메뉴 건너뛰기




Volumn 105, Issue 1, 1997, Pages 17-34

Modulation of glutathione conjugation in vivo: How to decrease glutathione conjugation in vivo or in intact cellular systems in vitro

Author keywords

[No Author keywords available]

Indexed keywords

1,2 DIBROMOETHANE; BUTHIONINE SULFOXIMINE; ENZYME INHIBITOR; ETACRYNIC ACID; GLUTATHIONE; GLUTATHIONE DERIVATIVE; GLUTATHIONE TRANSFERASE; MALEIC ACID DIETHYL ESTER; TIENILIC ACID;

EID: 0030789626     PISSN: 00092797     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0009-2797(97)00038-0     Document Type: Article
Times cited : (60)

References (85)
  • 1
    • 0021778327 scopus 로고
    • The isoenzymes of glutathione transferase
    • Mannervik B. The isoenzymes of glutathione transferase. Adv. Enzymol. 57:1985;357-417.
    • (1985) Adv. Enzymol. , vol.57 , pp. 357-417
    • Mannervik, B.1
  • 2
    • 0002333139 scopus 로고
    • Glutathione Conjugation
    • in: G.J. Mulder (Ed.), Taylor and Francis, London
    • B. Ketterer, G.J. Mulder, Glutathione Conjugation, in: G.J. Mulder (Ed.), Conjugation Reactions in Drug Metabolism, Taylor and Francis, London, 1990, pp. 307-364.
    • (1990) Conjugation Reactions in Drug Metabolism , pp. 307-364
    • Ketterer, B.1    Mulder, G.J.2
  • 3
    • 0029008428 scopus 로고
    • Enzymes and transport systems involved in the formation and disposition of glutathione S-conjugates
    • Commandeur J.N.M., Stijntjes G.J., Vermeulen N.P.E. Enzymes and transport systems involved in the formation and disposition of glutathione S-conjugates. Pharmacol. Revs. 47:1995;271-330.
    • (1995) Pharmacol. Revs. , vol.47 , pp. 271-330
    • Commandeur, J.N.M.1    Stijntjes, G.J.2    Vermeulen, N.P.E.3
  • 4
    • 0029561598 scopus 로고
    • The glutathione S-transferase supergene family: Regulation of GST and the contribution of the isoenzymes to cancer chemoprevention and drug resistance
    • Hayes J.D., Pulford D.J. The glutathione S-transferase supergene family: regulation of GST and the contribution of the isoenzymes to cancer chemoprevention and drug resistance. Crit. Revs Biochem. Mol. Biol. 30:1995;445-600.
    • (1995) Crit. Revs Biochem. Mol. Biol. , vol.30 , pp. 445-600
    • Hayes, J.D.1    Pulford, D.J.2
  • 5
    • 0028106016 scopus 로고
    • Glutathione-associated enzymes in anticancer drug resistance
    • Tew K.D. Glutathione-associated enzymes in anticancer drug resistance. Cancer Res. 54:1994;4313-4320.
    • (1994) Cancer Res. , vol.54 , pp. 4313-4320
    • Tew, K.D.1
  • 8
    • 0024269217 scopus 로고
    • Glutathione transferases-structure and catalytic activity
    • Mannervik B., Danielson U.H. Glutathione transferases-structure and catalytic activity. CRC Crit. Revs Biochem. 23:1988;283-337.
    • (1988) CRC Crit. Revs Biochem. , vol.23 , pp. 283-337
    • Mannervik, B.1    Danielson, U.H.2
  • 9
    • 0022657003 scopus 로고
    • Inhibition of hepatic and extrahepatic glutathione S-transferases by primary and secondary bile acids
    • Hayes J.D., Mantle T.J. Inhibition of hepatic and extrahepatic glutathione S-transferases by primary and secondary bile acids. Biochem. J. 233:1986;407-415.
    • (1986) Biochem. J. , vol.233 , pp. 407-415
    • Hayes, J.D.1    Mantle, T.J.2
  • 10
    • 0023195326 scopus 로고
    • Inhibition of human cationic glutathione S-transferase by nonsubstrate ligands
    • Boyer T.D., Vessey D.A. Inhibition of human cationic glutathione S-transferase by nonsubstrate ligands. Hepatology. 7:1987;843-848.
    • (1987) Hepatology , vol.7 , pp. 843-848
    • Boyer, T.D.1    Vessey, D.A.2
  • 12
    • 0028303457 scopus 로고
    • Inhibitory effects of plant polyphenols on rat liver glutathione S-transferases
    • Zhang K., Das N.P. Inhibitory effects of plant polyphenols on rat liver glutathione S-transferases. Biochem. Pharmacol. 47:1994;2063-2068.
    • (1994) Biochem. Pharmacol. , vol.47 , pp. 2063-2068
    • Zhang, K.1    Das, N.P.2
  • 13
    • 0024437208 scopus 로고
    • Activity of rat liver microsomal glutathione transferase toward products of lipid peroxidation and studies of the effect of inhibitors on glutathione-dependent protection against lipid peroxidation
    • Mosialou E., Morgenstern R. Activity of rat liver microsomal glutathione transferase toward products of lipid peroxidation and studies of the effect of inhibitors on glutathione-dependent protection against lipid peroxidation. Arch. Biochem. Biophys. 275:1989;289-294.
    • (1989) Arch. Biochem. Biophys. , vol.275 , pp. 289-294
    • Mosialou, E.1    Morgenstern, R.2
  • 14
    • 0028036292 scopus 로고
    • Detoxication of base propenals and other α,β-unsaturated aldehyde products of radical reactions and lipid peroxidation by human glutathione transferases
    • Berhane K., Widersten M., Engstrom A., Kozarich W., Mannervik B. Detoxication of base propenals and other α,β-unsaturated aldehyde products of radical reactions and lipid peroxidation by human glutathione transferases. Proc. Natl. Acad. Sci. 91:1994;1480-1484.
    • (1994) Proc. Natl. Acad. Sci. , vol.91 , pp. 1480-1484
    • Berhane, K.1    Widersten, M.2    Engstrom, A.3    Kozarich, W.4    Mannervik, B.5
  • 15
    • 0022525950 scopus 로고
    • Inhibition of rat liver glutathione S-tansferases by glutathione conjugates and corresponding L-cysteines and mercapturic acids
    • K Ong L., Clark A.C. Inhibition of rat liver glutathione S-tansferases by glutathione conjugates and corresponding L-cysteines and mercapturic acids. Biochem. Pharmacol. 35:1986;651-654.
    • (1986) Biochem. Pharmacol. , vol.35 , pp. 651-654
    • K. Ong, L.1    Clark, A.C.2
  • 16
    • 0023767510 scopus 로고
    • Inhibition of glutathione S-transferases from rat liver by S-nitroso-L-glutathione
    • Clark A.G., Debnam P. Inhibition of glutathione S-transferases from rat liver by S-nitroso-L-glutathione. Biochem. Pharmacol. 37:1988;3199-3201.
    • (1988) Biochem. Pharmacol. , vol.37 , pp. 3199-3201
    • Clark, A.G.1    Debnam, P.2
  • 18
    • 0028131953 scopus 로고
    • Active-site tyrosyl residues are targets in the irreversible inhibition of a class mu glutathione transferase by 2-(S-glutathionyl)-3,5,6-trichloro-1,4-benzoquinone
    • Ploemen J.H.T.M., Johnson W.W., Jesperson S., Vanderwall D., van Ommen B., van der Greef J., van Bladeren P.J., Armstrong R.N. Active-site tyrosyl residues are targets in the irreversible inhibition of a class mu glutathione transferase by 2-(S-glutathionyl)-3,5,6-trichloro-1,4-benzoquinone. J. Biol. Chem. 269:1994;26890-26897.
    • (1994) J. Biol. Chem. , vol.269 , pp. 26890-26897
    • Ploemen, J.H.T.M.1    Johnson, W.W.2    Jesperson, S.3    Vanderwall, D.4    Van Ommen, B.5    Van Der Greef, J.6    Van Bladeren, P.J.7    Armstrong, R.N.8
  • 19
    • 0026757472 scopus 로고
    • Investigation of te active site of human placenta glutathione transferase π by means of spin-labelled glutathione analogue
    • Cacurri A.M., Polizio F., Peimonte F., Tagliatesta P., Frederici G., Desideri A. Investigation of te active site of human placenta glutathione transferase π by means of spin-labelled glutathione analogue. Biochim. Biophys. Acta. 1122:1992;265-268.
    • (1992) Biochim. Biophys. Acta , vol.1122 , pp. 265-268
    • Cacurri, A.M.1    Polizio, F.2    Peimonte, F.3    Tagliatesta, P.4    Frederici, G.5    Desideri, A.6
  • 20
    • 0025150771 scopus 로고
    • Inhibition of rat and human glutathione S-transferase isoenzymes by ethacrynic acid and its glutathione conjugate
    • Ploemen J.H.T.M., van Ommen B., van Bladeren P.J. Inhibition of rat and human glutathione S-transferase isoenzymes by ethacrynic acid and its glutathione conjugate. Biochem. Pharmacol. 40:1990;1631-1635.
    • (1990) Biochem. Pharmacol. , vol.40 , pp. 1631-1635
    • Ploemen, J.H.T.M.1    Van Ommen, B.2    Van Bladeren, P.J.3
  • 21
    • 0025860039 scopus 로고
    • Irreversible inhibtion of human glutathione S-transferase isoenzymes by tetrachloro-1,4-benzoquinone and its glutathione conjugate
    • Ploemen J.H.T.M., van Ommen B., van Bladeren P.J. Irreversible inhibtion of human glutathione S-transferase isoenzymes by tetrachloro-1,4-benzoquinone and its glutathione conjugate. Biochem. Pharmacol. 41:1991;1665-1669.
    • (1991) Biochem. Pharmacol. , vol.41 , pp. 1665-1669
    • Ploemen, J.H.T.M.1    Van Ommen, B.2    Van Bladeren, P.J.3
  • 23
    • 0026320285 scopus 로고
    • S-(4-bromo-2, 3-dioxobutyl)glutathione: A new affinity label for the 4-4 isoenzyme of rate liver glutathione S-transferase
    • Katusz R.M., Colman R.F. S-(4-bromo-2, 3-dioxobutyl)glutathione: a new affinity label for the 4-4 isoenzyme of rate liver glutathione S-transferase. Biochemistry. 30:1991;11230-11238.
    • (1991) Biochemistry , vol.30 , pp. 11230-11238
    • Katusz, R.M.1    Colman, R.F.2
  • 24
    • 0026611616 scopus 로고
    • 111 of glutathione S-transferase, isoenzyme 1-1, by S-(4-bromo-2,3-dioxobutyl)glutathione
    • 111 of glutathione S-transferase, isoenzyme 1-1, by S-(4-bromo-2,3-dioxobutyl)glutathione. Biochemistry. 31:1992;8984-8990.
    • (1992) Biochemistry , vol.31 , pp. 8984-8990
    • Katusz, R.M.1    Bono, B.2    Colman, R.F.3
  • 25
    • 0025741192 scopus 로고
    • Inhibition of glutathione S-transferase 3-3 by glutathione derivatives that bind covalently to the active site
    • Adang A.E.P., Moree W.J., Brussee J., Mulder G.J., van der Gen A. Inhibition of glutathione S-transferase 3-3 by glutathione derivatives that bind covalently to the active site. Biochem J. 278:1991;63-68.
    • (1991) Biochem J. , vol.278 , pp. 63-68
    • Adang, A.E.P.1    Moree, W.J.2    Brussee, J.3    Mulder, G.J.4    Van Der Gen, A.5
  • 26
    • 0027535813 scopus 로고
    • Isoenzyme selective irreversible inhibition of rat and human glutathione S-transferases by ethacrynic acid and two brominated derivatives
    • Ploemen J.H.T.M., Boogaards J.J.P., Veldink G.A., van Ommen B., Jansen D.H.M., van Bladeren P.J. Isoenzyme selective irreversible inhibition of rat and human glutathione S-transferases by ethacrynic acid and two brominated derivatives. Biochem. Pharmacol. 45:1993;633-639.
    • (1993) Biochem. Pharmacol. , vol.45 , pp. 633-639
    • Ploemen, J.H.T.M.1    Boogaards, J.J.P.2    Veldink, G.A.3    Van Ommen, B.4    Jansen, D.H.M.5    Van Bladeren, P.J.6
  • 27
    • 0029808204 scopus 로고    scopus 로고
    • Haloenol lactone is a new isoenzyme-selective and active site-directed inactivator of glutathione S-transferase
    • Zheng J., Mitchell A.E., Jones A.D., Hammock B.D. Haloenol lactone is a new isoenzyme-selective and active site-directed inactivator of glutathione S-transferase. J. Biol. Chem. 271:1996;20421-20425.
    • (1996) J. Biol. Chem. , vol.271 , pp. 20421-20425
    • Zheng, J.1    Mitchell, A.E.2    Jones, A.D.3    Hammock, B.D.4
  • 28
    • 0026057780 scopus 로고
    • Inhibition of rat liver glutathione S-transferase isoenzymes by peptides stabilized against degradation by γ-glutamyltranspeptidase
    • Adang A.E.P., Brussee J., van der Gen A., Mulder G.J. Inhibition of rat liver glutathione S-transferase isoenzymes by peptides stabilized against degradation by γ-glutamyltranspeptidase. J. Biol. Chem. 266:1991;830-836.
    • (1991) J. Biol. Chem. , vol.266 , pp. 830-836
    • Adang, A.E.P.1    Brussee, J.2    Van Der Gen, A.3    Mulder, G.J.4
  • 29
    • 0023687171 scopus 로고
    • Substrate specificity of rat liver glutathione S-transferase isoenzymes for a series of glutathione analogues, modified at the γ-glutamyl moiety
    • Adang A.E.P., Brussee J., Meyer D.J., Coles B., Ketterer B., van der Gen A., Mulder G.J. Substrate specificity of rat liver glutathione S-transferase isoenzymes for a series of glutathione analogues, modified at the γ-glutamyl moiety. Biochem J. 255:1988;721-724.
    • (1988) Biochem J. , vol.255 , pp. 721-724
    • Adang, A.E.P.1    Brussee, J.2    Meyer, D.J.3    Coles, B.4    Ketterer, B.5    Van Der Gen, A.6    Mulder, G.J.7
  • 30
    • 0024848271 scopus 로고
    • Interaction of rat glutathione S-transferases 7-7 and 8-8 with γ glutamyl or glycyl-modified glutathione analogues
    • Adang A.E.P., Meyer D.J., Brussee J., van der Gen A., Ketterer B., Mulder G.J. Interaction of rat glutathione S-transferases 7-7 and 8-8 with γ glutamyl or glycyl-modified glutathione analogues. Biochem J. 264:1989;759-764.
    • (1989) Biochem J. , vol.264 , pp. 759-764
    • Adang, A.E.P.1    Meyer, D.J.2    Brussee, J.3    Van Der Gen, A.4    Ketterer, B.5    Mulder, G.J.6
  • 31
    • 0025340142 scopus 로고
    • The glutathione binding site in glutathione S-transferases: Investigation of the cysteinyl, glycyl and γ-glutamyl domains
    • Adang A.E.P., Brussee J., van der Gen A., Mulder G.J. The glutathione binding site in glutathione S-transferases: investigation of the cysteinyl, glycyl and γ-glutamyl domains. Biochem. J. 269:1990;47-54.
    • (1990) Biochem. J. , vol.269 , pp. 47-54
    • Adang, A.E.P.1    Brussee, J.2    Van Der Gen, A.3    Mulder, G.J.4
  • 34
    • 0030065613 scopus 로고    scopus 로고
    • Isozyme specific glutathione S-transferase inhibitors potentiate drug sensitivity in cultured human tumor cell lines
    • Morgan A.S., Ciaccio P.J., Tew K.D., Kauvar L.M. Isozyme specific glutathione S-transferase inhibitors potentiate drug sensitivity in cultured human tumor cell lines. Cancer Chemother. Pharmacol. 37:1996;363-370.
    • (1996) Cancer Chemother. Pharmacol. , vol.37 , pp. 363-370
    • Morgan, A.S.1    Ciaccio, P.J.2    Tew, K.D.3    Kauvar, L.M.4
  • 35
    • 0028989705 scopus 로고
    • Glutathione analogues as novel inhibitors of rat and human glutathione S-transferase isoenzymes, as well as of glutathione conjugation in isolated rat hepatocytes and the rat in vivo
    • Ouwerkerk-Mahadevan S., van Boom J.H., Dreef-Tromp M.C., Ploemen J.H.T.M., Meyer D.J., Mulder G.J. Glutathione analogues as novel inhibitors of rat and human glutathione S-transferase isoenzymes, as well as of glutathione conjugation in isolated rat hepatocytes and the rat in vivo. Biochem J. 308:1995;283-290.
    • (1995) Biochem J. , vol.308 , pp. 283-290
    • Ouwerkerk-Mahadevan, S.1    Van Boom, J.H.2    Dreef-Tromp, M.C.3    Ploemen, J.H.T.M.4    Meyer, D.J.5    Mulder, G.J.6
  • 36
    • 0030098240 scopus 로고    scopus 로고
    • Isoenzyme-selective inhibition of glutathione conjugation in vivo: Selective inhibition of the conjugation of S-2- bromoisovalerylurea in the rat
    • Ouwerkerk-Mahadevan S., van Boom J.H., Mulder G.J. Isoenzyme-selective inhibition of glutathione conjugation in vivo: selective inhibition of the conjugation of S-2- bromoisovalerylurea in the rat. J. Pharmacol. Exp. Therap. 276:1996;923-928.
    • (1996) J. Pharmacol. Exp. Therap. , vol.276 , pp. 923-928
    • Ouwerkerk-Mahadevan, S.1    Van Boom, J.H.2    Mulder, G.J.3
  • 37
    • 0343989809 scopus 로고    scopus 로고
    • h.D. Thesis, Leiden University
    • S. Ouwerkerk-Mahadevan, Ph.D. Thesis, Leiden University, 1997.
    • (1997)
    • Ouwerkerk-Mahadevan, S.1
  • 38
    • 0025002201 scopus 로고
    • Inhibition and recognition studies on the glutathione-binding site of equine liver glutathione S- transferase
    • D'Silva C. Inhibition and recognition studies on the glutathione-binding site of equine liver glutathione S- transferase. Biochem. J. 271:1990;161-165.
    • (1990) Biochem. J. , vol.271 , pp. 161-165
    • D'Silva, C.1
  • 39
    • 0028209437 scopus 로고
    • Reversible conjugation of ethacrynic acid with glutathione and human glutathione S-transferase P1-1
    • Ploemen J.H.T.M., van Schanke A., van Ommen B., van Bladeren P.J. Reversible conjugation of ethacrynic acid with glutathione and human glutathione S-transferase P1-1. Cancer Res. 54:1994;915-919.
    • (1994) Cancer Res. , vol.54 , pp. 915-919
    • Ploemen, J.H.T.M.1    Van Schanke, A.2    Van Ommen, B.3    Van Bladeren, P.J.4
  • 40
    • 0026481066 scopus 로고
    • Inhibition of human hepatic glutathione S-transferase isozymes by ethacrynic acid and its metabolites
    • Takamatsu Y., Inaba T. Inhibition of human hepatic glutathione S-transferase isozymes by ethacrynic acid and its metabolites. Toxicology Letters. 62:1992;241-245.
    • (1992) Toxicology Letters , vol.62 , pp. 241-245
    • Takamatsu, Y.1    Inaba, T.2
  • 42
    • 0023679751 scopus 로고
    • Ethacrynic acid and piriprost as enhancers of cytotoxicity in drug resistant and sensitive cell lines
    • Tew K.D., Bomber A.M., Hoffmann S.J. Ethacrynic acid and piriprost as enhancers of cytotoxicity in drug resistant and sensitive cell lines. Cancer Res. 48:1988;3622-3625.
    • (1988) Cancer Res. , vol.48 , pp. 3622-3625
    • Tew, K.D.1    Bomber, A.M.2    Hoffmann, S.J.3
  • 43
    • 0002576373 scopus 로고
    • Sensitization of human colon tumor xenografts to L-phenylalanine mustard using ethacrynic acid
    • Clapper M.L., Hoffmann S.J., Tew K.D. Sensitization of human colon tumor xenografts to L-phenylalanine mustard using ethacrynic acid. J. Cell Pharmacol. 1:1990;71-78.
    • (1990) J. Cell Pharmacol. , vol.1 , pp. 71-78
    • Clapper, M.L.1    Hoffmann, S.J.2    Tew, K.D.3
  • 44
    • 0026027666 scopus 로고
    • Sensitization of human melanoma cells to the cytotoxic effect of melphalan by the glutathione transferase inhibitor ethacrynic acid
    • Hansson J., Berhane K., Castro V.M., Jungnelius U., Mannervik B., Ringsborg U. Sensitization of human melanoma cells to the cytotoxic effect of melphalan by the glutathione transferase inhibitor ethacrynic acid. Cancer Res. 51:1991;94-98.
    • (1991) Cancer Res. , vol.51 , pp. 94-98
    • Hansson, J.1    Berhane, K.2    Castro, V.M.3    Jungnelius, U.4    Mannervik, B.5    Ringsborg, U.6
  • 46
    • 0002576373 scopus 로고
    • Sensitization of human colon xenografts to L-phenylalanine mustard using ethacrynic acid
    • Clapper M.L., Hofman S.J., D Tew K. Sensitization of human colon xenografts to L-phenylalanine mustard using ethacrynic acid. J. Cell Pharmacol. 1:1990;71-78.
    • (1990) J. Cell Pharmacol. , vol.1 , pp. 71-78
    • Clapper, M.L.1    Hofman, S.J.2    D. Tew, K.3
  • 47
    • 0028801402 scopus 로고
    • Modulation of detoxification gene expression in human colon HT29 cells by glutathione-S-transferase inhibitors
    • Ciaccio P.J., Shien H., Jaiswal A.K., Lyttle M.H., Tew K.D. Modulation of detoxification gene expression in human colon HT29 cells by glutathione-S-transferase inhibitors. Mol.Pharmacol. 48:1995;639-647.
    • (1995) Mol.Pharmacol. , vol.48 , pp. 639-647
    • Ciaccio, P.J.1    Shien, H.2    Jaiswal, A.K.3    Lyttle, M.H.4    Tew, K.D.5
  • 48
    • 0030001907 scopus 로고    scopus 로고
    • Effects of chronic ethacrynic acid exposure on glutathione conjugation and MRP expression in human colon tumor cells
    • Ciaccio P.J., Sie H., Kruh G.D., Tew K.D. Effects of chronic ethacrynic acid exposure on glutathione conjugation and MRP expression in human colon tumor cells. Biochem. Biophys. Res. Commun. 222:1996;111-115.
    • (1996) Biochem. Biophys. Res. Commun. , vol.222 , pp. 111-115
    • Ciaccio, P.J.1    Sie, H.2    Kruh, G.D.3    Tew, K.D.4
  • 49
    • 0026548495 scopus 로고
    • Increased levels of glutathione-S-transferase Pi transcript as a mechanism of resistance to ethacrynic acid
    • Kuzmich S., van der Veer L.A., Walsh E.S., LaCreta F.P., Tew K.D. Increased levels of glutathione-S-transferase Pi transcript as a mechanism of resistance to ethacrynic acid. Biochem. J. 281:1992;219-224.
    • (1992) Biochem. J. , vol.281 , pp. 219-224
    • Kuzmich, S.1    Van Der Veer, L.A.2    Walsh, E.S.3    Lacreta, F.P.4    Tew, K.D.5
  • 50
  • 51
    • 0018146999 scopus 로고
    • The effect of phenobarbital, probenicid and diethylmaleate on the pharmacokinetics and biliary excretion of ethacrynic acid in the rat
    • Wallin J.D., Clifton G., Kaplowitz N. The effect of phenobarbital, probenicid and diethylmaleate on the pharmacokinetics and biliary excretion of ethacrynic acid in the rat. J. Pharmacol. exp. Therap. 205:1978;471-476.
    • (1978) J. Pharmacol. Exp. Therap. , vol.205 , pp. 471-476
    • Wallin, J.D.1    Clifton, G.2    Kaplowitz, N.3
  • 53
    • 0024495410 scopus 로고
    • Effect of the glutathione S-transferase inhibitor, tienilic acid, on biliary excretion of sulphobromophthalein
    • Fehring S.I., Ahokas J.T. Effect of the glutathione S-transferase inhibitor, tienilic acid, on biliary excretion of sulphobromophthalein. Chem.-Biol. Interactions. 69:1989;23-32.
    • (1989) Chem.-Biol. Interactions , vol.69 , pp. 23-32
    • Fehring, S.I.1    Ahokas, J.T.2
  • 55
    • 0014768820 scopus 로고
    • The effect of some carbonyl compounds on rat liver glutathione levels
    • Boyland E., Chasseaud L.F. The effect of some carbonyl compounds on rat liver glutathione levels. Biochem. Pharmacol. 19:1970;1526-1528.
    • (1970) Biochem. Pharmacol. , vol.19 , pp. 1526-1528
    • Boyland, E.1    Chasseaud, L.F.2
  • 56
    • 0018225140 scopus 로고
    • Synergistic effects of phorone on the hepatotoxicity of bromobenzene and paracetamol in mice
    • R. van Doorn, C.M. Leijendekkers, P.T. Henderson, Synergistic effects of phorone on the hepatotoxicity of bromobenzene and paracetamol in mice, Toxicology, 11 (1978) 225-233.
    • (1978) Toxicology , vol.11 , pp. 225-233
    • Van Doorn, R.1    Leijendekkers, C.M.2    Henderson, P.T.3
  • 58
    • 0021168174 scopus 로고
    • Glutathione depletion and resynthesis in laboratory animals
    • Ecobichon D.J. Glutathione depletion and resynthesis in laboratory animals. Drug Chem. Toxicol. 7:1984;345-355.
    • (1984) Drug Chem. Toxicol. , vol.7 , pp. 345-355
    • Ecobichon, D.J.1
  • 59
    • 0026556657 scopus 로고
    • Glutathione and cystein depletion in rats and mice following acute intoxication with diethylmaleate
    • D-Gerard-Monnier S., Fougeat, Chaudriere J. Glutathione and cystein depletion in rats and mice following acute intoxication with diethylmaleate. Biochem. Pharmacol. 43:1992;451-456.
    • (1992) Biochem. Pharmacol. , vol.43 , pp. 451-456
    • D-Gerard-Monnier, S.1    Fougeat2    Chaudriere, J.3
  • 60
    • 0018168977 scopus 로고
    • Choleresis associated with metabolism and biliary excretion of diethyl maleate in the rat and the dog
    • Barnhart J.L., Combes B. Choleresis associated with metabolism and biliary excretion of diethyl maleate in the rat and the dog. J. Pharmacol. exp. Therap. 206:1978;614-623.
    • (1978) J. Pharmacol. Exp. Therap. , vol.206 , pp. 614-623
    • Barnhart, J.L.1    Combes, B.2
  • 61
    • 0018071643 scopus 로고
    • Glutathione synthesis and degradation in fetal and adult rat liver and Novikoff hepatoma
    • Wirth P.J., Thorgeirsson S.S. Glutathione synthesis and degradation in fetal and adult rat liver and Novikoff hepatoma. Cancer Res. 38:1978;2861-2865.
    • (1978) Cancer Res. , vol.38 , pp. 2861-2865
    • Wirth, P.J.1    Thorgeirsson, S.S.2
  • 62
    • 0026693485 scopus 로고
    • Relationship between glutathione content in liver and glutathione conjugation rate in the rat in vivo
    • Polhuijs M., Lankhaar G., Mulder G.J. Relationship between glutathione content in liver and glutathione conjugation rate in the rat in vivo. Biochem. J. 285:1992;401-404.
    • (1992) Biochem. J. , vol.285 , pp. 401-404
    • Polhuijs, M.1    Lankhaar, G.2    Mulder, G.J.3
  • 63
    • 0029074460 scopus 로고
    • Glutathione conjugation of bromosulfophthalein in relation to hepatic glutathione content in the rat in vivo and in the perfused rat liver
    • Snel C.A.W., Pang K.S., Mulder G.J. Glutathione conjugation of bromosulfophthalein in relation to hepatic glutathione content in the rat in vivo and in the perfused rat liver. Hepatology. 21:1995;1387-1394.
    • (1995) Hepatology , vol.21 , pp. 1387-1394
    • Snel, C.A.W.1    Pang, K.S.2    Mulder, G.J.3
  • 64
    • 0029585739 scopus 로고
    • Effect of ifosfamide treatment on glutathione and glutathione conjugation activity in patients with advanced cancers
    • Mulders T.M.T., Keizer H.J., Ouwerkerk J., van de Velde E.A., Breimer D.D., Mulder G.J. Effect of ifosfamide treatment on glutathione and glutathione conjugation activity in patients with advanced cancers. Clin. Cancer Res. 1:1995;1525-1536.
    • (1995) Clin. Cancer Res. , vol.1 , pp. 1525-1536
    • Mulders, T.M.T.1    Keizer, H.J.2    Ouwerkerk, J.3    Van De Velde, E.A.4    Breimer, D.D.5    Mulder, G.J.6
  • 66
    • 0018666729 scopus 로고
    • Potent and specific inhibition of glutathione synthesis by buthionine sulfoximine
    • Griffith O.W., Meister A. Potent and specific inhibition of glutathione synthesis by buthionine sulfoximine. J. Biol. Chem. 254:1979;1979-1982.
    • (1979) J. Biol. Chem. , vol.254 , pp. 1979-1982
    • Griffith, O.W.1    Meister, A.2
  • 67
    • 0020444895 scopus 로고
    • Mechanism of action, metabolism and toxicity of buthionine sulfoximine and its higher homologues, potent inhibitors of glutathione synthesis
    • Griffith O.W. Mechanism of action, metabolism and toxicity of buthionine sulfoximine and its higher homologues, potent inhibitors of glutathione synthesis. J. Biol. Chem. 257:1982;13704-13712.
    • (1982) J. Biol. Chem. , vol.257 , pp. 13704-13712
    • Griffith, O.W.1
  • 68
    • 0021219926 scopus 로고
    • The effect of buthionine sulfoximine on glutathione depletion and xenobiotic biotransformation
    • Drew R., Miners J.O. The effect of buthionine sulfoximine on glutathione depletion and xenobiotic biotransformation. Biochem. Pharmacol. 33:1984;2989-2994.
    • (1984) Biochem. Pharmacol. , vol.33 , pp. 2989-2994
    • Drew, R.1    Miners, J.O.2
  • 69
    • 0025668561 scopus 로고
    • Induction of rat UDP glucuronosyltransferase and glutathione S-transferase activities by L-buthionine sulfoximine without induction of cytochrome P450
    • Manning B.W., Franklin M.R. Induction of rat UDP glucuronosyltransferase and glutathione S-transferase activities by L-buthionine sulfoximine without induction of cytochrome P450. Toxicology. 65:1990;149-159.
    • (1990) Toxicology , vol.65 , pp. 149-159
    • Manning, B.W.1    Franklin, M.R.2
  • 70
  • 71
    • 0027297051 scopus 로고
    • Variable baseline gamma-glutamylcysteine synthetase messenger RNA expression in peripheral mononuclear cells of cancer patients and its induction by buthionine sulfoximine treatment
    • Yao K.S., Godwin A.K., Ozols R.F., Hamilton T.C., O'Dwyer P.J. Variable baseline gamma-glutamylcysteine synthetase messenger RNA expression in peripheral mononuclear cells of cancer patients and its induction by buthionine sulfoximine treatment. Cancer Res. 53:1993;3662-3666.
    • (1993) Cancer Res. , vol.53 , pp. 3662-3666
    • Yao, K.S.1    Godwin, A.K.2    Ozols, R.F.3    Hamilton, T.C.4    O'Dwyer, P.J.5
  • 72
    • 0029897434 scopus 로고    scopus 로고
    • Buthionine sulfoximine induction of γ-L-glutamyl-L-cysteine synthetase gene expression, kinetics of glutathione depletion and resynthesis and modulation of carmustine-induced DNA-DNA cross-linking and cytotoxicity in human glioma cells
    • Ali-Osman F., Antoun G., Wang H., Rajagopal S., Gagucas E. Buthionine sulfoximine induction of γ-L-glutamyl-L-cysteine synthetase gene expression, kinetics of glutathione depletion and resynthesis and modulation of carmustine-induced DNA-DNA cross-linking and cytotoxicity in human glioma cells. Mol. Pharmacol. 49:1996;1012-1020.
    • (1996) Mol. Pharmacol. , vol.49 , pp. 1012-1020
    • Ali-Osman, F.1    Antoun, G.2    Wang, H.3    Rajagopal, S.4    Gagucas, E.5
  • 73
    • 0029102099 scopus 로고
    • Markedly decreased expression of glutathione S-transferase Pi gene in human cancer cell lines resistant to buthionine sulfoximine, an inhibitor of cellular glutathione synthesis
    • Yokomizo A., Kohno K., Wada M., Ono M., Morrow C.S., Cowant K.H., Kuwano K.M. Markedly decreased expression of glutathione S-transferase Pi gene in human cancer cell lines resistant to buthionine sulfoximine, an inhibitor of cellular glutathione synthesis. J. Biol. Chem. 270:1995;19451-19457.
    • (1995) J. Biol. Chem. , vol.270 , pp. 19451-19457
    • Yokomizo, A.1    Kohno, K.2    Wada, M.3    Ono, M.4    Morrow, C.S.5    Cowant, K.H.6    Kuwano, K.M.7
  • 75
    • 0019765119 scopus 로고
    • Depletion of glutathione by inhibition of biosynthesis
    • Griffith O.W. Depletion of glutathione by inhibition of biosynthesis. Meth. Enzymol. 77:1981;59-63.
    • (1981) Meth. Enzymol. , vol.77 , pp. 59-63
    • Griffith, O.W.1
  • 76
    • 0022374850 scopus 로고
    • Effects of the long-term depletion of reduced glutathione in mice administered L-buthionine-S R-sulfoximine.
    • Sun J.D., Ragsdale S.S., Benson J.M., Henderson R.F. Effects of the long-term depletion of reduced glutathione in mice administered L-buthionine-S R-sulfoximine. Fund. Appl. Toxicol. 5:1985;913-919.
    • (1985) Fund. Appl. Toxicol. , vol.5 , pp. 913-919
    • Sun, J.D.1    Ragsdale, S.S.2    Benson, J.M.3    Henderson, R.F.4
  • 77
    • 0023119841 scopus 로고
    • Enhanced melphalan cytotoxicity in human ovarian cancer in vitro and in tumor-bearing nude mice by buthionine sulfoximine depletion of glutathione
    • Ozols R.F., Louie K.G., Plowman J., Behrens B.C., Fine R.L., Dykes D., Hamilton T.C. Enhanced melphalan cytotoxicity in human ovarian cancer in vitro and in tumor-bearing nude mice by buthionine sulfoximine depletion of glutathione. Biochem. Pharmacol. 36:1987;147-153.
    • (1987) Biochem. Pharmacol. , vol.36 , pp. 147-153
    • Ozols, R.F.1    Louie, K.G.2    Plowman, J.3    Behrens, B.C.4    Fine, R.L.5    Dykes, D.6    Hamilton, T.C.7
  • 80
    • 0342683551 scopus 로고
    • Continuous infusion of buthionine sulfoximine and melphalan produces depletion of tumor glutathione to less than 10% of baseline in patients undergoing phase I treatment
    • Bailey H.T., Mulcahy R.T., Ripple R.T., Tutsch K.P., Arzoomanian R.Z., Alberti D., Feierabend C., Mahvi D., Wilding G. Continuous infusion of buthionine sulfoximine and melphalan produces depletion of tumor glutathione to less than 10% of baseline in patients undergoing phase I treatment. Proc. ASCO. 14:1995;181.
    • (1995) Proc. ASCO , vol.14 , pp. 181
    • Bailey, H.T.1    Mulcahy, R.T.2    Ripple, R.T.3    Tutsch, K.P.4    Arzoomanian, R.Z.5    Alberti, D.6    Feierabend, C.7    Mahvi, D.8    Wilding, G.9
  • 83
    • 0028892242 scopus 로고
    • Time dependent pharmacokinetic models in cancer chemotherapy: Population pharmacodynamic model for glutathione depeltion following modulation by buthionine sulfoximine in a phase I trial of melphalan and BSO
    • Gallo J.M., Brennan J., Hamilton T.C., Halbherr T., Laub P.B., Ozols R.F., O'Dwyer P.J. Time dependent pharmacokinetic models in cancer chemotherapy: population pharmacodynamic model for glutathione depeltion following modulation by buthionine sulfoximine in a phase I trial of melphalan and BSO. Cancer Res. 55:1995;4507-4511.
    • (1995) Cancer Res. , vol.55 , pp. 4507-4511
    • Gallo, J.M.1    Brennan, J.2    Hamilton, T.C.3    Halbherr, T.4    Laub, P.B.5    Ozols, R.F.6    O'Dwyer, P.J.7
  • 84
    • 0029767940 scopus 로고    scopus 로고
    • Antitumor activity if S-(p-bromobenzyl)glutathione diesters in vitro: A structure activity study
    • Thornally P.J., Ladan M.J., Ridgway S.J.S., Kang Y. Antitumor activity if S-(p-bromobenzyl)glutathione diesters in vitro: a structure activity study. J. Med. Chem. 39:1996;3409-3411.
    • (1996) J. Med. Chem. , vol.39 , pp. 3409-3411
    • Thornally, P.J.1    Ladan, M.J.2    Ridgway, S.J.S.3    Kang, Y.4
  • 85
    • 0029680939 scopus 로고    scopus 로고
    • Transfection of glutathione S-transferase GST-P antisense complementary DNA increases the sensitivity of a colon cancer cell line to adriamycin, cisplatin, melphalan and etoposide
    • Ban N., Takahashi Y., Takayama T., Kura T., Katahira T., Sakamaki S., Niitsu Y. Transfection of glutathione S-transferase GST-P antisense complementary DNA increases the sensitivity of a colon cancer cell line to adriamycin, cisplatin, melphalan and etoposide. Cancer Res. 56:1996;3577-3582.
    • (1996) Cancer Res. , vol.56 , pp. 3577-3582
    • Ban, N.1    Takahashi, Y.2    Takayama, T.3    Kura, T.4    Katahira, T.5    Sakamaki, S.6    Niitsu, Y.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.