메뉴 건너뛰기




Volumn 43, Issue 2, 2006, Pages 143-181

Glutathione in cancer biology and therapy

Author keywords

Bcl 2; Cancer; Cell adhesion; Cell death; Endothelium; Glutathione; Invasion; Metastases; Mitochondria; Multidrug resistance proteins; Therapy

Indexed keywords

ABC TRANSPORTER; ACIVICIN; ADENINE NUCLEOTIDE TRANSLOCASE; ANTINEOPLASTIC AGENT; ANTISENSE OLIGODEOXYNUCLEOTIDE; BUTHIONINE SULFOXIMINE; DAUNORUBICIN; GLUTAMATE CYSTEINE LIGASE; GLUTATHIONE; GLUTATHIONE DISULFIDE; GLUTATHIONE PEROXIDASE; GLUTATHIONE PEROXIDASE 1; GREEN FLUORESCENT PROTEIN; MULTIDRUG RESISTANCE PROTEIN; MULTIDRUG RESISTANCE PROTEIN 1; OBLIMERSEN; PROTEIN BCL 2; RADIOSENSITIZING AGENT; TRANSMEMBRANE CONDUCTANCE REGULATOR; VASCULAR CELL ADHESION MOLECULE 1; VERAPAMIL; VERY LATE ACTIVATION ANTIGEN 4; VINCRISTINE; VOLTAGE GATED CHANNEL FORMING PROTEIN;

EID: 33744994567     PISSN: 10408363     EISSN: 1549781X     Source Type: Journal    
DOI: 10.1080/10408360500523878     Document Type: Review
Times cited : (896)

References (248)
  • 1
    • 0041495404 scopus 로고
    • Some relations between ascorbic acid and glutathione
    • Hopkins FG, Morgan EJ. Some relations between ascorbic acid and glutathione. Biochem J 1936; 30: 1446-1462.
    • (1936) Biochem J , vol.30 , pp. 1446-1462
    • Hopkins, F.G.1    Morgan, E.J.2
  • 2
    • 33745004282 scopus 로고
    • The influence of thiol-groups in the activity of dehydrogenases
    • Hopkins FG, Morgan EJ. The influence of thiol-groups in the activity of dehydrogenases. Biochem J 1938; 32: 611-620.
    • (1938) Biochem J , vol.32 , pp. 611-620
    • Hopkins, F.G.1    Morgan, E.J.2
  • 3
    • 0020537304 scopus 로고
    • Selective modification of glutathione metabolism
    • Meister A. Selective modification of glutathione metabolism. Science 1983; 220: 472-477.
    • (1983) Science , vol.220 , pp. 472-477
    • Meister, A.1
  • 4
    • 0024432603 scopus 로고
    • Regulation of cellular glutathione
    • Deneke SM, Fanburg BL. Regulation of cellular glutathione. Am J Physiol 1989; 257: L163-173.
    • (1989) Am J Physiol , vol.257
    • Deneke, S.M.1    Fanburg, B.L.2
  • 5
    • 0034068601 scopus 로고    scopus 로고
    • Mitochondrial control of cell death
    • Kroemer G, Reed JC. Mitochondrial control of cell death. Nat Med 2000; 6: 513-519.
    • (2000) Nat Med , vol.6 , pp. 513-519
    • Kroemer, G.1    Reed, J.C.2
  • 6
    • 1542376929 scopus 로고    scopus 로고
    • Glutathione metabolism and its implications for health
    • Wu G, Fang YZ, Yang S, Lupton JR, Turner ND. Glutathione metabolism and its implications for health. J Nutr 2004; 134: 489-492.
    • (2004) J Nutr , vol.134 , pp. 489-492
    • Wu, G.1    Fang, Y.Z.2    Yang, S.3    Lupton, J.R.4    Turner, N.D.5
  • 7
    • 0023260394 scopus 로고
    • Carcinogen treatment increases glutathione hydrolysis by gamma-glutamyl transpeptidase
    • Conway JG, Neptun DA, Garvey LK, Popp JA. Carcinogen treatment increases glutathione hydrolysis by gamma-glutamyl transpeptidase. Carcinogenesis 1987; 8: 999-1004.
    • (1987) Carcinogenesis , vol.8 , pp. 999-1004
    • Conway, J.G.1    Neptun, D.A.2    Garvey, L.K.3    Popp, J.A.4
  • 9
    • 0023756891 scopus 로고
    • Protective role of glutathione and glutathione transferases in mutagenesis and carcinogenesis
    • Ketterer B. Protective role of glutathione and glutathione transferases in mutagenesis and carcinogenesis. Mutat Res 1988; 202: 343-361.
    • (1988) Mutat Res , vol.202 , pp. 343-361
    • Ketterer, B.1
  • 11
    • 0033628853 scopus 로고    scopus 로고
    • Cellular mechanisms of multidrug resistance of tumor cells
    • Stavrovskaya AA. Cellular mechanisms of multidrug resistance of tumor cells. Biochemistry (Mosc) 2000; 65: 95-106.
    • (2000) Biochemistry (Mosc) , vol.65 , pp. 95-106
    • Stavrovskaya, A.A.1
  • 12
    • 0022256658 scopus 로고
    • Glutathione depletion greatly reduces neocarzinostatin cytotoxicity in Chinese hamster V79 cells
    • DeGraff WG, Russo A, Mitchell JB. Glutathione depletion greatly reduces neocarzinostatin cytotoxicity in Chinese hamster V79 cells. J Biol Chem 1985; 260: 8312-8315.
    • (1985) J Biol Chem , vol.260 , pp. 8312-8315
    • DeGraff, W.G.1    Russo, A.2    Mitchell, J.B.3
  • 13
    • 0022444380 scopus 로고
    • Glutathione depletion as a determinant of sensitivity of human leukemia cells to cyclophosphamide
    • Crook TR, Souhami RL, Whyman GD, McLean AE. Glutathione depletion as a determinant of sensitivity of human leukemia cells to cyclophosphamide. Cancer Res 1986; 46: 5035-5038.
    • (1986) Cancer Res , vol.46 , pp. 5035-5038
    • Crook, T.R.1    Souhami, R.L.2    Whyman, G.D.3    McLean, A.E.4
  • 14
    • 0023270590 scopus 로고
    • The role of glutathione in radiation and drug induced cytotoxicity
    • Mitchell JB, Russo A. The role of glutathione in radiation and drug induced cytotoxicity. Br J Cancer Suppl 1987; 8: 96-104.
    • (1987) Br J Cancer Suppl , vol.8 , pp. 96-104
    • Mitchell, J.B.1    Russo, A.2
  • 15
    • 0025302401 scopus 로고
    • Role of glutathione in the radiation response of mammalian cells in vitro and in vivo
    • Bump EA, Brown JM. Role of glutathione in the radiation response of mammalian cells in vitro and in vivo. Pharmacol Ther 1990; 47: 117-136.
    • (1990) Pharmacol Ther , vol.47 , pp. 117-136
    • Bump, E.A.1    Brown, J.M.2
  • 16
    • 0028944195 scopus 로고
    • Elimination of Ehrlich tumours by ATP-induced growth inhibition, glutathione depletion and X-rays
    • Estrela JM, Obrador E, Navarro J, Lasso De la Vega MC, Pellicer JA. Elimination of Ehrlich tumours by ATP-induced growth inhibition, glutathione depletion and X-rays. Nat Med 1995; 1: 84-88.
    • (1995) Nat Med , vol.1 , pp. 84-88
    • Estrela, J.M.1    Obrador, E.2    Navarro, J.3    Lasso De La Vega, M.C.4    Pellicer, J.A.5
  • 17
    • 18544399201 scopus 로고    scopus 로고
    • Clinical studies of reversal of drug resistance based on glutathione
    • Calvert P, Yao KS, Hamilton TC, O'Dwyer PJ. Clinical studies of reversal of drug resistance based on glutathione. Chem Biol Interact 1998; 111-112: 213-224.
    • (1998) Chem Biol Interact , vol.111-112 , pp. 213-224
    • Calvert, P.1    Yao, K.S.2    Hamilton, T.C.3    O'Dwyer, P.J.4
  • 19
    • 0035011654 scopus 로고    scopus 로고
    • Possible mechanisms for tumour cell sensitivity to TNF-alpha and potential therapeutic applications
    • Obrador E, Carretero J, Pellicer JA, Estrela JM. Possible mechanisms for tumour cell sensitivity to TNF-alpha and potential therapeutic applications. Curr Pharm Biotechnol 2001; 2: 119-30.
    • (2001) Curr Pharm Biotechnol , vol.2 , pp. 119-130
    • Obrador, E.1    Carretero, J.2    Pellicer, J.A.3    Estrela, J.M.4
  • 20
    • 0344393732 scopus 로고    scopus 로고
    • Strategies for reversing drug resistance
    • Fojo T, Bates S. Strategies for reversing drug resistance. Oncogene 2003; 22: 7512-7523.
    • (2003) Oncogene , vol.22 , pp. 7512-7523
    • Fojo, T.1    Bates, S.2
  • 21
    • 0642374221 scopus 로고    scopus 로고
    • The role of glutathione-S-transferase in anti-cancer drug resistance
    • Townsend DM, Tew KD. The role of glutathione-S-transferase in anti-cancer drug resistance. Oncogene 2003; 22: 7369-7375.
    • (2003) Oncogene , vol.22 , pp. 7369-7375
    • Townsend, D.M.1    Tew, K.D.2
  • 22
    • 0025312043 scopus 로고
    • Glutathione regulates activation-dependent DNA synthesis in highly purified normal human T lymphocytes stimulated via the CD2 and CD3 antigens
    • Suthanthiran M, Anderson ME, Sharma VK, Meister A. Glutathione regulates activation-dependent DNA synthesis in highly purified normal human T lymphocytes stimulated via the CD2 and CD3 antigens. Proc Natl Acad Sci USA 1990; 87: 3343-3347.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 3343-3347
    • Suthanthiran, M.1    Anderson, M.E.2    Sharma, V.K.3    Meister, A.4
  • 23
    • 0026343403 scopus 로고
    • Glutathione deficiency produced by inhibition of its synthesis, and its reversal; applications in research and therapy
    • Meister A. Glutathione deficiency produced by inhibition of its synthesis, and its reversal; applications in research and therapy. Pharmacol Ther 1991; 51: 155-194.
    • (1991) Pharmacol Ther , vol.51 , pp. 155-194
    • Meister, A.1
  • 24
    • 0027225367 scopus 로고
    • Depletion of tumour glutathione in vivo by buthionine sulphoximine: Modulation by the rate of cellular proliferation and inhibition of cancer growth
    • Terradez P, Asensi M, Lasso de la Vega MC, Puertes IR, Vina J, Estrela JM. Depletion of tumour glutathione in vivo by buthionine sulphoximine: modulation by the rate of cellular proliferation and inhibition of cancer growth. Biochem J 1993; 292: 477-483.
    • (1993) Biochem J , vol.292 , pp. 477-483
    • Terradez, P.1    Asensi, M.2    Lasso De La Vega, M.C.3    Puertes, I.R.4    Vina, J.5    Estrela, J.M.6
  • 25
    • 0028918334 scopus 로고
    • Superoxide and hydrogen peroxide in relation to mammalian cell proliferation
    • Burdon RH. Superoxide and hydrogen peroxide in relation to mammalian cell proliferation. Free Radic Biol Med 1995; 18: 775-794.
    • (1995) Free Radic Biol Med , vol.18 , pp. 775-794
    • Burdon, R.H.1
  • 28
    • 33744982319 scopus 로고
    • The importance of sulfhydryl groups in biology and medicine
    • Barron ES. The importance of sulfhydryl groups in biology and medicine. Tex Rep Biol Med 1953; 11: 653-670.
    • (1953) Tex Rep Biol Med , vol.11 , pp. 653-670
    • Barron, E.S.1
  • 29
    • 33744978022 scopus 로고
    • Mechanism of natural and acquired resistance to methyl-bis-(beta- chlorethyl)-amine N-oxide in ascites tumors
    • Hirono I. Mechanism of natural and acquired resistance to methyl-bis-(beta-chlorethyl)-amine N-oxide in ascites tumors. Gann 1961; 52: 39-48.
    • (1961) Gann , vol.52 , pp. 39-48
    • Hirono, I.1
  • 30
    • 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 1999; 27: 916-921.
    • (1999) Free Radic Biol Med , vol.27 , pp. 916-921
    • Sies, H.1
  • 31
    • 0021127473 scopus 로고
    • Glutathione metabolism as a determinant of therapeutic efficacy: A review
    • Arrick BA, Nathan CF. Glutathione metabolism as a determinant of therapeutic efficacy: a review. Cancer Res 1984; 44: 4224-4232.
    • (1984) Cancer Res , vol.44 , pp. 4224-4232
    • Arrick, B.A.1    Nathan, C.F.2
  • 33
    • 0035854787 scopus 로고    scopus 로고
    • Tumoricidal activity of endothelial cells. Inhibition of endothelial nitric oxide production abrogates tumor cytotoxicity induced by hepatic sinusoidal endothelium in response to B16 melanoma adhesion in vitro
    • Carretero J, Obrador E, Esteve JM, Ortega A, Pellicer JA, Sempere FV, Estrela JM. Tumoricidal activity of endothelial cells. Inhibition of endothelial nitric oxide production abrogates tumor cytotoxicity induced by hepatic sinusoidal endothelium in response to B16 melanoma adhesion in vitro. J Biol Chem 2001; 276: 25775-25782.
    • (2001) J Biol Chem , vol.276 , pp. 25775-25782
    • Carretero, J.1    Obrador, E.2    Esteve, J.M.3    Ortega, A.4    Pellicer, J.A.5    Sempere, F.V.6    Estrela, J.M.7
  • 34
    • 20544437870 scopus 로고    scopus 로고
    • Overview of tumor cell chemoresistance mechanisms
    • Gatti L, Zunino F. Overview of tumor cell chemoresistance mechanisms. Methods Mol Med 2005; 111: 127-148.
    • (2005) Methods Mol Med , vol.111 , pp. 127-148
    • Gatti, L.1    Zunino, F.2
  • 37
    • 0033231162 scopus 로고    scopus 로고
    • Biologic and pharmacologic regulation of mammalian glutathione synthesis
    • Griffith OW. Biologic and pharmacologic regulation of mammalian glutathione synthesis. Free Radic Biol Med 1999; 27: 922-935.
    • (1999) Free Radic Biol Med , vol.27 , pp. 922-935
    • Griffith, O.W.1
  • 38
    • 0022272497 scopus 로고
    • Methods for the selective modification of glutathione metabolism and study of glutathione transport
    • Meister A. Methods for the selective modification of glutathione metabolism and study of glutathione transport. Methods Enzymol 1985; 113: 571-585.
    • (1985) Methods Enzymol , vol.113 , pp. 571-585
    • Meister, A.1
  • 39
    • 0033067354 scopus 로고    scopus 로고
    • Regulation of hepatic glutathione synthesis: Current concepts and controversies
    • Lu SC. Regulation of hepatic glutathione synthesis: current concepts and controversies. FASEB J 1999; 13: 1169-1183.
    • (1999) FASEB J , vol.13 , pp. 1169-1183
    • Lu, S.C.1
  • 40
    • 0014876254 scopus 로고
    • The gamma-glutamyl cycle: A possible transport system for amino acids
    • Orlowski M, Meister A. The gamma-glutamyl cycle: a possible transport system for amino acids. Proc Natl Acad Sci USA 1970; 67: 1248-1255.
    • (1970) Proc Natl Acad Sci USA , vol.67 , pp. 1248-1255
    • Orlowski, M.1    Meister, A.2
  • 41
    • 0032617250 scopus 로고    scopus 로고
    • The enzymes of glutathione synthesis: Gamma-glutamylcysteine synthetase
    • Griffith OW, Mulcahy RT. The enzymes of glutathione synthesis: gamma-glutamylcysteine synthetase. Adv Enzymol Relat Areas Mol Biol 1999; 73: xii, 209-267.
    • (1999) Adv Enzymol Relat Areas Mol Biol , vol.73
    • Griffith, O.W.1    Mulcahy, R.T.2
  • 42
    • 0025091990 scopus 로고
    • Amino acid sequence of rat kidney gamma-glutamylcysteine synthetase
    • Yan N, Meister A. Amino acid sequence of rat kidney gamma- glutamylcysteine synthetase. J Biol Chem 1990; 265: 1588-1593.
    • (1990) J Biol Chem , vol.265 , pp. 1588-1593
    • Yan, N.1    Meister, A.2
  • 43
    • 0027171195 scopus 로고
    • Catalytic and regulatory properties of the heavy subunit of rat kidney gamma-glutamylcysteine synthetase
    • Huang CS, Chang LS, Anderson ME, Meister A. Catalytic and regulatory properties of the heavy subunit of rat kidney gamma-glutamylcysteine synthetase. J Biol Chem 1993; 268: 19675-19680.
    • (1993) J Biol Chem , vol.268 , pp. 19675-19680
    • Huang, C.S.1    Chang, L.S.2    Anderson, M.E.3    Meister, A.4
  • 44
    • 0029591133 scopus 로고
    • Mapping of the glutamate-cysteine ligase catalytic subunit gene (GLCLC) to human chromosome 6p12 and mouse chromosome 9D-E and of the regulatory subunit gene (GLCLR) to human chromosome 1p21-p22 and mouse chromosome 3H1-3
    • Tsuchiya K, Mulcahy RT, Reid LL, Disteche CM, Kavanagh TJ. Mapping of the glutamate-cysteine ligase catalytic subunit gene (GLCLC) to human chromosome 6p12 and mouse chromosome 9D-E and of the regulatory subunit gene (GLCLR) to human chromosome 1p21-p22 and mouse chromosome 3H1-3. Genomics 1995; 30: 630-632.
    • (1995) Genomics , vol.30 , pp. 630-632
    • Tsuchiya, K.1    Mulcahy, R.T.2    Reid, L.L.3    Disteche, C.M.4    Kavanagh, T.J.5
  • 45
    • 0027052233 scopus 로고
    • Loss of suppression of GSH synthesis at low cell density in primary cultures of rat hepatocytes
    • Lu SC, Ge JL. Loss of suppression of GSH synthesis at low cell density in primary cultures of rat hepatocytes. Am J Physiol 1992; 263: C1181-1189.
    • (1992) Am J Physiol , vol.263
    • Lu, S.C.1    Ge, J.L.2
  • 46
    • 0032435501 scopus 로고    scopus 로고
    • Regulation of hepatic glutathione synthesis
    • Lu SC. Regulation of hepatic glutathione synthesis. Semin Liver Dis 1998; 18: 331-343.
    • (1998) Semin Liver Dis , vol.18 , pp. 331-343
    • Lu, S.C.1
  • 47
    • 21344445674 scopus 로고    scopus 로고
    • Activation of c-Jun-N-terminal kinase is required for apoptosis triggered by glutathione disulfide in neuroblastoma cells
    • Filomeni G, Aquilano K, Civitareale P, Rotilio G, Ciriolo MR. Activation of c-Jun-N-terminal kinase is required for apoptosis triggered by glutathione disulfide in neuroblastoma cells. Free Radic Biol Med 2005; 39: 345-354.
    • (2005) Free Radic Biol Med , vol.39 , pp. 345-354
    • Filomeni, G.1    Aquilano, K.2    Civitareale, P.3    Rotilio, G.4    Ciriolo, M.R.5
  • 48
    • 0018801016 scopus 로고
    • Glutathione synthetase. Purification from rat kidney and mapping of the substrate binding sites
    • Oppenheimer L, Wellner VP, Griffith OW, Meister A. Glutathione synthetase. Purification from rat kidney and mapping of the substrate binding sites. J Biol Chem 1979; 254: 5184-5190.
    • (1979) J Biol Chem , vol.254 , pp. 5184-5190
    • Oppenheimer, L.1    Wellner, V.P.2    Griffith, O.W.3    Meister, A.4
  • 49
    • 0030747207 scopus 로고    scopus 로고
    • Glutathione synthetase is dispensable for growth under both normal and oxidative stress conditions in the yeast Saccharomyces cerevisiae due to an accumulation of the dipeptide gamma-glutamylcysteine
    • Grant CM, MacIver FH, Dawes IW. Glutathione synthetase is dispensable for growth under both normal and oxidative stress conditions in the yeast Saccharomyces cerevisiae due to an accumulation of the dipeptide gamma-glutamylcysteine. Mol Biol Cell 1997; 8: 1699-1707.
    • (1997) Mol Biol Cell , vol.8 , pp. 1699-1707
    • Grant, C.M.1    MacIver, F.H.2    Dawes, I.W.3
  • 50
    • 0024264526 scopus 로고
    • Glutathione metabolism and its selective modification
    • Meister A. Glutathione metabolism and its selective modification. J Biol Chem 1988; 263: 17205-17208.
    • (1988) J Biol Chem , vol.263 , pp. 17205-17208
    • Meister, A.1
  • 51
    • 0021695489 scopus 로고
    • New aspects of glutathione biochemistry and transport - Selective alteration of glutathione metabolism
    • Meister A. New aspects of glutathione biochemistry and transport - selective alteration of glutathione metabolism. Nutr Rev 1984; 42: 397-410.
    • (1984) Nutr Rev , vol.42 , pp. 397-410
    • Meister, A.1
  • 52
    • 0022460516 scopus 로고
    • Intracellular cysteine and glutathione delivery systems
    • Meister A, Anderson ME, Hwang O. Intracellular cysteine and glutathione delivery systems. J Am Coll Nutr 1986; 5: 137-151.
    • (1986) J Am Coll Nutr , vol.5 , pp. 137-151
    • Meister, A.1    Anderson, M.E.2    Hwang, O.3
  • 54
    • 0037505644 scopus 로고    scopus 로고
    • Analysis of glutathione: Implication in redox and detoxification
    • Pastore A, Federici G, Bertini E, Piemonte F. Analysis of glutathione: implication in redox and detoxification. Clin Chim Acta 2003; 333: 19-39.
    • (2003) Clin Chim Acta , vol.333 , pp. 19-39
    • Pastore, A.1    Federici, G.2    Bertini, E.3    Piemonte, F.4
  • 55
    • 0025802732 scopus 로고
    • Glutathione conjugation with phosphoramide mustard and cyclophosphamide. A mechanistic study using tandem mass spectrometry
    • Yuan ZM, Smith PB, Brundrett RB, Colvin M, Fenselau C. Glutathione conjugation with phosphoramide mustard and cyclophosphamide. A mechanistic study using tandem mass spectrometry. Drug Metab Dispos 1991; 19: 625-629.
    • (1991) Drug Metab Dispos , vol.19 , pp. 625-629
    • Yuan, Z.M.1    Smith, P.B.2    Brundrett, R.B.3    Colvin, M.4    Fenselau, C.5
  • 58
    • 0032421171 scopus 로고    scopus 로고
    • Role of the liver in interorgan homeostasis of glutathione and cyst(e)ine
    • Ookhtens M, Kaplowitz N. Role of the liver in interorgan homeostasis of glutathione and cyst(e)ine. Semin Liver Dis 1998; 18: 313-329.
    • (1998) Semin Liver Dis , vol.18 , pp. 313-329
    • Ookhtens, M.1    Kaplowitz, N.2
  • 59
    • 0032610934 scopus 로고    scopus 로고
    • Glutathione and the regulation of cell death
    • Hall AG. Glutathione and the regulation of cell death. Adv Exp Med Biol 1999; 457: 199-203.
    • (1999) Adv Exp Med Biol , vol.457 , pp. 199-203
    • Hall, A.G.1
  • 60
    • 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 RB, Jr., 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
  • 61
    • 0033655446 scopus 로고    scopus 로고
    • Regulation of glutathione synthesis
    • Lu SC. Regulation of glutathione synthesis. Curr Top Cell Regul 2000; 36: 95-116.
    • (2000) Curr Top Cell Regul , vol.36 , pp. 95-116
    • Lu, S.C.1
  • 62
    • 0036804710 scopus 로고    scopus 로고
    • Free radicals, antioxidants, and nutrition
    • Fang YZ, Yang S, Wu G. Free radicals, antioxidants, and nutrition. Nutrition 2002; 18: 872-879.
    • (2002) Nutrition , vol.18 , pp. 872-879
    • Fang, Y.Z.1    Yang, S.2    Wu, G.3
  • 63
    • 0036123235 scopus 로고    scopus 로고
    • In vivo antioxidant role of glutathione peroxidase: Evidence from knockout mice
    • Lei XG. In vivo antioxidant role of glutathione peroxidase: evidence from knockout mice. Methods Enzymol 2002; 347: 213-225.
    • (2002) Methods Enzymol , vol.347 , pp. 213-225
    • Lei, X.G.1
  • 64
    • 0033231351 scopus 로고    scopus 로고
    • Gene expression and the thiol redox state
    • Arrigo AP. Gene expression and the thiol redox state. Free Radic Biol Med 1999; 27: 936-944.
    • (1999) Free Radic Biol Med , vol.27 , pp. 936-944
    • Arrigo, A.P.1
  • 65
    • 0032874845 scopus 로고    scopus 로고
    • Glutathione and glutathione-dependent enzymes represent a co-ordinately regulated defence against oxidative stress
    • Hayes JD, McLellan LI. Glutathione and glutathione-dependent enzymes represent a co-ordinately regulated defence against oxidative stress. Free Radic Res 1999; 31: 273-300.
    • (1999) Free Radic Res , vol.31 , pp. 273-300
    • Hayes, J.D.1    McLellan, L.I.2
  • 66
    • 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
  • 67
    • 0029984062 scopus 로고    scopus 로고
    • Antioxidant and redox regulation of gene transcription
    • Sen CK, Packer L. Antioxidant and redox regulation of gene transcription. FASEB J 1996; 10: 709-720.
    • (1996) FASEB J , vol.10 , pp. 709-720
    • Sen, C.K.1    Packer, L.2
  • 68
    • 0024446703 scopus 로고
    • Transport of glutathione, glutathione disulfide, and glutathione conjugates across the hepatocyte plasma membrane
    • Akerboom TP, Sies H. Transport of glutathione, glutathione disulfide, and glutathione conjugates across the hepatocyte plasma membrane. Methods Enzymol 1989; 173: 523-534.
    • (1989) Methods Enzymol , vol.173 , pp. 523-534
    • Akerboom, T.P.1    Sies, H.2
  • 69
    • 0031021397 scopus 로고    scopus 로고
    • Structure, catalytic mechanism, and evolution of the glutathione transferases
    • Armstrong RN. Structure, catalytic mechanism, and evolution of the glutathione transferases. Chem Res Toxicol 1997; 10: 2-18.
    • (1997) Chem Res Toxicol , vol.10 , pp. 2-18
    • Armstrong, R.N.1
  • 73
    • 18044374624 scopus 로고    scopus 로고
    • Glutathione s-transferase polymorphisms (GSTM1, GSTP1 and GSTT1) and the risk of acute leukaemia: A systematic review and meta-analysis
    • Ye Z, Song H. Glutathione s-transferase polymorphisms (GSTM1, GSTP1 and GSTT1) and the risk of acute leukaemia: a systematic review and meta-analysis. Eur J Cancer 2005; 41: 980-989.
    • (2005) Eur J Cancer , vol.41 , pp. 980-989
    • Ye, Z.1    Song, H.2
  • 74
    • 0024262737 scopus 로고
    • Efficacy of oral N-acetylcysteine in the treatment of acetaminophen overdose. Analysis of the national multicenter study (1976 to 1985)
    • Smilkstein MJ, Knapp GL, Kulig KW, Rumack BH. Efficacy of oral N-acetylcysteine in the treatment of acetaminophen overdose. Analysis of the national multicenter study (1976 to 1985). N Engl J Med 1988; 319: 1557-1562.
    • (1988) N Engl J Med , vol.319 , pp. 1557-1562
    • Smilkstein, M.J.1    Knapp, G.L.2    Kulig, K.W.3    Rumack, B.H.4
  • 75
    • 0036363795 scopus 로고    scopus 로고
    • Gene expression and thiol redox state
    • Kretz-Remy C, Arrigo AP. Gene expression and thiol redox state. Methods Enzymol 2002; 348: 200-215.
    • (2002) Methods Enzymol , vol.348 , pp. 200-215
    • Kretz-Remy, C.1    Arrigo, A.P.2
  • 76
    • 0033869092 scopus 로고    scopus 로고
    • Regulation of protein function by S-glutathiolation in response to oxidative and nitrosative stress
    • Klatt P, Lamas S. Regulation of protein function by S-glutathiolation in response to oxidative and nitrosative stress. Eur J Biochem 2000; 267: 4928-4944.
    • (2000) Eur J Biochem , vol.267 , pp. 4928-4944
    • Klatt, P.1    Lamas, S.2
  • 77
    • 16644389632 scopus 로고    scopus 로고
    • Glutathione depletion-induced chromosomal DNA fragmentation associated with apoptosis and necrosis
    • Higuchi Y. Glutathione depletion-induced chromosomal DNA fragmentation associated with apoptosis and necrosis. J Cell Mol Med 2004; 8: 455-464.
    • (2004) J Cell Mol Med , vol.8 , pp. 455-464
    • Higuchi, Y.1
  • 78
    • 0032955185 scopus 로고    scopus 로고
    • Glutathione S-transferases - A review
    • Salinas AE, Wong MG. Glutathione S-transferases - a review. Curr Med Chem 1999; 6: 279-309.
    • (1999) Curr Med Chem , vol.6 , pp. 279-309
    • Salinas, A.E.1    Wong, M.G.2
  • 79
    • 0142150156 scopus 로고    scopus 로고
    • Does glutathione S-transferase Pi (GST-Pi) a marker protein for cancer?
    • Aliya S, Reddanna P, Thyagaraju K. Does glutathione S-transferase Pi (GST-Pi) a marker protein for cancer? Mol Cell Biochem 2003; 253: 319-327.
    • (2003) Mol Cell Biochem , vol.253 , pp. 319-327
    • Aliya, S.1    Reddanna, P.2    Thyagaraju, K.3
  • 80
    • 2442638662 scopus 로고    scopus 로고
    • Regulatory mechanism of glutathione S-transferase P-form during chemical hepatocarcinogenesis: Old wine in a new bottle
    • Higashi K, Hiai H, Higashi T, Muramatsu M. Regulatory mechanism of glutathione S-transferase P-form during chemical hepatocarcinogenesis: old wine in a new bottle. Cancer Lett 2004; 209: 155-163.
    • (2004) Cancer Lett , vol.209 , pp. 155-163
    • Higashi, K.1    Hiai, H.2    Higashi, T.3    Muramatsu, M.4
  • 81
    • 22544436117 scopus 로고    scopus 로고
    • 7-Nitro-2,1,3-benzoxadiazole derivatives, a new class of suicide inhibitors for glutathione S-transferases. Mechanism of action of potential anticancer drugs
    • Ricci G, De Maria F, Antonini G, Turella P, Bullo A, Stella L, Filomeni G, Federici G, Caccuri AM. 7-Nitro-2,1,3-benzoxadiazole derivatives, a new class of suicide inhibitors for glutathione S-transferases. Mechanism of action of potential anticancer drugs. J Biol Chem 2005; 280: 26397-26405.
    • (2005) J Biol Chem , vol.280 , pp. 26397-26405
    • Ricci, G.1    De Maria, F.2    Antonini, G.3    Turella, P.4    Bullo, A.5    Stella, L.6    Filomeni, G.7    Federici, G.8    Caccuri, A.M.9
  • 82
    • 3242686012 scopus 로고    scopus 로고
    • Glutathione metabolism during aging and in Alzheimer disease
    • Liu H, Wang H, Shenvi S, Hagen TM, Liu RM. Glutathione metabolism during aging and in Alzheimer disease. Ann NY Acad Sci 2004; 1019: 346-349.
    • (2004) Ann NY Acad Sci , vol.1019 , pp. 346-349
    • Liu, H.1    Wang, H.2    Shenvi, S.3    Hagen, T.M.4    Liu, R.M.5
  • 83
    • 0020478933 scopus 로고
    • Status of the mitochondrial pool of glutathione in the isolated hepatocyte
    • Meredith MJ, Reed DJ. Status of the mitochondrial pool of glutathione in the isolated hepatocyte. J Biol Chem 1982; 257: 3747-3753.
    • (1982) J Biol Chem , vol.257 , pp. 3747-3753
    • Meredith, M.J.1    Reed, D.J.2
  • 84
    • 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
  • 85
    • 0001547757 scopus 로고
    • Origin and turnover of mitochondrial glutathione
    • Griffith OW, Meister A. Origin and turnover of mitochondrial glutathione. Proc Natl Acad Sci USA 1985; 82: 4668-4672.
    • (1985) Proc Natl Acad Sci USA , vol.82 , pp. 4668-4672
    • Griffith, O.W.1    Meister, A.2
  • 88
    • 0037853201 scopus 로고    scopus 로고
    • Tumor cytotoxicity by endothelial cells. Impairment of the mitochondrial system for glutathione uptake in mouse B16 melanoma cells that survive after in vitro interaction with the hepatic sinusoidal endothelium
    • Ortega AL, Carretero J, Obrador E, Gambini J, Asensi M, Rodilla V, Estrela JM. Tumor cytotoxicity by endothelial cells. Impairment of the mitochondrial system for glutathione uptake in mouse B16 melanoma cells that survive after in vitro interaction with the hepatic sinusoidal endothelium. J Biol Chem 2003; 278: 13888-13897.
    • (2003) J Biol Chem , vol.278 , pp. 13888-13897
    • Ortega, A.L.1    Carretero, J.2    Obrador, E.3    Gambini, J.4    Asensi, M.5    Rodilla, V.6    Estrela, J.M.7
  • 89
    • 1242291926 scopus 로고    scopus 로고
    • A role for the 2-oxoglutarate carrier in glutathione transport into hepatocyte mitochondria?
    • author reply 571
    • Estrela JM, Ortega AL, Carretero J. A role for the 2-oxoglutarate carrier in glutathione transport into hepatocyte mitochondria? Hepatology 2004; 39: 570-571; author reply 571.
    • (2004) Hepatology , vol.39 , pp. 570-571
    • Estrela, J.M.1    Ortega, A.L.2    Carretero, J.3
  • 90
    • 0031918742 scopus 로고    scopus 로고
    • The mitochondrial death/life regulator in apoptosis and necrosis
    • Kroemer G, Dallaporta B, Resche-Rigon M. The mitochondrial death/life regulator in apoptosis and necrosis. Annu Rev Physiol 1998; 60: 619-642.
    • (1998) Annu Rev Physiol , vol.60 , pp. 619-642
    • Kroemer, G.1    Dallaporta, B.2    Resche-Rigon, M.3
  • 91
    • 0033088957 scopus 로고    scopus 로고
    • Review: The role of glutathione in the regulation of apoptosis
    • Hall AG. Review: The role of glutathione in the regulation of apoptosis. Em J Clin Invest 1999; 29: 238-245.
    • (1999) Em J Clin Invest , vol.29 , pp. 238-245
    • Hall, A.G.1
  • 92
    • 1242294484 scopus 로고    scopus 로고
    • A major fraction of ndoplasmic reticulum-located glutathione is present as mixed disulfides with protein
    • Bass R, Ruddock LW, Klappa P, Freedman RB. A major fraction of ndoplasmic reticulum-located glutathione is present as mixed disulfides with protein. J Biol Chem 2004; 279: 5257-5262.
    • (2004) J Biol Chem , vol.279 , pp. 5257-5262
    • Bass, R.1    Ruddock, L.W.2    Klappa, P.3    Freedman, R.B.4
  • 93
    • 0029006074 scopus 로고
    • Measurement of glutathione redox state in cytosol and secretory pathway of cultured cells
    • Hwang C, Lodish HF, Sinskey AJ. Measurement of glutathione redox state in cytosol and secretory pathway of cultured cells. Methods Enzymol 1995; 251: 212-221.
    • (1995) Methods Enzymol , vol.251 , pp. 212-221
    • Hwang, C.1    Lodish, H.F.2    Sinskey, A.J.3
  • 98
    • 0032921258 scopus 로고    scopus 로고
    • Changes in glutathione status and the antioxidant system in blood and in cancer cells associate with tumour growth in vivo
    • Navarro J, Obrador E, Carretero J, Petschen I, Avino J, Perez P, Estrela JM. Changes in glutathione status and the antioxidant system in blood and in cancer cells associate with tumour growth in vivo. Free Radic Biol Med 1999; 26: 410-418.
    • (1999) Free Radic Biol Med , vol.26 , pp. 410-418
    • Navarro, J.1    Obrador, E.2    Carretero, J.3    Petschen, I.4    Avino, J.5    Perez, P.6    Estrela, J.M.7
  • 99
    • 0027952488 scopus 로고
    • Changes in plasma glutathione concentrations, turnover, and disposal in developing rats
    • Ookhtens M, Mittur AV, Erhart NA. Changes in plasma glutathione concentrations, turnover, and disposal in developing rats. Am J Physiol 1994; 266: R979-988.
    • (1994) Am J Physiol , vol.266
    • Ookhtens, M.1    Mittur, A.V.2    Erhart, N.A.3
  • 100
    • 0032407040 scopus 로고    scopus 로고
    • Roles of MRP2 and oatp1 in hepatocellular export of reduced glutathione
    • Ballatori N, Rebbeor JF. Roles of MRP2 and oatp1 in hepatocellular export of reduced glutathione. Semin Liver Dis 1998; 18: 377-387.
    • (1998) Semin Liver Dis , vol.18 , pp. 377-387
    • Ballatori, N.1    Rebbeor, J.F.2
  • 101
    • 0019173673 scopus 로고
    • Dynamic state of glutathione in blood plasma
    • Anderson ME, Meister A. Dynamic state of glutathione in blood plasma. J Biol Chem 1980; 255: 9530-9533.
    • (1980) J Biol Chem , vol.255 , pp. 9530-9533
    • Anderson, M.E.1    Meister, A.2
  • 103
    • 0028817509 scopus 로고
    • Expression of gamma-glutamyl transpeptidase provides tumor cells with a selective growth advantage at physiologic concentrations of cyst(e)ine
    • Hanigan MH. Expression of gamma-glutamyl transpeptidase provides tumor cells with a selective growth advantage at physiologic concentrations of cyst(e)ine. Carcinogenesis 1995; 16: 181-185.
    • (1995) Carcinogenesis , vol.16 , pp. 181-185
    • Hanigan, M.H.1
  • 104
    • 0029954846 scopus 로고    scopus 로고
    • Glutathione and related enzymes in multidrug resistance
    • O'Brien ML, Tew KD. Glutathione and related enzymes in multidrug resistance. Em J Cancer 1996; 32A: 967-978.
    • (1996) Em J Cancer , vol.32 A , pp. 967-978
    • O'Brien, M.L.1    Tew, K.D.2
  • 105
    • 0032605942 scopus 로고    scopus 로고
    • Multidrug resistance protein MRP1, glutathione, and related enzymes. Their importance in acute myeloid leukemia
    • van der Kolk DM, Vellenga E, Muller M, de Vries EG. Multidrug resistance protein MRP1, glutathione, and related enzymes. Their importance in acute myeloid leukemia. Adv Exp Med Biol 1999; 457: 187-198.
    • (1999) Adv Exp Med Biol , vol.457 , pp. 187-198
    • Van Der Kolk, D.M.1    Vellenga, E.2    Muller, M.3    De Vries, E.G.4
  • 106
    • 0036140408 scopus 로고    scopus 로고
    • gamma-Glutamyl transpeptidase overexpression increases metastatic growth of B16 melanoma cells in the mouse liver
    • Obrador E, Carretero J, Ortega A, Medina I, Rodilla V, Pellicer JA, Estrela JM. gamma-Glutamyl transpeptidase overexpression increases metastatic growth of B16 melanoma cells in the mouse liver. Hepatology 2002; 35: 74-81.
    • (2002) Hepatology , vol.35 , pp. 74-81
    • Obrador, E.1    Carretero, J.2    Ortega, A.3    Medina, I.4    Rodilla, V.5    Pellicer, J.A.6    Estrela, J.M.7
  • 107
    • 0141925744 scopus 로고    scopus 로고
    • Down-regulation of glutathione and Bcl-2 synthesis in mouse B16 melanoma cells avoids their survival during interaction with the vascular endothelium
    • Ortega A, Ferrer P, Carretero J, Obrador E, Asensi M, Pellicer JA, Estrela JM. Down-regulation of glutathione and Bcl-2 synthesis in mouse B16 melanoma cells avoids their survival during interaction with the vascular endothelium. J Biol Chem 2003; 278: 39591-39599.
    • (2003) J Biol Chem , vol.278 , pp. 39591-39599
    • Ortega, A.1    Ferrer, P.2    Carretero, J.3    Obrador, E.4    Asensi, M.5    Pellicer, J.A.6    Estrela, J.M.7
  • 108
    • 14844286405 scopus 로고    scopus 로고
    • Acceleration of glutathione efflux and inhibition of gamma- glutamyltranspeptidase sensitize metastatic B16 melanoma cells to endothelium-induced cytotoxicity
    • Benlloch M, Ortega A, Ferrer P, Segarra R, Obrador E, Asensi M, Carretero J, Estrela JM. Acceleration of glutathione efflux and inhibition of gamma-glutamyltranspeptidase sensitize metastatic B16 melanoma cells to endothelium-induced cytotoxicity. J Biol Chem 2005; 280: 6950-6959.
    • (2005) J Biol Chem , vol.280 , pp. 6950-6959
    • Benlloch, M.1    Ortega, A.2    Ferrer, P.3    Segarra, R.4    Obrador, E.5    Asensi, M.6    Carretero, J.7    Estrela, J.M.8
  • 110
    • 0142107445 scopus 로고    scopus 로고
    • Multidrug resistance-associated pro teins: Export pumps for conjugates with glutathione, glucuronate or sulfate
    • Homolya L, Varadi A, Sarkadi B. Multidrug resistance-associated pro teins: export pumps for conjugates with glutathione, glucuronate or sulfate. Biofactors 2003; 17: 103-114.
    • (2003) Biofactors , vol.17 , pp. 103-114
    • Homolya, L.1    Varadi, A.2    Sarkadi, B.3
  • 112
    • 0034674901 scopus 로고    scopus 로고
    • A family of drug transporters: The multidrug resistance-associated proteins
    • Borst P, Evers R, Kool M, Wijnholds J. A family of drug transporters: the multidrug resistance-associated proteins. J Natl Cancer Inst 2000; 92: 1295-1302.
    • (2000) J Natl Cancer Inst , vol.92 , pp. 1295-1302
    • Borst, P.1    Evers, R.2    Kool, M.3    Wijnholds, J.4
  • 113
    • 0036364467 scopus 로고    scopus 로고
    • Multidrug resistance in cancer: Role of ATP-dependent transporters
    • Gottesman MM, Fojo T, Bates SE. Multidrug resistance in cancer: role of ATP-dependent transporters. Nat Rev Cancer 2002; 2: 48-58.
    • (2002) Nat Rev Cancer , vol.2 , pp. 48-58
    • Gottesman, M.M.1    Fojo, T.2    Bates, S.E.3
  • 114
    • 0346365485 scopus 로고    scopus 로고
    • Natural mechanisms protecting against cancer
    • Jakobisiak M, Lasek W, Golab J. Natural mechanisms protecting against cancer. Immunol Lett 2003; 90: 103-122.
    • (2003) Immunol Lett , vol.90 , pp. 103-122
    • Jakobisiak, M.1    Lasek, W.2    Golab, J.3
  • 116
    • 0029097316 scopus 로고
    • Molecular controls of growth arrest and apoptosis: P53-dependent and independent pathways
    • Liebermann DA, Hoffman B, Steinman RA. Molecular controls of growth arrest and apoptosis: p53-dependent and independent pathways. Oncogene 1995; 11: 199-210.
    • (1995) Oncogene , vol.11 , pp. 199-210
    • Liebermann, D.A.1    Hoffman, B.2    Steinman, R.A.3
  • 118
    • 0025021774 scopus 로고
    • Identifying tumor suppressor genes in human colorectal cancer
    • Stanbridge EJ. Identifying tumor suppressor genes in human colorectal cancer. Science 1990; 247: 12-13.
    • (1990) Science , vol.247 , pp. 12-13
    • Stanbridge, E.J.1
  • 119
    • 0019792243 scopus 로고
    • The natural history of carcinogenesis: Implications of experimental carcinogenesis in the genesis of human cancer
    • Pitot HC, Goldsworthy T, Moran S. The natural history of carcinogenesis: implications of experimental carcinogenesis in the genesis of human cancer. J Supramol Struct Cell Biochem 1981; 17: 133-146.
    • (1981) J Supramol Struct Cell Biochem , vol.17 , pp. 133-146
    • Pitot, H.C.1    Goldsworthy, T.2    Moran, S.3
  • 124
    • 2642573655 scopus 로고    scopus 로고
    • Role of oxidative stress and the antioxidant network in cutaneous carcinogenesis
    • Sander CS, Chang H, Hamm F, Elsner P, Thiele JJ. Role of oxidative stress and the antioxidant network in cutaneous carcinogenesis. Int J Dermatol 2004; 43: 326-335.
    • (2004) Int J Dermatol , vol.43 , pp. 326-335
    • Sander, C.S.1    Chang, H.2    Hamm, F.3    Elsner, P.4    Thiele, J.J.5
  • 125
    • 0023925468 scopus 로고
    • Detection and identification of activated oncogenes in human skin cancers occurring on sun-exposed body sites
    • Ananthaswamy HN, Price JE, Goldberg LH, Bales ES. Detection and identification of activated oncogenes in human skin cancers occurring on sun-exposed body sites. Cancer Res 1988; 48: 3341-3346.
    • (1988) Cancer Res , vol.48 , pp. 3341-3346
    • Ananthaswamy, H.N.1    Price, J.E.2    Goldberg, L.H.3    Bales, E.S.4
  • 127
    • 18244422745 scopus 로고    scopus 로고
    • Genetic and epigenetic damage induced by reactive nitrogen species: Implications in carcinogenesis
    • Ohshima H. Genetic and epigenetic damage induced by reactive nitrogen species: implications in carcinogenesis. Toxicol Lett 2003; 140-141: 99-104.
    • (2003) Toxicol Lett , vol.140-141 , pp. 99-104
    • Ohshima, H.1
  • 128
    • 0042062310 scopus 로고    scopus 로고
    • Chemical basis of inflammation-induced carcinogenesis
    • Ohshima H, Tatemichi M, Sawa T. Chemical basis of inflammation-induced carcinogenesis. Arch Biochem Biophys 2003; 417: 3-11.
    • (2003) Arch Biochem Biophys , vol.417 , pp. 3-11
    • Ohshima, H.1    Tatemichi, M.2    Sawa, T.3
  • 129
    • 17444424206 scopus 로고    scopus 로고
    • Intestinal glutathione: Determinant of mucosal peroxide transport, metabolism, and oxidative susceptibility
    • Aw TY. Intestinal glutathione: determinant of mucosal peroxide transport, metabolism, and oxidative susceptibility. Toxicol Appl Pharmacol 2005; 204: 320-328.
    • (2005) Toxicol Appl Pharmacol , vol.204 , pp. 320-328
    • Aw, T.Y.1
  • 130
    • 0030568065 scopus 로고    scopus 로고
    • Role of tissue antioxidant defence in thyroid cancers
    • Sadani GR, Nadkarni GD. Role of tissue antioxidant defence in thyroid cancers. Cancer Lett 1996; 109: 231-235.
    • (1996) Cancer Lett , vol.109 , pp. 231-235
    • Sadani, G.R.1    Nadkarni, G.D.2
  • 133
    • 0028111564 scopus 로고
    • Sensitive enzymatic cycling assay for glutathione: Measurements of glutathione content and its modulation by buthionine sulfoximine in vivo and in vitro in human colon cancer
    • Berger SJ, Gosky D, Zborowska E, Willson JK, Berger NA. Sensitive enzymatic cycling assay for glutathione: measurements of glutathione content and its modulation by buthionine sulfoximine in vivo and in vitro in human colon cancer. Cancer Res 1994; 54: 4077-4083.
    • (1994) Cancer Res , vol.54 , pp. 4077-4083
    • Berger, S.J.1    Gosky, D.2    Zborowska, E.3    Willson, J.K.4    Berger, N.A.5
  • 134
    • 0027272622 scopus 로고
    • Glutathione levels and variability in breast tumors and normal tissue
    • Perry RR, Mazetta JA, Levin M, Barranco SC. Glutathione levels and variability in breast tumors and normal tissue. Cancer 1993; 72: 783-787.
    • (1993) Cancer , vol.72 , pp. 783-787
    • Perry, R.R.1    Mazetta, J.A.2    Levin, M.3    Barranco, S.C.4
  • 137
    • 0033568661 scopus 로고    scopus 로고
    • Repression of gene expression by oxidative stress
    • Morel Y, Barouki R. Repression of gene expression by oxidative stress. Biochem J 1999; 342: 481-496.
    • (1999) Biochem J , vol.342 , pp. 481-496
    • Morel, Y.1    Barouki, R.2
  • 138
    • 0029927983 scopus 로고    scopus 로고
    • Induction of the mammalian stress response gene GADD153 by oxidative stress: Role of AP-1 element
    • Guyton KZ, Xu Q, Holbrook NJ. Induction of the mammalian stress response gene GADD153 by oxidative stress: role of AP-1 element. Biochem J 1996; 314: 547-554.
    • (1996) Biochem J , vol.314 , pp. 547-554
    • Guyton, K.Z.1    Xu, Q.2    Holbrook, N.J.3
  • 139
    • 0029990552 scopus 로고    scopus 로고
    • Role of oxidants and antioxidants in the induction of AP-1, NF-kappaB, and glutathione S-transferase gene expression
    • Pinkus R, Weiner LM, Daniel V. Role of oxidants and antioxidants in the induction of AP-1, NF-kappaB, and glutathione S-transferase gene expression. J Biol Chem 1996; 271: 13422-13429.
    • (1996) J Biol Chem , vol.271 , pp. 13422-13429
    • Pinkus, R.1    Weiner, L.M.2    Daniel, V.3
  • 140
    • 0000128590 scopus 로고    scopus 로고
    • Inhibition of AP-1 DNA binding by nitric oxide involving conserved cysteine residues in Jun and Fos
    • Nikitovic D, Holmgren A, Spyrou G. Inhibition of AP-1 DNA binding by nitric oxide involving conserved cysteine residues in Jun and Fos. Biochem Biophys Res Commun 1998; 242: 109-112.
    • (1998) Biochem Biophys Res Commun , vol.242 , pp. 109-112
    • Nikitovic, D.1    Holmgren, A.2    Spyrou, G.3
  • 141
    • 0030936568 scopus 로고    scopus 로고
    • AP-1 transcriptional activity is regulated by a direct association between thioredoxin and Ref-1
    • Hirota K, Matsui M, Iwata S, Nishiyama A, Mori K, Yodoi J. AP-1 transcriptional activity is regulated by a direct association between thioredoxin and Ref-1. Proc Natl Acad Sci USA 1997; 94: 3633-3638.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 3633-3638
    • Hirota, K.1    Matsui, M.2    Iwata, S.3    Nishiyama, A.4    Mori, K.5    Yodoi, J.6
  • 142
    • 0025049139 scopus 로고
    • High-affinity transport of glutathione is part of a multicomponent system essential for mitochondrial function
    • Martensson J, Lai JC, Meister A. High-affinity transport of glutathione is part of a multicomponent system essential for mitochondrial function. Proc Natl Acad Sci USA 1990; 87: 7185-7189.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 7185-7189
    • Martensson, J.1    Lai, J.C.2    Meister, A.3
  • 143
    • 0027379264 scopus 로고
    • Distribution of the monochlorobimane-glutathione conjugate between nucleus and cytosol in isolated hepatocytes
    • Briviba K, Fraser G, Sies H, Ketterer B. Distribution of the monochlorobimane-glutathione conjugate between nucleus and cytosol in isolated hepatocytes. Biochem J 1993; 294: 631-633.
    • (1993) Biochem J , vol.294 , pp. 631-633
    • Briviba, K.1    Fraser, G.2    Sies, H.3    Ketterer, B.4
  • 145
    • 0025024469 scopus 로고
    • Presence of a potent transcription activating sequence in the p53 protein
    • Fields S, Jang SK. Presence of a potent transcription activating sequence in the p53 protein. Science 1990; 249: 1046-1049.
    • (1990) Science , vol.249 , pp. 1046-1049
    • Fields, S.1    Jang, S.K.2
  • 147
    • 0032563191 scopus 로고    scopus 로고
    • Pyrrolidine dithiocarbamate prevents p53 activation and promotes p53 cysteine residue oxidation
    • Wu HH, Momand J. Pyrrolidine dithiocarbamate prevents p53 activation and promotes p53 cysteine residue oxidation. J Biol Chem 1998; 273: 18898-18905.
    • (1998) J Biol Chem , vol.273 , pp. 18898-18905
    • Wu, H.H.1    Momand, J.2
  • 148
    • 0032191655 scopus 로고    scopus 로고
    • Inhibition of p53-dependent apoptosis by the KIT tyrosine kinase: Regulation of mitochondrial permeability transition and reactive oxygen species generation
    • Lee JM. Inhibition of p53-dependent apoptosis by the KIT tyrosine kinase: regulation of mitochondrial permeability transition and reactive oxygen species generation. Oncogene 1998; 17: 1653-1662.
    • (1998) Oncogene , vol.17 , pp. 1653-1662
    • Lee, J.M.1
  • 149
    • 0024443522 scopus 로고
    • The spectrum of mutations generated by passage of a hydrogen peroxide damaged shuttle vector plasmid through a mammalian host
    • Moraes EC, Keyse SM, Pidoux M, Tyrrell RM. The spectrum of mutations generated by passage of a hydrogen peroxide damaged shuttle vector plasmid through a mammalian host. Nucleic Acids Res 1989; 17: 8301-8312.
    • (1989) Nucleic Acids Res , vol.17 , pp. 8301-8312
    • Moraes, E.C.1    Keyse, S.M.2    Pidoux, M.3    Tyrrell, R.M.4
  • 150
    • 0025122267 scopus 로고
    • Mutagenesis by hydrogen peroxide treatment of mammalian cells: A molecular analysis
    • Moraes EC, Keyse SM, Tyrrell RM. Mutagenesis by hydrogen peroxide treatment of mammalian cells: a molecular analysis. Carcinogenesis 1990; 11: 283-293.
    • (1990) Carcinogenesis , vol.11 , pp. 283-293
    • Moraes, E.C.1    Keyse, S.M.2    Tyrrell, R.M.3
  • 151
    • 0027194309 scopus 로고
    • Oxidative mechanisms in carcinogenesis
    • Guyton KZ, Kensler TW. Oxidative mechanisms in carcinogenesis. Br Med Bull 1993; 49: 523-544.
    • (1993) Br Med Bull , vol.49 , pp. 523-544
    • Guyton, K.Z.1    Kensler, T.W.2
  • 152
    • 0018195287 scopus 로고
    • The glutathione status of cells
    • Kosower NS, Kosower EM. The glutathione status of cells. Int Rev Cytol 1978; 54: 109-160.
    • (1978) Int Rev Cytol , vol.54 , pp. 109-160
    • Kosower, N.S.1    Kosower, E.M.2
  • 153
    • 0020597282 scopus 로고
    • Regulation of protein synthesis initiation in eucaryotes
    • Ochoa S. Regulation of protein synthesis initiation in eucaryotes. Arch Biochem Biophys 1983; 223: 325-349.
    • (1983) Arch Biochem Biophys , vol.223 , pp. 325-349
    • Ochoa, S.1
  • 154
    • 1842604189 scopus 로고
    • Glutathione export by human lymphoid cells: Depletion of glutathione by inhibition of its synthesis decreases export and increases sensitivity to irradiation
    • Dethmers JK, Meister A. Glutathione export by human lymphoid cells: depletion of glutathione by inhibition of its synthesis decreases export and increases sensitivity to irradiation. Proc Natl Acad Sci USA 1981; 78: 7492-7496.
    • (1981) Proc Natl Acad Sci USA , vol.78 , pp. 7492-7496
    • Dethmers, J.K.1    Meister, A.2
  • 155
    • 0025057333 scopus 로고
    • Glutathione content and growth in A549 human lung carcinoma cells
    • Kang YJ, Enger MD. Glutathione content and growth in A549 human lung carcinoma cells. Exp Cell Res 1990; 187: 177-179.
    • (1990) Exp Cell Res , vol.187 , pp. 177-179
    • Kang, Y.J.1    Enger, M.D.2
  • 156
    • 0023764824 scopus 로고
    • The molecular heterogeneity of protein kinase C and its implications for cellular regulation
    • Nishizuka Y. The molecular heterogeneity of protein kinase C and its implications for cellular regulation. Nature 1988; 334: 661-665.
    • (1988) Nature , vol.334 , pp. 661-665
    • Nishizuka, Y.1
  • 157
    • 0014865396 scopus 로고
    • Metastasis: Guantitative analysis of distribution and fate of tumor embolilabeled with 125 I-5-iodo-2′-deoxyuridine
    • Fidler IJ. Metastasis: guantitative analysis of distribution and fate of tumor embolilabeled with 125 I-5-iodo-2′-deoxyuridine. J Natl Cancer Inst 1970; 45: 773-782.
    • (1970) J Natl Cancer Inst , vol.45 , pp. 773-782
    • Fidler, I.J.1
  • 158
    • 0025083071 scopus 로고
    • Critical factors in the biology of human cancer metastasis: Twenty-eighth G. H. A. Clowes memorial award lecture
    • Fidler IJ. Critical factors in the biology of human cancer metastasis: twenty-eighth G. H. A. Clowes memorial award lecture. Cancer Res 1990; 50: 6130-6138.
    • (1990) Cancer Res , vol.50 , pp. 6130-6138
    • Fidler, I.J.1
  • 159
    • 0025256084 scopus 로고
    • Metastatic inefficiency
    • Weiss L. Metastatic inefficiency. Adv Cancer Res 1990; 54: 159-211.
    • (1990) Adv Cancer Res , vol.54 , pp. 159-211
    • Weiss, L.1
  • 160
    • 0026069593 scopus 로고
    • Direct in vitro lysis of metastatic tumor cells by cytokine-activated murine vascular endothelial cells
    • Li LM, Nicolson GL, Fidler IJ. Direct in vitro lysis of metastatic tumor cells by cytokine-activated murine vascular endothelial cells. Cancer Res 1991; 51: 245-254.
    • (1991) Cancer Res , vol.51 , pp. 245-254
    • Li, L.M.1    Nicolson, G.L.2    Fidler, I.J.3
  • 161
    • 0029871281 scopus 로고    scopus 로고
    • Role of Kupffer cells in arresting circulating tumor cells and controlling metastatic growth in the liver
    • Bayon LG, Izquierdo MA, Sirovich I, van Rooijen N, Beelen RH, Meijer S. Role of Kupffer cells in arresting circulating tumor cells and controlling metastatic growth in the liver. Hepatology 1996; 23: 1224-1231.
    • (1996) Hepatology , vol.23 , pp. 1224-1231
    • Bayon, L.G.1    Izquierdo, M.A.2    Sirovich, I.3    Van Rooijen, N.4    Beelen, R.H.5    Meijer, S.6
  • 162
    • 0030987804 scopus 로고    scopus 로고
    • Sinusoidal endothelium release of hydrogen peroxide enhances very late antigen-4-mediated melanoma cell adherence and tumor cytotoxicity during interleukin-1 promotion of hepatic melanoma metastasis in mice
    • Anasagasti MJ, Alvarez A, Martin JJ, Mendoza L, Vidal-Vanaclocha F. Sinusoidal endothelium release of hydrogen peroxide enhances very late antigen-4-mediated melanoma cell adherence and tumor cytotoxicity during interleukin-1 promotion of hepatic melanoma metastasis in mice. Hepatology 1997; 25: 840-846.
    • (1997) Hepatology , vol.25 , pp. 840-846
    • Anasagasti, M.J.1    Alvarez, A.2    Martin, J.J.3    Mendoza, L.4    Vidal-Vanaclocha, F.5
  • 163
    • 0034094341 scopus 로고    scopus 로고
    • Interactions between cancer cells and the endothelium in metastasis
    • Orr FW, Wang HH, Lafrenie RM, Scherbarth S, Nance DM. Interactions between cancer cells and the endothelium in metastasis. J Pathol 2000; 190: 310-329.
    • (2000) J Pathol , vol.190 , pp. 310-329
    • Orr, F.W.1    Wang, H.H.2    Lafrenie, R.M.3    Scherbarth, S.4    Nance, D.M.5
  • 164
    • 0000629930 scopus 로고
    • Selection of successive tumour lines for metastasis
    • Fidler IJ. Selection of successive tumour lines for metastasis. Nat New Biol 1973; 242: 148-149.
    • (1973) Nat New Biol , vol.242 , pp. 148-149
    • Fidler, I.J.1
  • 165
    • 0017138981 scopus 로고
    • Organ selectivity for implantation survival and growth of B16 melanoma variant tumor lines
    • Fidler IJ, Nicolson GL. Organ selectivity for implantation survival and growth of B16 melanoma variant tumor lines. J Natl Cancer Inst 1976; 57: 1199-1202.
    • (1976) J Natl Cancer Inst , vol.57 , pp. 1199-1202
    • Fidler, I.J.1    Nicolson, G.L.2
  • 166
    • 0031937846 scopus 로고    scopus 로고
    • Mannose receptor-mediated endothelial cell activation contributes to B16 melanoma cell adhesion and metastasis in liver
    • Mendoza L, Olaso E, Anasagasti MJ, Fuentes AM, Vidal-Vanaclocha F. Mannose receptor-mediated endothelial cell activation contributes to B16 melanoma cell adhesion and metastasis in liver. J Cell Physiol 1998; 174: 322-330.
    • (1998) J Cell Physiol , vol.174 , pp. 322-330
    • Mendoza, L.1    Olaso, E.2    Anasagasti, M.J.3    Fuentes, A.M.4    Vidal-Vanaclocha, F.5
  • 168
    • 0023023315 scopus 로고
    • Increased superoxide anion release from human endothelial cells in response to cytokines
    • Matsubara T, Ziff M. Increased superoxide anion release from human endothelial cells in response to cytokines. J Immunol 1986; 137: 3295-3298.
    • (1986) J Immunol , vol.137 , pp. 3295-3298
    • Matsubara, T.1    Ziff, M.2
  • 169
    • 0026719323 scopus 로고
    • Lipopolysaccharide treatment of rats alters antigen expression and oxidative metabolism in hepatic macrophages and endothelial cells
    • McCloskey TW, Todaro JA, Laskin DL. Lipopolysaccharide treatment of rats alters antigen expression and oxidative metabolism in hepatic macrophages and endothelial cells. Hepatology 1992; 16: 191-203.
    • (1992) Hepatology , vol.16 , pp. 191-203
    • McCloskey, T.W.1    Todaro, J.A.2    Laskin, D.L.3
  • 170
    • 0029919620 scopus 로고    scopus 로고
    • Interleukin-1-mediated H2O2 production by hepatic sinusoidal endothelium in response to B16 melanoma cell adhesion
    • Anasagasti MJ, Alvarez A, Avivi C, Vidal-Vanaclocha F. Interleukin-1-mediated H2O2 production by hepatic sinusoidal endothelium in response to B16 melanoma cell adhesion. J Cell Physiol 1996; 167: 314-323.
    • (1996) J Cell Physiol , vol.167 , pp. 314-323
    • Anasagasti, M.J.1    Alvarez, A.2    Avivi, C.3    Vidal-Vanaclocha, F.4
  • 171
    • 0028351137 scopus 로고
    • Reactive oxygen species rapidly increase endothelial ICAM-1 ability to bind neutrophils without detectable upregulation
    • Sellak H, Franzini E, Hakim J, Pasquier C. Reactive oxygen species rapidly increase endothelial ICAM-1 ability to bind neutrophils without detectable upregulation. Blood 1994; 83: 2669-2677.
    • (1994) Blood , vol.83 , pp. 2669-2677
    • Sellak, H.1    Franzini, E.2    Hakim, J.3    Pasquier, C.4
  • 172
    • 0027365599 scopus 로고
    • Vascular cell adhesion molecule-1 (VCAM-1) gene transcription and expression are egulated through an antioxidant-sensitive mechanism in human vascular endothelial cells
    • Marui N, Offermann MK, Swerlick R, Kunsch C, Rosen CA, Ahmad M, Alexander RW, Medford RM. Vascular cell adhesion molecule-1 (VCAM-1) gene transcription and expression are egulated through an antioxidant-sensitive mechanism in human vascular endothelial cells. J Clin Invest 1993; 92: 1866-1874.
    • (1993) J Clin Invest , vol.92 , pp. 1866-1874
    • Marui, N.1    Offermann, M.K.2    Swerlick, R.3    Kunsch, C.4    Rosen, C.A.5    Ahmad, M.6    Alexander, R.W.7    Medford, R.M.8
  • 173
    • 0034667417 scopus 로고    scopus 로고
    • B16 melanoma cell arrest in the mouse liver induces nitric oxide release and sinusoidal cytotoxicity: A natural hepatic defense against metastasis
    • Wang HH, McIntosh AR, Hasinoff BB, Rector ES, Ahmed N, Nance DM, Orr FW. B16 melanoma cell arrest in the mouse liver induces nitric oxide release and sinusoidal cytotoxicity: a natural hepatic defense against metastasis. Cancer Res 2000; 60: 5862-5869.
    • (2000) Cancer Res , vol.60 , pp. 5862-5869
    • Wang, H.H.1    McIntosh, A.R.2    Hasinoff, B.B.3    Rector, E.S.4    Ahmed, N.5    Nance, D.M.6    Orr, F.W.7
  • 175
    • 0031794120 scopus 로고    scopus 로고
    • Macrophage-derived nitric oxide induces apoptosis of rat hepatoma cells in vivo
    • Nishikawa M, Sato EF, Kuroki T, Utsumi K, Inoue M. Macrophage-derived nitric oxide induces apoptosis of rat hepatoma cells in vivo. Hepatology 1998; 28: 1474-1480.
    • (1998) Hepatology , vol.28 , pp. 1474-1480
    • Nishikawa, M.1    Sato, E.F.2    Kuroki, T.3    Utsumi, K.4    Inoue, M.5
  • 178
    • 0027451972 scopus 로고
    • Cytotoxicity of nitric oxide in Fu5 rat hepatoma cells: Evidence for co-operative action with hydrogen peroxide
    • Ioannidis I, de Groot H. Cytotoxicity of nitric oxide in Fu5 rat hepatoma cells: evidence for co-operative action with hydrogen peroxide. Biochem J 1993; 296: 341-345.
    • (1993) Biochem J , vol.296 , pp. 341-345
    • Ioannidis, I.1    De Groot, H.2
  • 179
    • 0033561507 scopus 로고    scopus 로고
    • Reactive nitrogen and oxygen radicals formed during hepatic ischemia-reperfusion kill weakly metastatic colorectal cancer cells
    • Jessup JM, Battle P, Waller H, Edmiston KH, Stolz DB, Watkins SC, Locker J, Skena K. Reactive nitrogen and oxygen radicals formed during hepatic ischemia-reperfusion kill weakly metastatic colorectal cancer cells. Cancer Res 1999; 59: 1825-1829.
    • (1999) Cancer Res , vol.59 , pp. 1825-1829
    • Jessup, J.M.1    Battle, P.2    Waller, H.3    Edmiston, K.H.4    Stolz, D.B.5    Watkins, S.C.6    Locker, J.7    Skena, K.8
  • 181
    • 0029918676 scopus 로고    scopus 로고
    • The chemistry and tumoricidal activity of nitric oxide/hydrogen peroxide and the implications to cell resistance/susceptibility
    • Farias-Eisner R, Chaudhuri G, Aeberhard E, Fukuto JM. The chemistry and tumoricidal activity of nitric oxide/hydrogen peroxide and the implications to cell resistance/susceptibility. J Biol Chem 1996; 271: 6144-6151.
    • (1996) J Biol Chem , vol.271 , pp. 6144-6151
    • Farias-Eisner, R.1    Chaudhuri, G.2    Aeberhard, E.3    Fukuto, J.M.4
  • 182
    • 0034663296 scopus 로고    scopus 로고
    • The role of oxygen and reduced oxygen species in nitric oxide-mediated cytotoxicity: Studies in the yeast Saccharomyces cerevisiae model system
    • Chiang KT, Switzer CH, Akali KO, Fukuto JM. The role of oxygen and reduced oxygen species in nitric oxide-mediated cytotoxicity: studies in the yeast Saccharomyces cerevisiae model system. Toxicol Appl Pharmacol 2000; 167: 30-36.
    • (2000) Toxicol Appl Pharmacol , vol.167 , pp. 30-36
    • Chiang, K.T.1    Switzer, C.H.2    Akali, K.O.3    Fukuto, J.M.4
  • 184
    • 0030837370 scopus 로고    scopus 로고
    • Nitric oxide attenuates hydrogen peroxide-mediated injury to porcine pulmonary artery endothelial cells
    • Gupta MP, Evanoff V, Hart CM. Nitric oxide attenuates hydrogen peroxide-mediated injury to porcine pulmonary artery endothelial cells. Am J Physiol 1997; 272: L1133-1141.
    • (1997) Am J Physiol , vol.272
    • Gupta, M.P.1    Evanoff, V.2    Hart, C.M.3
  • 185
    • 0032694302 scopus 로고    scopus 로고
    • The broad spectrum of responses to oxidants in proliferating cells: A new paradigm for oxidative stress
    • Davies KJ. The broad spectrum of responses to oxidants in proliferating cells: a new paradigm for oxidative stress. IUBMB Life 1999; 48: 41-47.
    • (1999) IUBMB Life , vol.48 , pp. 41-47
    • Davies, K.J.1
  • 186
    • 0038629734 scopus 로고
    • Molecular biology of nitric oxide synthases
    • Stamler JS, Gross SS, Moncada S, Higgs EA, Eds. London: Portland Press
    • Han J, Stamler JS, Li H, Griffith OW. Molecular biology of nitric oxide synthases. In Stamler JS, Gross SS, Moncada S, Higgs EA, Eds. The Biology of Nitric Oxide. Pp 84-93. London: Portland Press, 1995.
    • (1995) The Biology of Nitric Oxide , pp. 84-93
    • Han, J.1    Stamler, J.S.2    Li, H.3    Griffith, O.W.4
  • 190
    • 0037012040 scopus 로고    scopus 로고
    • Mitochondrial dysfunction is an essential step for killing of non-small cell lung carcinomas resistant to conventional treatment
    • Joseph B, Marchetti P, Formstecher P, Kroemer G, Lewensohn R, Zhivotovsky B. Mitochondrial dysfunction is an essential step for killing of non-small cell lung carcinomas resistant to conventional treatment. Oncogene 2002; 21: 65-77.
    • (2002) Oncogene , vol.21 , pp. 65-77
    • Joseph, B.1    Marchetti, P.2    Formstecher, P.3    Kroemer, G.4    Lewensohn, R.5    Zhivotovsky, B.6
  • 191
    • 0033582533 scopus 로고    scopus 로고
    • Mitochondrial phospholipid hydroperoxide glutathione peroxidase plays a major role in preventing oxidative injury to cells
    • Arai M, Imai H, Koumura T, Yoshida M, Emoto K, Umeda M, Chiba N, Nakagawa Y. Mitochondrial phospholipid hydroperoxide glutathione peroxidase plays a major role in preventing oxidative injury to cells. J Biol Chem 1999; 274: 4924-4933.
    • (1999) J Biol Chem , vol.274 , pp. 4924-4933
    • Arai, M.1    Imai, H.2    Koumura, T.3    Yoshida, M.4    Emoto, K.5    Umeda, M.6    Chiba, N.7    Nakagawa, Y.8
  • 193
    • 0032513362 scopus 로고    scopus 로고
    • Activation of the OxyR transcription factor by reversible disulfide bond formation
    • Zheng M, Aslund F, Storz G. Activation of the OxyR transcription factor by reversible disulfide bond formation. Science 1998; 279: 1718-1721.
    • (1998) Science , vol.279 , pp. 1718-1721
    • Zheng, M.1    Aslund, F.2    Storz, G.3
  • 194
    • 0029760957 scopus 로고    scopus 로고
    • Redox regulation of transcriptional activators
    • Sun Y, Oberley LW. Redox regulation of transcriptional activators. Free Radic Biol Med 1996; 21: 335-348.
    • (1996) Free Radic Biol Med , vol.21 , pp. 335-348
    • Sun, Y.1    Oberley, L.W.2
  • 195
    • 0035227318 scopus 로고    scopus 로고
    • Mechanism and significance of increased glutathione level in human hepatocellular carcinoma and liver regeneration
    • Huang ZZ, Chen C, Zeng Z, Yang H, Oh J, Chen L, Lu SC. Mechanism and significance of increased glutathione level in human hepatocellular carcinoma and liver regeneration. FASEB J 2001; 15: 19-21.
    • (2001) FASEB J , vol.15 , pp. 19-21
    • Huang, Z.Z.1    Chen, C.2    Zeng, Z.3    Yang, H.4    Oh, J.5    Chen, L.6    Lu, S.C.7
  • 197
    • 0025738538 scopus 로고
    • Hormone-mediated down-regulation of hepatic glutathione synthesis in the rat
    • Lu SC, Kuhlenkamp J, Garcia-Ruiz C, Kaplowitz N. Hormone-mediated down-regulation of hepatic glutathione synthesis in the rat. J Clin Invest 1991; 88: 260-269.
    • (1991) J Clin Invest , vol.88 , pp. 260-269
    • Lu, S.C.1    Kuhlenkamp, J.2    Garcia-Ruiz, C.3    Kaplowitz, N.4
  • 198
    • 0029848066 scopus 로고    scopus 로고
    • Regulation of gamma-glutamylcysteine synthetase by protein phos-phorylation
    • Sun WM, Huang ZZ, Lu SC. Regulation of gamma-glutamylcysteine synthetase by protein phos-phorylation. Biochem J 1996; 320 (Pt 1): 321-328.
    • (1996) Biochem J , vol.320 , Issue.1 PART , pp. 321-328
    • Sun, W.M.1    Huang, Z.Z.2    Lu, S.C.3
  • 200
    • 0026445242 scopus 로고
    • Cancer cell interactions with injured or activated endothelium
    • Lafrenie R, Shaughnessy SG, Orr FW. Cancer cell interactions with injured or activated endothelium. Cancer Metastasis Rev 1992; 11: 377-388.
    • (1992) Cancer Metastasis Rev , vol.11 , pp. 377-388
    • Lafrenie, R.1    Shaughnessy, S.G.2    Orr, F.W.3
  • 201
    • 0033815334 scopus 로고    scopus 로고
    • Nitrosation and oxidation in the regulation of gene expression
    • Marshall HE, Merchant K, Stamler JS. Nitrosation and oxidation in the regulation of gene expression. FASEB J 2000; 14: 1889-1900.
    • (2000) FASEB J , vol.14 , pp. 1889-1900
    • Marshall, H.E.1    Merchant, K.2    Stamler, J.S.3
  • 202
    • 0029102925 scopus 로고
    • Glutathione and related enzymes in tumor progression and metastases of human melanoma
    • Schadendorf D, Jurgovsky K, Kohlmus CM, Czarnetzki BM. Glutathione and related enzymes in tumor progression and metastases of human melanoma. J Invest Dermatol 1995; 105: 109-112.
    • (1995) J Invest Dermatol , vol.105 , pp. 109-112
    • Schadendorf, D.1    Jurgovsky, K.2    Kohlmus, C.M.3    Czarnetzki, B.M.4
  • 203
    • 0028242382 scopus 로고
    • Selective toxicity of buthionine sulfoximine (BSO) to melanoma cells in vitro and in vivo
    • Revesz L, Edgren MR, Wainson AA. Selective toxicity of buthionine sulfoximine (BSO) to melanoma cells in vitro and in vivo. Int J Radiat Oncol Biol Phys 1994; 29: 403-406.
    • (1994) Int J Radiat Oncol Biol Phys , vol.29 , pp. 403-406
    • Revesz, L.1    Edgren, M.R.2    Wainson, A.A.3
  • 204
    • 0025767987 scopus 로고
    • Induction of glutathione content in murine melanocytes after transformation with c-H-ras oncogene
    • Thrall BD, Meadows GG. Induction of glutathione content in murine melanocytes after transformation with c-H-ras oncogene. Carcinogenesis 1991; 12: 1319-1323.
    • (1991) Carcinogenesis , vol.12 , pp. 1319-1323
    • Thrall, B.D.1    Meadows, G.G.2
  • 206
    • 0021905244 scopus 로고
    • Hepatic thiol and glutathione efflux under the influence of vasopressin, phenylephrine and adrenaline
    • Sies H, Graf P. Hepatic thiol and glutathione efflux under the influence of vasopressin, phenylephrine and adrenaline. Biochem J 1985; 2: 545-549.
    • (1985) Biochem J , vol.2 , pp. 545-549
    • Sies, H.1    Graf, P.2
  • 207
    • 0030911923 scopus 로고    scopus 로고
    • Interleukin-2 increases intracellular glutathione levels and reverses the growth inhibiting effects of cyclophosphamide on B16 melanoma cells
    • Palomares T, Alonso-Varona A, Alvarez A, Castro B, Calle Y, Bilbao P. Interleukin-2 increases intracellular glutathione levels and reverses the growth inhibiting effects of cyclophosphamide on B16 melanoma cells. Clin Exp Metastasis 1997; 15: 329-337.
    • (1997) Clin Exp Metastasis , vol.15 , pp. 329-337
    • Palomares, T.1    Alonso-Varona, A.2    Alvarez, A.3    Castro, B.4    Calle, Y.5    Bilbao, P.6
  • 208
    • 0025972103 scopus 로고
    • Historical aspects of glutathione and cancer chemotherapy
    • Mistry P, Harrap KR. Historical aspects of glutathione and cancer chemotherapy. Pharmacol Ther 1991; 49: 125-132.
    • (1991) Pharmacol Ther , vol.49 , pp. 125-132
    • Mistry, P.1    Harrap, K.R.2
  • 209
    • 33744979651 scopus 로고    scopus 로고
    • Glutathione depletion by buthionine sulfoximine induces DNA deletions in mice
    • Reliene R, Schiestl RH. Glutathione depletion by buthionine sulfoximine induces DNA deletions in mice. Carcinogenesis 2005;
    • (2005) Carcinogenesis
    • Reliene, R.1    Schiestl, R.H.2
  • 211
    • 0030754701 scopus 로고    scopus 로고
    • Resistance to radiation-induced apoptosis in Bcl-2-expressing cells is reversed by depleting cellular thiols
    • Mirkovic N, Voehringer DW, Story MD, McConkey DJ, McDonnell TJ, Meyn RE. Resistance to radiation-induced apoptosis in Bcl-2-expressing cells is reversed by depleting cellular thiols. Oncogene 1997; 15: 1461-1470.
    • (1997) Oncogene , vol.15 , pp. 1461-1470
    • Mirkovic, N.1    Voehringer, D.W.2    Story, M.D.3    McConkey, D.J.4    McDonnell, T.J.5    Meyn, R.E.6
  • 212
    • 0036673665 scopus 로고    scopus 로고
    • Glutathione depletion enforces the mitochondrial permeability transition and causes cell death in Bcl-2 overexpressing HL60 cells
    • Armstrong JS, Jones DP. Glutathione depletion enforces the mitochondrial permeability transition and causes cell death in Bcl-2 overexpressing HL60 cells. FASEB J 2002; 16: 1263-1265.
    • (2002) FASEB J , vol.16 , pp. 1263-1265
    • Armstrong, J.S.1    Jones, D.P.2
  • 214
    • 0036087028 scopus 로고    scopus 로고
    • Role of Bcl-2 family of proteins in malignancy
    • Baliga BC, Kumar S. Role of Bcl-2 family of proteins in malignancy. Hematol Oncol 2002; 20: 63-74.
    • (2002) Hematol Oncol , vol.20 , pp. 63-74
    • Baliga, B.C.1    Kumar, S.2
  • 216
    • 0032476609 scopus 로고    scopus 로고
    • Fas and Fas ligand interactions suppress melanoma lung metastasis
    • Owen-Schaub LB, van Golen KL, Hill LL, Price JE. Fas and Fas ligand interactions suppress melanoma lung metastasis. J Exp Med 1998; 188: 1717-1723.
    • (1998) J Exp Med , vol.188 , pp. 1717-1723
    • Owen-Schaub, L.B.1    Van Golen, K.L.2    Hill, L.L.3    Price, J.E.4
  • 217
  • 219
    • 0037050735 scopus 로고    scopus 로고
    • Upregulation of Bcl-2 is involved in the mediation of chemotherapy resistance in human small cell lung cancer cell lines
    • Sartorius UA, Krammer PH. Upregulation of Bcl-2 is involved in the mediation of chemotherapy resistance in human small cell lung cancer cell lines. Int J Cancer 2002; 97: 584-592.
    • (2002) Int J Cancer , vol.97 , pp. 584-592
    • Sartorius, U.A.1    Krammer, P.H.2
  • 220
    • 0036467477 scopus 로고    scopus 로고
    • Apoptosis and tumourigenesis
    • Hickman JA. Apoptosis and tumourigenesis. Curr Opin Genet Dev 2002; 12: 67-72.
    • (2002) Curr Opin Genet Dev , vol.12 , pp. 67-72
    • Hickman, J.A.1
  • 222
    • 0029782288 scopus 로고    scopus 로고
    • Down-regulation of apoptosis-related bcl-2 but not bcl-xL or bax proteins in multidrug-resistant MCF-7/Adr human breast cancer cells
    • Ogretmen B, Safa AR. Down-regulation of apoptosis-related bcl-2 but not bcl-xL or bax proteins in multidrug-resistant MCF-7/Adr human breast cancer cells. Int J Cancer 1996; 67: 608-614.
    • (1996) Int J Cancer , vol.67 , pp. 608-614
    • Ogretmen, B.1    Safa, A.R.2
  • 223
    • 0032525112 scopus 로고    scopus 로고
    • The Ig heavy chain 3′ end confers a posttranscriptional processing advantage to Bcl-2IgH fusion RNA in t(14;18) lymphoma
    • Petrovic AS, Young RL, Hilgarth B, Ambros P, Korsmeyer SJ, Jaeger U. The Ig heavy chain 3′ end confers a posttranscriptional processing advantage to Bcl-2IgH fusion RNA in t(14;18) lymphoma. Blood 1998; 91: 3952-3961.
    • (1998) Blood , vol.91 , pp. 3952-3961
    • Petrovic, A.S.1    Young, R.L.2    Hilgarth, B.3    Ambros, P.4    Korsmeyer, S.J.5    Jaeger, U.6
  • 224
    • 0033957550 scopus 로고    scopus 로고
    • A conserved AU-rich element in the 3′ untranslated region of bcl-2 mRNA is endowed with a destabilizing function that is involved in bcl-2 down-regulation during apoptosis
    • Schiavone N, Rosini P, Quattrone A, Donnini M, Lapucci A, Citti L, Bevilacqua A, Nicolin A, Capaccioli S. A conserved AU-rich element in the 3′ untranslated region of bcl-2 mRNA is endowed with a destabilizing function that is involved in bcl-2 down-regulation during apoptosis. FASEB J 2000; 14: 174-184.
    • (2000) FASEB J , vol.14 , pp. 174-184
    • Schiavone, N.1    Rosini, P.2    Quattrone, A.3    Donnini, M.4    Lapucci, A.5    Citti, L.6    Bevilacqua, A.7    Nicolin, A.8    Capaccioli, S.9
  • 225
    • 0030678131 scopus 로고    scopus 로고
    • Evidence that the multidrug resistance protein (MRP) functions as a co-transporter of glutathione and natural product toxins
    • Rappa G, Lorico A, Flavell RA, Sartorelli AC. Evidence that the multidrug resistance protein (MRP) functions as a co-transporter of glutathione and natural product toxins. Cancer Res 1997; 57: 5232-5237.
    • (1997) Cancer Res , vol.57 , pp. 5232-5237
    • Rappa, G.1    Lorico, A.2    Flavell, R.A.3    Sartorelli, A.C.4
  • 226
    • 0028793942 scopus 로고
    • Expression of multidrug resistance-associated protein (MRP) and multidrug resistance (MDR1) genes in cute myeloid leukemia
    • Zhou DC, Zittoun R, Marie JP. Expression of multidrug resistance-associated protein (MRP) and multidrug resistance (MDR1) genes in cute myeloid leukemia. Leukemia 1995; 9: 1661-1666.
    • (1995) Leukemia , vol.9 , pp. 1661-1666
    • Zhou, D.C.1    Zittoun, R.2    Marie, J.P.3
  • 227
    • 23644450562 scopus 로고    scopus 로고
    • Combined effects of GSTP1 and MRP1 in melanoma drug resistance
    • Depeille P, Cuq P, Passagne I, Evrard A, Vian L. Combined effects of GSTP1 and MRP1 in melanoma drug resistance. Br J Cancer 2005; 93: 216-223.
    • (2005) Br J Cancer , vol.93 , pp. 216-223
    • Depeille, P.1    Cuq, P.2    Passagne, I.3    Evrard, A.4    Vian, L.5
  • 228
    • 0029029449 scopus 로고
    • Regulation by glutathione of drug transport in multidrug-resistant human lung tumour cell lines overexpressing multidrug resistance-associated protein
    • Versantvoort CH, Broxterman HJ, Bagrij T, Scheper RJ, Twentyman PR. Regulation by glutathione of drug transport in multidrug-resistant human lung tumour cell lines overexpressing multidrug resistance-associated protein. Br J Cancer 1995; 72: 82-89.
    • (1995) Br J Cancer , vol.72 , pp. 82-89
    • Versantvoort, C.H.1    Broxterman, H.J.2    Bagrij, T.3    Scheper, R.J.4    Twentyman, P.R.5
  • 229
  • 230
    • 0032936619 scopus 로고    scopus 로고
    • Control of CFTR channel gating by phosphorylation and nucleotide hydrolysis
    • Gadsby DC, Nairn AC. Control of CFTR channel gating by phosphorylation and nucleotide hydrolysis. Physiol Rev 1999; 79(1 suppl): S77-107.
    • (1999) Physiol Rev , vol.79 , Issue.1 SUPPL.
    • Gadsby, D.C.1    Nairn, A.C.2
  • 231
    • 0029127312 scopus 로고
    • Basal expression of the cystic fibrosis transmembrane conductance regulator gene is dependent on protein kinase A activity
    • McDonald RA, Matthews RP, Idzerda RL, McKnight GS. Basal expression of the cystic fibrosis transmembrane conductance regulator gene is dependent on protein kinase A activity. Proc Natl Acad Sci USA 1995; 92: 7560-7564.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 7560-7564
    • McDonald, R.A.1    Matthews, R.P.2    Idzerda, R.L.3    McKnight, G.S.4
  • 232
    • 0035882764 scopus 로고    scopus 로고
    • Verapamil-stimulated glutathione transport by the multidrug resistance-associated protein (MRP1) in leukaemia cells
    • Cullen KV, Davey RA, Davey MW. Verapamil-stimulated glutathione transport by the multidrug resistance-associated protein (MRP1) in leukaemia cells. Biochem Pharmacol 2001; 62: 417-424.
    • (2001) Biochem Pharmacol , vol.62 , pp. 417-424
    • Cullen, K.V.1    Davey, R.A.2    Davey, M.W.3
  • 233
    • 0034012019 scopus 로고    scopus 로고
    • Verapamil stimulates glutathione transport by the 190-kDa multidrug resistance protein 1 (MRP1)
    • Loe DW, Deeley RG, Cole SP. Verapamil stimulates glutathione transport by the 190-kDa multidrug resistance protein 1 (MRP1). J Pharmacol Exp Ther 2000; 293: 530-538.
    • (2000) J Pharmacol Exp Ther , vol.293 , pp. 530-538
    • Loe, D.W.1    Deeley, R.G.2    Cole, S.P.3
  • 234
    • 0019430432 scopus 로고
    • Overcoming of vincristine resistance in P388 leukemia in vivo and in vitro through enhanced cytotoxicity of vincristine and vinblastine by verapamil
    • Tsuruo T, Iida H, Tsukagoshi S, Sakurai Y. Overcoming of vincristine resistance in P388 leukemia in vivo and in vitro through enhanced cytotoxicity of vincristine and vinblastine by verapamil. Cancer Res 1981; 41: 1967-1972.
    • (1981) Cancer Res , vol.41 , pp. 1967-1972
    • Tsuruo, T.1    Iida, H.2    Tsukagoshi, S.3    Sakurai, Y.4
  • 235
    • 0027136660 scopus 로고
    • Clinical trials of agents that reverse multidrug resistance. A literature review
    • Raderer M, Scheithauer W. Clinical trials of agents that reverse multidrug resistance. A literature review. Cancer 1993; 72: 3553-3563.
    • (1993) Cancer , vol.72 , pp. 3553-3563
    • Raderer, M.1    Scheithauer, W.2
  • 236
    • 0028168829 scopus 로고
    • Interaction of gamma-glutamyl transpeptidase with acivicin
    • Stole E, Smith TK, Manning JM, Meister A. Interaction of gamma-glutamyl transpeptidase with acivicin. J Biol Chem 1994; 269: 21435-21439.
    • (1994) J Biol Chem , vol.269 , pp. 21435-21439
    • Stole, E.1    Smith, T.K.2    Manning, J.M.3    Meister, A.4
  • 237
    • 0036850631 scopus 로고    scopus 로고
    • Potential roles of antisense oligonucleotides in cancer therapy. The example of Bcl-2 antisense oligonucleotides
    • Dias N, Stein CA. Potential roles of antisense oligonucleotides in cancer therapy. The example of Bcl-2 antisense oligonucleotides. Eur J Pharm Biopharm 2002; 54: 263-269.
    • (2002) Eur J Pharm Biopharm , vol.54 , pp. 263-269
    • Dias, N.1    Stein, C.A.2
  • 238
    • 0032785072 scopus 로고    scopus 로고
    • Targeting bcl-2 gene to delay androgen-independent progression and enhance chemosensitivity in prostate cancer using antisense bcl-2 oligodeoxynucleotides
    • Gleave ME, Miayake H, Goldie J, Nelson C, Tolcher A. Targeting bcl-2 gene to delay androgen-independent progression and enhance chemosensitivity in prostate cancer using antisense bcl-2 oligodeoxynucleotides. Urology 1999; 54: 36-46.
    • (1999) Urology , vol.54 , pp. 36-46
    • Gleave, M.E.1    Miayake, H.2    Goldie, J.3    Nelson, C.4    Tolcher, A.5
  • 239
    • 0033567003 scopus 로고    scopus 로고
    • Antisense Bcl-2 oligodeoxynucleotides inhibit progression to androgen-independence after castration in the Shionogi tumor model
    • Miyake H, Tolcher A, Gleave ME. Antisense Bcl-2 oligodeoxynucleotides inhibit progression to androgen-independence after castration in the Shionogi tumor model. Cancer Res 1999; 59: 4030-4034.
    • (1999) Cancer Res , vol.59 , pp. 4030-4034
    • Miyake, H.1    Tolcher, A.2    Gleave, M.E.3
  • 240
    • 0031664988 scopus 로고    scopus 로고
    • Synergistic cytotoxicity of bcl-2 anti-sense oligodeoxynucleotides and etoposide, doxorubicin and cisplatin on small-cell lung cancer cell lines
    • Zangemeister-Wittke U, Schenker T, Luedke GH, Stahel RA. Synergistic cytotoxicity of bcl-2 anti-sense oligodeoxynucleotides and etoposide, doxorubicin and cisplatin on small-cell lung cancer cell lines. Br J Cancer 1998; 78: 1035-1042.
    • (1998) Br J Cancer , vol.78 , pp. 1035-1042
    • Zangemeister-Wittke, U.1    Schenker, T.2    Luedke, G.H.3    Stahel, R.A.4
  • 241
    • 0034083410 scopus 로고    scopus 로고
    • Eradication of human non-Hodgkin's lymphoma in SCID mice by BCL-2 antisense oligonucleotides combined with low-dose cyclophosphamide
    • Klasa RJ, Bally MB, Ng R, Goldie JH, Gascoyne RD, Wong FM. Eradication of human non-Hodgkin's lymphoma in SCID mice by BCL-2 antisense oligonucleotides combined with low-dose cyclophosphamide. Clin Cancer Res 2000; 6: 2492-2500.
    • (2000) Clin Cancer Res , vol.6 , pp. 2492-2500
    • Klasa, R.J.1    Bally, M.B.2    Ng, R.3    Goldie, J.H.4    Gascoyne, R.D.5    Wong, F.M.6
  • 242
    • 1642618055 scopus 로고    scopus 로고
    • Molecular and pharmacokinetic properties associated with the therapeutics of bcl-2 antisense oligonucleotide G3139 combined with free and liposomal doxorubicin
    • Lopes de Menezes DE, Hudon N, McIntosh N, Mayer LD. Molecular and pharmacokinetic properties associated with the therapeutics of bcl-2 antisense oligonucleotide G3139 combined with free and liposomal doxorubicin. Clin Cancer Res 2000; 6: 2891-2902.
    • (2000) Clin Cancer Res , vol.6 , pp. 2891-2902
    • Lopes De Menezes, D.E.1    Hudon, N.2    McIntosh, N.3    Mayer, L.D.4
  • 243
    • 0011369737 scopus 로고
    • Overcoming the multidrug resistance phenotype
    • De Vita VT Jr, Hellman S, Rosenberg SA, Eds. Philadelphia: J. B. Lippincott
    • Dalton WS. Overcoming the multidrug resistance phenotype. In De Vita VT Jr, Hellman S, Rosenberg SA, Eds. Cancer: Principles and Practice of Oncology. Pp 2655-2666. Philadelphia: J. B. Lippincott, 1993.
    • (1993) Cancer: Principles and Practice of Oncology , pp. 2655-2666
    • Dalton, W.S.1
  • 244
    • 0031757391 scopus 로고    scopus 로고
    • A Phase I and pharmacological study of the glutamine antagonist acivicin with the amino acid solution aminosyn in patients with advanced solid malignancies
    • Hidalgo M, Rodriguez G, Kuhn JG, Brown T, Weiss G, MacGovren JP, Von Hoff DD, Rowinsky EK. A Phase I and pharmacological study of the glutamine antagonist acivicin with the amino acid solution aminosyn in patients with advanced solid malignancies. Clin Cancer Res 1998; 4: 2763-2770.
    • (1998) Clin Cancer Res , vol.4 , pp. 2763-2770
    • Hidalgo, M.1    Rodriguez, G.2    Kuhn, J.G.3    Brown, T.4    Weiss, G.5    MacGovren, J.P.6    Von Hoff, D.D.7    Rowinsky, E.K.8
  • 245
    • 0028951043 scopus 로고
    • Dormancy of micrometastases: Balanced proliferation and apoptosis in the presence of angiogenesis suppression
    • Holmgren L, O'Reilly MS, Folkman J. Dormancy of micrometastases: balanced proliferation and apoptosis in the presence of angiogenesis suppression. Nat Med 1995; 1: 149-153.
    • (1995) Nat Med , vol.1 , pp. 149-153
    • Holmgren, L.1    O'Reilly, M.S.2    Folkman, J.3
  • 246
    • 17144397637 scopus 로고    scopus 로고
    • Role of intracellular glutathione in cell sensitivity to the apoptosis induced by tumor necrosis factor {alpha}-related apoptosis-inducing ligand/anticancer drug combinations
    • Meurette O, Lefeuvre-Orfila L, Rebillard A, Lagadic-Gossmann D, Dimanche-Boitrel MT. Role of intracellular glutathione in cell sensitivity to the apoptosis induced by tumor necrosis factor {alpha}-related apoptosis-inducing ligand/anticancer drug combinations. Clin Cancer Res 2005; 11: 3075-3083.
    • (2005) Clin Cancer Res , vol.11 , pp. 3075-3083
    • Meurette, O.1    Lefeuvre-Orfila, L.2    Rebillard, A.3    Lagadic-Gossmann, D.4    Dimanche-Boitrel, M.T.5
  • 247
    • 0022382737 scopus 로고
    • Recombinant human tumor necrosis factor-alpha: Effects on proliferation of normal and transformed cells in vitro
    • Sugarman BJ, Aggarwal BB, Hass PE, Figari IS, Palladino MA, Jr, Shepard HM. Recombinant human tumor necrosis factor-alpha: effects on proliferation of normal and transformed cells in vitro. Science 1985; 230: 943-945.
    • (1985) Science , vol.230 , pp. 943-945
    • Sugarman, B.J.1    Aggarwal, B.B.2    Hass, P.E.3    Figari, I.S.4    Palladino Jr., M.A.5    Shepard, H.M.6
  • 248
    • 33744988897 scopus 로고    scopus 로고
    • Bcl-2 and MnSOD antisense oligodeoxinucleotides and a glutamine enriched diet facilitate elimination of highly resistant B16 melanoma cells by TNF-α and chemotherapy
    • November 1(E Pub)
    • Benlloch M, Mena S, Ferrer P, Obrador E, Asensi M, Pellicer A, Carretero J, Ortega A, Estrela JM. Bcl-2 and MnSOD antisense oligodeoxinucleotides and a glutamine enriched diet facilitate elimination of highly resistant B16 melanoma cells by TNF-α and chemotherapy. J Biol Chem 2005; November 1(E Pub).
    • (2005) J Biol Chem
    • Benlloch, M.1    Mena, S.2    Ferrer, P.3    Obrador, E.4    Asensi, M.5    Pellicer, A.6    Carretero, J.7    Ortega, A.8    Estrela, J.M.9


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.