Holmgren, A.1
  • 19
    • 33746111275 scopus 로고    scopus 로고
    • A novel role for human sulfiredoxin in the reversal of glutathionylation
    • This work describes a new de-glutathionylating enzyme.
    • 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 work describes a new de-glutathionylating enzyme.
    • (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
  • 21
    • 0033972054 scopus 로고    scopus 로고
    • On the functional interchangeability, oxidant versus reductant, of members of the thioredoxin superfamily
    • Debarbieux L., and Beckwith J. On the functional interchangeability, oxidant versus reductant, of members of the thioredoxin superfamily. J Bacteriol 182 (2000) 723-727
    • (2000) J Bacteriol , vol.182 , pp. 723-727
    • Debarbieux, L.1    Beckwith, J.2
  • 22
    • 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 A.C., and Holmgren A. Relative contributions of thioltransferase- and thioredoxin-dependent systems in reduction of low-molecular-mass and protein disulphides. Biochem J 213 (1983) 519-523
    • (1983) Biochem J , vol.213 , pp. 519-523
    • Mannervik, B.1    Axelsson, K.2    Sundewall, A.C.3    Holmgren, A.4
  • 23
    • 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
  • 24
    • 33846809031 scopus 로고    scopus 로고
    • Glutathiolation regulates tumor necrosis factor-alpha-induced caspase-3 cleavage and apoptosis: key role for glutaredoxin in the death pathway
    • A key paper showing how glutathionylation can regulate apoptosis by modulating caspase 3.
    • Pan S., and Berk B.C. Glutathiolation regulates tumor necrosis factor-alpha-induced caspase-3 cleavage and apoptosis: key role for glutaredoxin in the death pathway. Circ Res 100 (2007) 213-219. A key paper showing how glutathionylation can regulate apoptosis by modulating caspase 3.
    • (2007) Circ Res , vol.100 , pp. 213-219
    • Pan, S.1    Berk, B.C.2
  • 25
    • 33751181030 scopus 로고    scopus 로고
    • On the potential of thioredoxin reductase inhibitors for cancer therapy
    • Urig S., and Becker K. On the potential of thioredoxin reductase inhibitors for cancer therapy. Semin Cancer Biol 16 (2006) 452-465
    • (2006) Semin Cancer Biol , vol.16 , pp. 452-465
    • Urig, S.1    Becker, K.2
  • 26
    • 33749005947 scopus 로고    scopus 로고
    • The thiol-based redox networks of pathogens: unexploited targets in the search for new drugs
    • Two reviews providing examples of the pharmacological interest of protein disulfide oxidoreductase inhibitors.
    • Jaeger T., and Flohe L. The thiol-based redox networks of pathogens: unexploited targets in the search for new drugs. Biofactors 27 (2006) 109-120. Two reviews providing examples of the pharmacological interest of protein disulfide oxidoreductase inhibitors.
    • (2006) Biofactors , vol.27 , pp. 109-120
    • Jaeger, T.1    Flohe, L.2
  • 27
    • 24644499053 scopus 로고    scopus 로고
    • Modulating sarco(endo)plasmic reticulum Ca2+ ATPase 2 (SERCA2) activity: cell biological implications
    • Vangheluwe P., Raeymaekers L., Dode L., and Wuytack F. Modulating sarco(endo)plasmic reticulum Ca2+ ATPase 2 (SERCA2) activity: cell biological implications. Cell Calcium 38 (2005) 291-302
    • (2005) Cell Calcium , vol.38 , pp. 291-302
    • Vangheluwe, P.1    Raeymaekers, L.2    Dode, L.3    Wuytack, F.4
  • 29
    • 25444491515 scopus 로고    scopus 로고
    • Gene expression profiling reveals a signaling role of glutathione in redox regulation
    • Two studies showing the key role of GSH in regulating gene expression.
    • Fratelli M., Goodwin L.O., Orom U.A., Lombardi S., Tonelli R., Mengozzi M., and Ghezzi P. Gene expression profiling reveals a signaling role of glutathione in redox regulation. Proc Natl Acad Sci USA 102 (2005) 13998-14003. Two studies showing the key role of GSH in regulating gene expression.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 13998-14003
    • Fratelli, M.1    Goodwin, L.O.2    Orom, U.A.3    Lombardi, S.4    Tonelli, R.5    Mengozzi, M.6    Ghezzi, P.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.