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Volumn 66, Issue 8, 2003, Pages 1499-1503

The changing faces of glutathione, a cellular protagonist

Author keywords

Cell regulation; Detoxication; Glutathione; Glutathione dependent enzymes; Thiols

Indexed keywords

CYSTEINE; DISULFIDE; FREE RADICAL; GAMMA GLUTAMYLTRANSFERASE; GLUTATHIONE; GLUTATHIONE PEROXIDASE; REACTIVE OXYGEN METABOLITE; THIOL; GLUTATHIONE TRANSFERASE; METAL; THIOL DERIVATIVE;

EID: 0642283965     PISSN: 00062952     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-2952(03)00504-5     Document Type: Conference Paper
Times cited : (1137)

References (46)
  • 1
    • 0033230043 scopus 로고    scopus 로고
    • Glutathione and its role in cellular functions
    • Sies H. Glutathione and its role in cellular functions. Free Radic. Biol. Med. 27:1999;916-921.
    • (1999) Free Radic. Biol. Med. , vol.27 , pp. 916-921
    • Sies, H.1
  • 2
    • 0032874845 scopus 로고    scopus 로고
    • Glutathione and glutathione-dependent enzymes represent a co-ordinately regulated defence against oxidative stress
    • Hayes J.D., McLellan L.I. Glutathione and glutathione-dependent enzymes represent a co-ordinately regulated defence against oxidative stress. Free Radic. Res. 31:1999;273-300.
    • (1999) Free Radic. Res. , vol.31 , pp. 273-300
    • Hayes, J.D.1    McLellan, L.I.2
  • 3
    • 0023740342 scopus 로고
    • Formation of toxic metabolites from drugs and other xenobiotics by glutathione conjugation
    • van Bladeren P.J. Formation of toxic metabolites from drugs and other xenobiotics by glutathione conjugation. Trends Pharmacol. Sci. 9:1988;295-299.
    • (1988) Trends Pharmacol. Sci. , vol.9 , pp. 295-299
    • Van Bladeren, P.J.1
  • 4
    • 0142012164 scopus 로고    scopus 로고
    • Detoxification of electrophilic compounds by glutathione S-transferase catalysis: Determinants of individual response to chemical carcinogens and chemotherapeutic drugs?
    • in press.
    • Coles B, Kadlubar F. Detoxification of electrophilic compounds by glutathione S-transferase catalysis: determinants of individual response to chemical carcinogens and chemotherapeutic drugs? Biofactors 2003, in press.
    • (2003) Biofactors
    • Coles, B.1    Kadlubar, F.2
  • 5
    • 0020325662 scopus 로고
    • Mechanisms of cell injury in the killing of cultured hepatocytes by bromobenzene
    • Casini A., Giorli M., Hyland R.J., Serroni A., Gilfor D., Farber J.L. Mechanisms of cell injury in the killing of cultured hepatocytes by bromobenzene. J. Biol. Chem. 257:1982;6721-6728.
    • (1982) J. Biol. Chem. , vol.257 , pp. 6721-6728
    • Casini, A.1    Giorli, M.2    Hyland, R.J.3    Serroni, A.4    Gilfor, D.5    Farber, J.L.6
  • 6
    • 0021953004 scopus 로고
    • Liver glutathione depletion induced by bromobenzene, iodobenzene and diethylmaleate poisoning and its relation to lipid peroxidation and necrosis
    • Casini A.F., Pompella A., Comporti M. Liver glutathione depletion induced by bromobenzene, iodobenzene and diethylmaleate poisoning and its relation to lipid peroxidation and necrosis. Am. J. Pathol. 118:1985;225-237.
    • (1985) Am. J. Pathol. , vol.118 , pp. 225-237
    • Casini, A.F.1    Pompella, A.2    Comporti, M.3
  • 7
    • 0024438921 scopus 로고
    • Three models of free radical-induced cell injury
    • Comporti M. Three models of free radical-induced cell injury. Chem.-Biol. Interact. 72:1989;1-56.
    • (1989) Chem.-Biol. Interact. , vol.72 , pp. 1-56
    • Comporti, M.1
  • 9
    • 0028176627 scopus 로고
    • Glucose-6-phosphate dehydrogenase: A "housekeeping" enzyme subject to tissue-specific regulation by hormones, nutrients, and oxidant stress
    • Kletzien R.F., Harris P.K., Foellmi L.A. Glucose-6-phosphate dehydrogenase: a "housekeeping" enzyme subject to tissue-specific regulation by hormones, nutrients, and oxidant stress. FASEB J. 8:1994;174-181.
    • (1994) FASEB J. , vol.8 , pp. 174-181
    • Kletzien, R.F.1    Harris, P.K.2    Foellmi, L.A.3
  • 10
    • 0019879698 scopus 로고
    • Human cell dehydroascorbate reductase kinetic and functional properties
    • Bigley R., Riddle M., Layman D., Stankowa L. Human cell dehydroascorbate reductase kinetic and functional properties. Biochim. Biophys. Acta. 659:1981;15-22.
    • (1981) Biochim. Biophys. Acta , vol.659 , pp. 15-22
    • Bigley, R.1    Riddle, M.2    Layman, D.3    Stankowa, L.4
  • 11
    • 0025754161 scopus 로고
    • Glutathione deficiency decreases tissue ascorbate levels in newborn rats: Ascorbate spares glutathione and protects
    • Martensson J., Meister A. Glutathione deficiency decreases tissue ascorbate levels in newborn rats: ascorbate spares glutathione and protects. Proc. Natl. Acad. Sci. U.S.A. 88:1991;4656-4660.
    • (1991) Proc. Natl. Acad. Sci. U.S.A. , vol.88 , pp. 4656-4660
    • Martensson, J.1    Meister, A.2
  • 12
    • 0018348794 scopus 로고
    • Direct observation of a free radical interaction between vitamin e and vitamin C
    • Packer J.E., Slater T.F., Willson R.L. Direct observation of a free radical interaction between vitamin E and vitamin C. Nature. 278:1979;737-738.
    • (1979) Nature , vol.278 , pp. 737-738
    • Packer, J.E.1    Slater, T.F.2    Willson, R.L.3
  • 13
    • 0021226504 scopus 로고
    • Formation of alpha-tocopherol radical and recycling of alpha-tocopherol by ascorbate during peroxidation of phosphatidylcholine liposomes. An electron paramagnetic resonance study
    • Scarpa M., Rigo T.F., Maiorino M., Ursini F., Gregolin C. Formation of alpha-tocopherol radical and recycling of alpha-tocopherol by ascorbate during peroxidation of phosphatidylcholine liposomes. An electron paramagnetic resonance study. Biochim. Biophys. Acta. 801:1984;215-219.
    • (1984) Biochim. Biophys. Acta , vol.801 , pp. 215-219
    • Scarpa, M.1    Rigo, T.F.2    Maiorino, M.3    Ursini, F.4    Gregolin, C.5
  • 14
    • 0025082330 scopus 로고
    • Mammalian thioltransferase (glutaredoxin) and protein disulfide isomerase have dehydroascorbate reductase activity
    • Wells W.W., Xu D.P., Yang Y., Rocque P.A. Mammalian thioltransferase (glutaredoxin) and protein disulfide isomerase have dehydroascorbate reductase activity. J. Biol. Chem. 265:1990;15361-15364.
    • (1990) J. Biol. Chem. , vol.265 , pp. 15361-15364
    • Wells, W.W.1    Xu, D.P.2    Yang, Y.3    Rocque, P.A.4
  • 15
    • 0033524429 scopus 로고    scopus 로고
    • The catalytic mechanism of the glutathione-dependent dehydroascorbate reductase activity of thioltransferase (glutaredoxin)
    • Washburn M.P., Wells W.W. The catalytic mechanism of the glutathione-dependent dehydroascorbate reductase activity of thioltransferase (glutaredoxin). Biochemistry. 38:1999;268-274.
    • (1999) Biochemistry , vol.38 , pp. 268-274
    • Washburn, M.P.1    Wells, W.W.2
  • 16
    • 0028015887 scopus 로고
    • Purification and characterization of glutathione-dependent dehydroascorbate reductase from rat liver
    • Maellaro E., Del Bello B., Sugherini L., Santucci A., Comporti M., Casini A.F. Purification and characterization of glutathione-dependent dehydroascorbate reductase from rat liver. Biochem. J. 301:1994;471-476.
    • (1994) Biochem. J. , vol.301 , pp. 471-476
    • Maellaro, E.1    Del Bello, B.2    Sugherini, L.3    Santucci, A.4    Comporti, M.5    Casini, A.F.6
  • 17
    • 0032582815 scopus 로고    scopus 로고
    • Molecular cloning and functional expression of rat liver glutathione-dependent dehydroascorbate reductase
    • Ishikawa T., Casini A.F., Nishikimi M. Molecular cloning and functional expression of rat liver glutathione-dependent dehydroascorbate reductase. J. Biol. Chem. 273:1998;28708-28712.
    • (1998) J. Biol. Chem. , vol.273 , pp. 28708-28712
    • Ishikawa, T.1    Casini, A.F.2    Nishikimi, M.3
  • 18
    • 0037081748 scopus 로고    scopus 로고
    • Ascorbic acid: Much more than just an antioxidant
    • Arrigoni O., De Tullio M.C. Ascorbic acid: much more than just an antioxidant. Biochim. Biophys. Acta. 1569:2002;1-9.
    • (2002) Biochim. Biophys. Acta , vol.1569 , pp. 1-9
    • Arrigoni, O.1    De Tullio, M.C.2
  • 19
    • 0032100603 scopus 로고    scopus 로고
    • Redox signaling and the emerging therapeutic potential of thiol antioxidants
    • Sen C.K. Redox signaling and the emerging therapeutic potential of thiol antioxidants. Biochem. Pharmacol. 55:1998;1747-1758.
    • (1998) Biochem. Pharmacol. , vol.55 , pp. 1747-1758
    • Sen, C.K.1
  • 20
    • 0033231351 scopus 로고    scopus 로고
    • Gene expression and the thiol redox state
    • Arrigo A.P. Gene expression and the thiol redox state. Free Radic. Biol. Med. 27:1999;936-944.
    • (1999) Free Radic. Biol. Med. , vol.27 , pp. 936-944
    • Arrigo, A.P.1
  • 21
    • 0035371184 scopus 로고    scopus 로고
    • Redox environment of the cell as viewed through the redox state of the glutathione disulfide/glutathione couple
    • Schafer F.Q., Buettner G.R. Redox environment of the cell as viewed through the redox state of the glutathione disulfide/glutathione couple. Free Radic. Biol. Med. 30:2001;1191-1212.
    • (2001) Free Radic. Biol. Med. , vol.30 , pp. 1191-1212
    • Schafer, F.Q.1    Buettner, G.R.2
  • 22
    • 0020624295 scopus 로고
    • Identification and quantitation of glutathione and its relationship to glutathione disulfide
    • Brigelius R., Muckel C., Akerboom T.P.M., Sies H. Identification and quantitation of glutathione and its relationship to glutathione disulfide. Biochem. Pharmacol. 32:1983;2529-2534.
    • (1983) Biochem. Pharmacol. , vol.32 , pp. 2529-2534
    • Brigelius, R.1    Muckel, C.2    Akerboom, T.P.M.3    Sies, H.4
  • 23
    • 0023073336 scopus 로고
    • Hormones, glutathione status and protein S-thiolation
    • Sies H., Brigelius R., Graf P. Hormones, glutathione status and protein S-thiolation. Adv. Enzyme Regul. 26:1987;175-189.
    • (1987) Adv. Enzyme Regul. , vol.26 , pp. 175-189
    • Sies, H.1    Brigelius, R.2    Graf, P.3
  • 24
    • 0021891877 scopus 로고
    • Role of reversible oxidation-reduction of thiol-disulfides in metabolic regulation
    • Ziegler D.M. Role of reversible oxidation-reduction of thiol-disulfides in metabolic regulation. Annu. Rev. Biochem. 54:1985;305-329.
    • (1985) Annu. Rev. Biochem. , vol.54 , pp. 305-329
    • Ziegler, D.M.1
  • 27
    • 0035310359 scopus 로고    scopus 로고
    • Oxidative modification of H-ras: S-thiolation and S-nitrosylation of reactive cysteines
    • Mallis R.J., Buss J.E., Thomas J.A. Oxidative modification of H-ras: S-thiolation and S-nitrosylation of reactive cysteines. Biochem. J. 355:2001;145-153.
    • (2001) Biochem. J. , vol.355 , pp. 145-153
    • Mallis, R.J.1    Buss, J.E.2    Thomas, J.A.3
  • 32
    • 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., Newcombe F.M., Starke D.W., Ott D.E., Mieyal J.J., 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    Newcombe, F.M.2    Starke, D.W.3    Ott, D.E.4    Mieyal, J.J.5    Yarchoan, R.6
  • 33
    • 0030746981 scopus 로고    scopus 로고
    • Redox state regulates binding of p53 to sequence-specific DNA, but not to non-specific or mismatched DNA
    • Parks D., Bolinger R., Mann K. Redox state regulates binding of p53 to sequence-specific DNA, but not to non-specific or mismatched DNA. Nucl. Acid Res. 25:1997;1289-1295.
    • (1997) Nucl. Acid Res. , vol.25 , pp. 1289-1295
    • Parks, D.1    Bolinger, R.2    Mann, K.3
  • 34
    • 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., 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
  • 35
    • 0025301763 scopus 로고
    • Reconstitution of Cu, Zn-superoxide dismutase by the Cu(I)-glutathione complex
    • Ciriolo M.R., Desideri A., Paci M., Rotilio G. Reconstitution of Cu, Zn-superoxide dismutase by the Cu(I)-glutathione complex. J. Biol. Chem. 265:1990;11030-11034.
    • (1990) J. Biol. Chem. , vol.265 , pp. 11030-11034
    • Ciriolo, M.R.1    Desideri, A.2    Paci, M.3    Rotilio, G.4
  • 36
    • 0019804120 scopus 로고
    • Toxic drug effects associated with oxygen metabolism: Redox cycling and lipid peroxidation
    • Kappus H., Sies H. Toxic drug effects associated with oxygen metabolism: redox cycling and lipid peroxidation. Experientia. 37:1981;1233-1241.
    • (1981) Experientia , vol.37 , pp. 1233-1241
    • Kappus, H.1    Sies, H.2
  • 39
    • 0028021850 scopus 로고
    • Thiol-mediated NTA-Fe(III) reduction and lipid peroxidation
    • Spear N., Aust S.D. Thiol-mediated NTA-Fe(III) reduction and lipid peroxidation. Arch. Biochem. Biophys. 312:1994;198-202.
    • (1994) Arch. Biochem. Biophys. , vol.312 , pp. 198-202
    • Spear, N.1    Aust, S.D.2
  • 44
    • 0032488513 scopus 로고    scopus 로고
    • Recent trends in glutathione biochemistry - Glutathione-protein interactions: A molecular link between oxidative stress and cell proliferation?
    • Cotgreave I.A., Gerdes R.G. Recent trends in glutathione biochemistry - glutathione-protein interactions: a molecular link between oxidative stress and cell proliferation? Biochim. Biophys. Res. Commun. 242:1998;1-9.
    • (1998) Biochim. Biophys. Res. Commun. , vol.242 , pp. 1-9
    • Cotgreave, I.A.1    Gerdes, R.G.2
  • 45
    • 0033953170 scopus 로고    scopus 로고
    • GSH extrusion and the mitochondrial pathway of apoptotic signalling
    • Coppola S., Ghibelli L. GSH extrusion and the mitochondrial pathway of apoptotic signalling. Biochem. Soc. Trans. 28:2000;56-61.
    • (2000) Biochem. Soc. Trans. , vol.28 , pp. 56-61
    • Coppola, S.1    Ghibelli, L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.