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Volumn 74, Issue 12, 2007, Pages 1677-1685

Harnessing drug resistance: Using ABC transporter proteins to target cancer cells

Author keywords

Chemotherapy; Flavonoids; Glutathione; Multidrug resistance proteins; Oxidative stress

Indexed keywords

2 BROMOMETHAMPHETAMINE; ABC TRANSPORTER; ANTIRETROVIRUS AGENT; BUTHIONINE SULFOXIMINE; COLCHICINE; CYCLIC NUCLEOTIDE; CYCLOSPORIN A; DAUNORUBICIN; DIGOXIN; DOXORUBICIN; ELACRIDAR; ETOPOSIDE; GLUTATHIONE; IRINOTECAN; MELPHALAN; METHOTREXATE; MITOXANTRONE; MULTIDRUG RESISTANCE PROTEIN; PACLITAXEL; PROSTAGLANDIN DERIVATIVE; PSC 8233; PURINE DERIVATIVE; RHODAMINE; SAQUINAVIR; SULFINPYRAZONE; TOPOTECAN; UNCLASSIFIED DRUG; UNINDEXED DRUG; VERAPAMIL; VINBLASTINE; VINCRISTINE;

EID: 36048948042     PISSN: 00062952     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bcp.2007.05.014     Document Type: Note
Times cited : (39)

References (75)
  • 1
    • 0017868339 scopus 로고
    • Cellular transport mechanisms
    • Wilson D.B. Cellular transport mechanisms. Annu Rev Biochem 47 (1978) 933-965
    • (1978) Annu Rev Biochem , vol.47 , pp. 933-965
    • Wilson, D.B.1
  • 2
    • 0016327218 scopus 로고
    • Different mechanisms of energy coupling for the shock-sensitive and shock-resistant amino acid permeases of Escherichia coli
    • Berger E.A., and Heppel L.A. Different mechanisms of energy coupling for the shock-sensitive and shock-resistant amino acid permeases of Escherichia coli. J Biol Chem 249 (1974) 7747-7755
    • (1974) J Biol Chem , vol.249 , pp. 7747-7755
    • Berger, E.A.1    Heppel, L.A.2
  • 3
    • 0020451714 scopus 로고
    • Extensive homology between membrane-associated components of histidine and maltose transport systems of Salmonella typhimurium and Escherichia coli
    • Gilson E., Higgins C.F., Hofnung M., Ferro-Luzzi Ames G., and Nikaido H. Extensive homology between membrane-associated components of histidine and maltose transport systems of Salmonella typhimurium and Escherichia coli. J Biol Chem 257 (1982) 9915-9918
    • (1982) J Biol Chem , vol.257 , pp. 9915-9918
    • Gilson, E.1    Higgins, C.F.2    Hofnung, M.3    Ferro-Luzzi Ames, G.4    Nikaido, H.5
  • 4
    • 0019965825 scopus 로고
    • Complete nucleotide sequence and identification of membrane components of the histidine transport operon of S. typhimurium
    • Higgins C.F., Haag P.D., Nikaido K., Ardeshir F., Garcia G., and Ames G.F. Complete nucleotide sequence and identification of membrane components of the histidine transport operon of S. typhimurium. Nature 298 (1982) 723-727
    • (1982) Nature , vol.298 , pp. 723-727
    • Higgins, C.F.1    Haag, P.D.2    Nikaido, K.3    Ardeshir, F.4    Garcia, G.5    Ames, G.F.6
  • 5
    • 0001607723 scopus 로고
    • Distantly related sequences in the alpha- and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold
    • Walker J.E., Saraste M., Runswick M.J., and Gay N.J. Distantly related sequences in the alpha- and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold. EMBO J 1 (1982) 945-951
    • (1982) EMBO J , vol.1 , pp. 945-951
    • Walker, J.E.1    Saraste, M.2    Runswick, M.J.3    Gay, N.J.4
  • 6
    • 0021717782 scopus 로고
    • ATP-binding sites in the membrane components of histidine permease, a periplasmic transport system
    • Hobson A.C., Weatherwax R., and Ames G.F. ATP-binding sites in the membrane components of histidine permease, a periplasmic transport system. Proc Natl Acad Sci USA 81 (1984) 7333-7337
    • (1984) Proc Natl Acad Sci USA , vol.81 , pp. 7333-7337
    • Hobson, A.C.1    Weatherwax, R.2    Ames, G.F.3
  • 7
    • 0022051849 scopus 로고
    • Nucleotide binding by membrane components of bacterial periplasmic binding protein-dependent transport systems
    • Higgins C.F., Hiles I.D., Whalley K., and Jamieson D.J. Nucleotide binding by membrane components of bacterial periplasmic binding protein-dependent transport systems. EMBO J 4 (1985) 1033-1039
    • (1985) EMBO J , vol.4 , pp. 1033-1039
    • Higgins, C.F.1    Hiles, I.D.2    Whalley, K.3    Jamieson, D.J.4
  • 8
    • 0022534951 scopus 로고
    • A family of related ATP-binding subunits coupled to many distinct biological processes in bacteria
    • Higgins C.F., Hiles I.D., Salmond G.P., Gill D.R., Downie J.A., Evans I.J., et al. A family of related ATP-binding subunits coupled to many distinct biological processes in bacteria. Nature 323 (1986) 448-450
    • (1986) Nature , vol.323 , pp. 448-450
    • Higgins, C.F.1    Hiles, I.D.2    Salmond, G.P.3    Gill, D.R.4    Downie, J.A.5    Evans, I.J.6
  • 9
    • 0024726144 scopus 로고
    • Reconstitution of a bacterial periplasmic permease in proteoliposomes and demonstration of ATP hydrolysis concomitant with transport
    • Bishop L., Agbayani Jr. R., Ambudkar S.V., Maloney P.C., and Ames G.F. Reconstitution of a bacterial periplasmic permease in proteoliposomes and demonstration of ATP hydrolysis concomitant with transport. Proc Natl Acad Sci USA 86 (1989) 6953-6957
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 6953-6957
    • Bishop, L.1    Agbayani Jr., R.2    Ambudkar, S.V.3    Maloney, P.C.4    Ames, G.F.5
  • 10
    • 0024853842 scopus 로고
    • Energy coupling to periplasmic binding protein-dependent transport systems: stoichiometry of ATP hydrolysis during transport in vivo
    • Mimmack M.L., Gallagher M.P., Pearce S.R., Hyde S.C., Booth I.R., and Higgins C.F. Energy coupling to periplasmic binding protein-dependent transport systems: stoichiometry of ATP hydrolysis during transport in vivo. Proc Natl Acad Sci USA 86 (1989) 8257-8261
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 8257-8261
    • Mimmack, M.L.1    Gallagher, M.P.2    Pearce, S.R.3    Hyde, S.C.4    Booth, I.R.5    Higgins, C.F.6
  • 12
    • 0029586715 scopus 로고
    • Evolution of ATP-binding cassette transporter genes
    • Dean M., and Allikmets R. Evolution of ATP-binding cassette transporter genes. Curr Opin Genet Dev 5 (1995) 779-785
    • (1995) Curr Opin Genet Dev , vol.5 , pp. 779-785
    • Dean, M.1    Allikmets, R.2
  • 13
    • 0029820166 scopus 로고    scopus 로고
    • Characterization of the human ABC superfamily: isolation and mapping of 21 new genes using the expressed sequence tags database
    • Allikmets R., Gerrard B., Hutchinson A., and Dean M. Characterization of the human ABC superfamily: isolation and mapping of 21 new genes using the expressed sequence tags database. Hum Mol Genet 5 (1996) 1649-1655
    • (1996) Hum Mol Genet , vol.5 , pp. 1649-1655
    • Allikmets, R.1    Gerrard, B.2    Hutchinson, A.3    Dean, M.4
  • 14
    • 0022993652 scopus 로고
    • Mammalian multidrug resistance gene: complete cDNA sequence indicates strong homology to bacterial transport proteins
    • Gros P., Croop J., and Housman D. Mammalian multidrug resistance gene: complete cDNA sequence indicates strong homology to bacterial transport proteins. Cell 47 (1986) 371-380
    • (1986) Cell , vol.47 , pp. 371-380
    • Gros, P.1    Croop, J.2    Housman, D.3
  • 15
    • 0022972654 scopus 로고
    • Internal duplication and homology with bacterial transport proteins in the mdr1 (P-glycoprotein) gene from multidrug-resistant human cells
    • Chen C.J., Chin J.E., Ueda K., Clark D.P., Pastan I., and Gottesman M.M.E.-A. Internal duplication and homology with bacterial transport proteins in the mdr1 (P-glycoprotein) gene from multidrug-resistant human cells. Cell 47 (1986) 381-389
    • (1986) Cell , vol.47 , pp. 381-389
    • Chen, C.J.1    Chin, J.E.2    Ueda, K.3    Clark, D.P.4    Pastan, I.5    Gottesman, M.M.E.-A.6
  • 18
    • 21744447836 scopus 로고    scopus 로고
    • Anticancer multidrug resistance mediated by MRP1: recent advances in the discovery of reversal agents
    • Boumendjel A., Baubichon-Cortay H., Trompier D., Perrotton T., and Di Pietro A. Anticancer multidrug resistance mediated by MRP1: recent advances in the discovery of reversal agents. Med Res Rev 25 (2005) 453-472
    • (2005) Med Res Rev , vol.25 , pp. 453-472
    • Boumendjel, A.1    Baubichon-Cortay, H.2    Trompier, D.3    Perrotton, T.4    Di Pietro, A.5
  • 20
    • 0035985610 scopus 로고    scopus 로고
    • Expression of multidrug resistance-associated protein 2 (MRP2) in normal human tissues and carcinomas using tissue microarrays
    • Sandusky G.E., Mintze K.S., Pratt S.E., and Dantzig A.H. Expression of multidrug resistance-associated protein 2 (MRP2) in normal human tissues and carcinomas using tissue microarrays. Histopathology 41 (2002) 65-74
    • (2002) Histopathology , vol.41 , pp. 65-74
    • Sandusky, G.E.1    Mintze, K.S.2    Pratt, S.E.3    Dantzig, A.H.4
  • 21
    • 23044472581 scopus 로고    scopus 로고
    • Distribution of breast cancer resistance protein (BCRP/ABCG2) mRNA expression along the human GI tract
    • Gutmann H., Hruz P., Zimmermann C., Beglinger C., and Drewe J. Distribution of breast cancer resistance protein (BCRP/ABCG2) mRNA expression along the human GI tract. Biochem Pharmacol 70 (2005) 695-699
    • (2005) Biochem Pharmacol , vol.70 , pp. 695-699
    • Gutmann, H.1    Hruz, P.2    Zimmermann, C.3    Beglinger, C.4    Drewe, J.5
  • 22
    • 0035870289 scopus 로고    scopus 로고
    • Subcellular localization and distribution of the breast cancer resistance protein transporter in normal human tissues
    • Maliepaard M., Scheffer G.L., Faneyte I.F., van Gastelen M.A., Pijnenborg A.C., Schinkel A.H., et al. Subcellular localization and distribution of the breast cancer resistance protein transporter in normal human tissues. Cancer Res 61 (2001) 3458-3464
    • (2001) Cancer Res , vol.61 , pp. 3458-3464
    • Maliepaard, M.1    Scheffer, G.L.2    Faneyte, I.F.3    van Gastelen, M.A.4    Pijnenborg, A.C.5    Schinkel, A.H.6
  • 23
    • 0030841332 scopus 로고    scopus 로고
    • Analysis of expression of cMOAT (MRP2), MRP3, MRP4, and MRP5, homologues of the multidrug resistance-associated protein gene (MRP1), in human cancer cell lines
    • Kool M., de Haas M., Scheffer G.L., Scheper R.J., van Eijk M.J., Juijn J.A., et al. Analysis of expression of cMOAT (MRP2), MRP3, MRP4, and MRP5, homologues of the multidrug resistance-associated protein gene (MRP1), in human cancer cell lines. Cancer Res 57 (1997) 3537-3547
    • (1997) Cancer Res , vol.57 , pp. 3537-3547
    • Kool, M.1    de Haas, M.2    Scheffer, G.L.3    Scheper, R.J.4    van Eijk, M.J.5    Juijn, J.A.6
  • 24
    • 0037305372 scopus 로고    scopus 로고
    • Real-time reverse transcription-PCR expression profiling of the complete human ATP-binding cassette transporter superfamily in various tissues
    • Langmann T., Mauerer R., Zahn A., Moehle C., Probst M., Stremmel W., et al. Real-time reverse transcription-PCR expression profiling of the complete human ATP-binding cassette transporter superfamily in various tissues. Clin Chem 49 (2003) 230-238
    • (2003) Clin Chem , vol.49 , pp. 230-238
    • Langmann, T.1    Mauerer, R.2    Zahn, A.3    Moehle, C.4    Probst, M.5    Stremmel, W.6
  • 25
    • 33644854071 scopus 로고    scopus 로고
    • Tissue-specific mRNA expression profiles of human ATP-binding cassette and solute carrier transporter superfamilies
    • Nishimura M., and Naito S. Tissue-specific mRNA expression profiles of human ATP-binding cassette and solute carrier transporter superfamilies. Drug Metab Pharmacokinet 20 (2005) 452-477
    • (2005) Drug Metab Pharmacokinet , vol.20 , pp. 452-477
    • Nishimura, M.1    Naito, S.2
  • 26
    • 0031694229 scopus 로고    scopus 로고
    • Immunohistochemical detection of multidrug resistance protein in human lung cancer and normal lung
    • Wright S.R., Boag A.H., Valdimarsson G., Hipfner D.R., Campling B.G., Cole S.P., et al. Immunohistochemical detection of multidrug resistance protein in human lung cancer and normal lung. Clin Cancer Res 4 (1998) 2279-2289
    • (1998) Clin Cancer Res , vol.4 , pp. 2279-2289
    • Wright, S.R.1    Boag, A.H.2    Valdimarsson, G.3    Hipfner, D.R.4    Campling, B.G.5    Cole, S.P.6
  • 27
    • 0034665559 scopus 로고    scopus 로고
    • Specific detection of multidrug resistance proteins MRP1, MRP2, MRP3, MRP5, and MDR3 P-glycoprotein with a panel of monoclonal antibodies
    • Scheffer G.L., Kool M., Heijn M., de Haas M., Pijnenborg A.C., Wijnholds J., et al. Specific detection of multidrug resistance proteins MRP1, MRP2, MRP3, MRP5, and MDR3 P-glycoprotein with a panel of monoclonal antibodies. Cancer Res 60 (2000) 5269-5277
    • (2000) Cancer Res , vol.60 , pp. 5269-5277
    • Scheffer, G.L.1    Kool, M.2    Heijn, M.3    de Haas, M.4    Pijnenborg, A.C.5    Wijnholds, J.6
  • 30
    • 5144226566 scopus 로고    scopus 로고
    • Predicting drug sensitivity and resistance: profiling ABC transporter genes in cancer cells
    • Szakacs G., Annereau J.P., Lababidi S., Shankavaram U., Arciello A., et al. Predicting drug sensitivity and resistance: profiling ABC transporter genes in cancer cells. Cancer Cell 6 (2004) 129-137
    • (2004) Cancer Cell , vol.6 , pp. 129-137
    • Szakacs, G.1    Annereau, J.P.2    Lababidi, S.3    Shankavaram, U.4    Arciello, A.5
  • 31
    • 0345688619 scopus 로고    scopus 로고
    • Introduction to resistance to anticancer agents
    • Kruh G.D. Introduction to resistance to anticancer agents. Oncogene 22 (2003) 7262-7264
    • (2003) Oncogene , vol.22 , pp. 7262-7264
    • Kruh, G.D.1
  • 32
    • 0028793942 scopus 로고
    • Expression of multidrug resistance-associated protein (MRP) and multidrug resistance (MDR1) genes in acute myeloid leukemia
    • Zhou D.C., Zittoun R., and Marie J.P. Expression of multidrug resistance-associated protein (MRP) and multidrug resistance (MDR1) genes in acute myeloid leukemia. Leukemia 9 (1995) 1661-1666
    • (1995) Leukemia , vol.9 , pp. 1661-1666
    • Zhou, D.C.1    Zittoun, R.2    Marie, J.P.3
  • 33
    • 0021591010 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. Fed Proc 43 (1984) 3031-3042
    • (1984) Fed Proc , vol.43 , pp. 3031-3042
    • Meister, A.1
  • 34
    • 0035824674 scopus 로고    scopus 로고
    • Characterization of drug transport by the human multidrug resistance protein 3 (ABCC3)
    • Zelcer N., Saeki T., Reid G., Beijnen J.H., and Borst P. Characterization of drug transport by the human multidrug resistance protein 3 (ABCC3). J Biol Chem 276 (2001) 46400-46407
    • (2001) J Biol Chem , vol.276 , pp. 46400-46407
    • Zelcer, N.1    Saeki, T.2    Reid, G.3    Beijnen, J.H.4    Borst, P.5
  • 35
    • 0030665969 scopus 로고    scopus 로고
    • Disruption of the murine MRP (multidrug resistance protein) gene leads to increased sensitivity to etoposide (VP-16) and increased levels of glutathione
    • Lorico A., Rappa G., Finch R.A., Yang D., Flavell R.A., and Sartorelli A.C. Disruption of the murine MRP (multidrug resistance protein) gene leads to increased sensitivity to etoposide (VP-16) and increased levels of glutathione. Cancer Res 57 (1997) 5238-5242
    • (1997) Cancer Res , vol.57 , pp. 5238-5242
    • Lorico, A.1    Rappa, G.2    Finch, R.A.3    Yang, D.4    Flavell, R.A.5    Sartorelli, A.C.6
  • 36
    • 1842431869 scopus 로고    scopus 로고
    • Role for cystic fibrosis transmembrane conductance regulator protein in a glutathione response to bronchopulmonary pseudomonas infection
    • Day B.J., van Heeckeren A.M., Min E., and Velsor L.W. Role for cystic fibrosis transmembrane conductance regulator protein in a glutathione response to bronchopulmonary pseudomonas infection. Infect Immun 72 (2004) 2045-2051
    • (2004) Infect Immun , vol.72 , pp. 2045-2051
    • Day, B.J.1    van Heeckeren, A.M.2    Min, E.3    Velsor, L.W.4
  • 37
    • 17444419342 scopus 로고    scopus 로고
    • Molecular mechanisms of reduced glutathione transport: role of the MRP/CFTR/ABCC and OATP/SLC21A families of membrane proteins
    • Ballatori N., Hammond C.L., Cunningham J.B., Krance S.M., and Marchan R. Molecular mechanisms of reduced glutathione transport: role of the MRP/CFTR/ABCC and OATP/SLC21A families of membrane proteins. Toxicol Appl Pharmacol 204 (2005) 238-255
    • (2005) Toxicol Appl Pharmacol , vol.204 , pp. 238-255
    • Ballatori, N.1    Hammond, C.L.2    Cunningham, J.B.3    Krance, S.M.4    Marchan, R.5
  • 38
    • 33746925983 scopus 로고    scopus 로고
    • Up-regulation of P-glycoprotein expression by glutathione depletion-induced oxidative stress in rat brain microvessel endothelial cells
    • Hong H., Lu Y., Ji Z.N., and Liu G.Q. Up-regulation of P-glycoprotein expression by glutathione depletion-induced oxidative stress in rat brain microvessel endothelial cells. J Neurochem 98 (2006) 1465-1473
    • (2006) J Neurochem , vol.98 , pp. 1465-1473
    • Hong, H.1    Lu, Y.2    Ji, Z.N.3    Liu, G.Q.4
  • 39
    • 0034618582 scopus 로고    scopus 로고
    • Structure-activity studies of verapamil analogs that modulate transport of leukotriene C(4) and reduced glutathione by multidrug resistance protein MRP1
    • Loe D.W., Oleschuk C.J., Deeley R.G., and Cole S.P. Structure-activity studies of verapamil analogs that modulate transport of leukotriene C(4) and reduced glutathione by multidrug resistance protein MRP1. Biochem Biophys Res Commun 275 (2000) 795-803
    • (2000) Biochem Biophys Res Commun , vol.275 , pp. 795-803
    • Loe, D.W.1    Oleschuk, C.J.2    Deeley, R.G.3    Cole, S.P.4
  • 40
    • 0013016426 scopus 로고    scopus 로고
    • Bioflavonoid stimulation of glutathione transport by the 190-kDa multidrug resistance protein 1 (MRP1)
    • Leslie E.M., Deeley R.G., and Cole S.P. Bioflavonoid stimulation of glutathione transport by the 190-kDa multidrug resistance protein 1 (MRP1). Drug Metab Dispos 31 (2003) 11-15
    • (2003) Drug Metab Dispos , vol.31 , pp. 11-15
    • Leslie, E.M.1    Deeley, R.G.2    Cole, S.P.3
  • 42
    • 2442660256 scopus 로고    scopus 로고
    • Mutations of charged amino acids in or near the transmembrane helices of the second membrane spanning domain differentially affect the substrate specificity and transport activity of the multidrug resistance protein MRP1 (ABCC1)
    • Haimeur A., Conseil G., Deeley R.G., and Cole S.P. Mutations of charged amino acids in or near the transmembrane helices of the second membrane spanning domain differentially affect the substrate specificity and transport activity of the multidrug resistance protein MRP1 (ABCC1). Mol Pharmacol 65 (2004) 1375-1385
    • (2004) Mol Pharmacol , vol.65 , pp. 1375-1385
    • Haimeur, A.1    Conseil, G.2    Deeley, R.G.3    Cole, S.P.4
  • 43
    • 18044364401 scopus 로고    scopus 로고
    • Differential modulation of normal and tumor cell proliferation by reactive oxygen species
    • Nicco C., Laurent A., Chereau C., Weill B., and Batteux F. Differential modulation of normal and tumor cell proliferation by reactive oxygen species. Biomed Pharmacother 59 (2005) 169-174
    • (2005) Biomed Pharmacother , vol.59 , pp. 169-174
    • Nicco, C.1    Laurent, A.2    Chereau, C.3    Weill, B.4    Batteux, F.5
  • 44
    • 32244436232 scopus 로고    scopus 로고
    • Mitochondria: a target for cancer therapy
    • Armstrong J.S. Mitochondria: a target for cancer therapy. Br J Pharmacol 147 (2006) 239-248
    • (2006) Br J Pharmacol , vol.147 , pp. 239-248
    • Armstrong, J.S.1
  • 45
    • 34548554576 scopus 로고    scopus 로고
    • Selected flavonoids potentiate the toxicity of cisplatin in human lung adenocarcinoma cells: a role for glutathione depletion
    • Kachadourian R., Leitner H.M., and Day B.J. Selected flavonoids potentiate the toxicity of cisplatin in human lung adenocarcinoma cells: a role for glutathione depletion. Int J Oncol 31 (2007) 161-168
    • (2007) Int J Oncol , vol.31 , pp. 161-168
    • Kachadourian, R.1    Leitner, H.M.2    Day, B.J.3
  • 46
    • 0141788593 scopus 로고    scopus 로고
    • Effects of oxygen on the antioxidant responses of normal and transformed cells
    • Allen R.G., and Balin A.K. Effects of oxygen on the antioxidant responses of normal and transformed cells. Exp Cell Res 289 (2003) 307-316
    • (2003) Exp Cell Res , vol.289 , pp. 307-316
    • Allen, R.G.1    Balin, A.K.2
  • 47
    • 0001136010 scopus 로고
    • Glutathione reductase
    • Dolphin D., Poulson R., and Avramovic O. (Eds), Wiley, New York
    • Schirmer R., Drauth-Siegel R., and Schulz G.E. Glutathione reductase. In: Dolphin D., Poulson R., and Avramovic O. (Eds). Coenzymes and cofactors (1989), Wiley, New York 553-596
    • (1989) Coenzymes and cofactors , pp. 553-596
    • Schirmer, R.1    Drauth-Siegel, R.2    Schulz, G.E.3
  • 48
    • 0642374221 scopus 로고    scopus 로고
    • The role of glutathione-S-transferase in anti-cancer drug resistance
    • Townsend D.M., and Tew K.D. The role of glutathione-S-transferase in anti-cancer drug resistance. Oncogene 22 (2003) 7369-7375
    • (2003) Oncogene , vol.22 , pp. 7369-7375
    • Townsend, D.M.1    Tew, K.D.2
  • 50
    • 33746430147 scopus 로고    scopus 로고
    • Thioredoxin reductase as a novel molecular target for cancer therapy
    • Nguyen P., Awwad R.T., Smart D.D., Spitz D.R., and Gius D. Thioredoxin reductase as a novel molecular target for cancer therapy. Cancer Lett 236 (2006) 164-174
    • (2006) Cancer Lett , vol.236 , pp. 164-174
    • Nguyen, P.1    Awwad, R.T.2    Smart, D.D.3    Spitz, D.R.4    Gius, D.5
  • 52
    • 36048991108 scopus 로고
    • Differences between cancers in terms of therapeutic responses
    • Karnofsky D.A. Differences between cancers in terms of therapeutic responses. Cancer Res 16 (1956) 684-697
    • (1956) Cancer Res , vol.16 , pp. 684-697
    • Karnofsky, D.A.1
  • 53
    • 0006424538 scopus 로고
    • Differences between cancers in terms of evolution of drug resistance
    • Law L.W. Differences between cancers in terms of evolution of drug resistance. Cancer Res 16 (1956) 698-716
    • (1956) Cancer Res , vol.16 , pp. 698-716
    • Law, L.W.1
  • 54
    • 0014017284 scopus 로고
    • Comparison of nitrogen-mustard sensitive and -resistant Yoshida sarcomas
    • Ball C.R., Connors T.A., Double J.A., Ujhazy V., and Whisson M.E. Comparison of nitrogen-mustard sensitive and -resistant Yoshida sarcomas. Int J Cancer 1 (1966) 319-327
    • (1966) Int J Cancer , vol.1 , pp. 319-327
    • Ball, C.R.1    Connors, T.A.2    Double, J.A.3    Ujhazy, V.4    Whisson, M.E.5
  • 55
    • 0020086089 scopus 로고
    • Reduction in glutathione content of L-PAM resistant L1210 Cells confers drug sensitivity
    • Suzukake K., Petro B.J., and Vistica D.T. Reduction in glutathione content of L-PAM resistant L1210 Cells confers drug sensitivity. Biochem Pharmacol 31 (1982) 121-124
    • (1982) Biochem Pharmacol , vol.31 , pp. 121-124
    • Suzukake, K.1    Petro, B.J.2    Vistica, D.T.3
  • 56
    • 0017804058 scopus 로고
    • Differential inhibition of glutamine and gamma-glutamylcysteine synthetases by alpha-alkyl analogs of methionine sulfoximine that induce convulsions
    • Griffith O.W., and Meister A. Differential inhibition of glutamine and gamma-glutamylcysteine synthetases by alpha-alkyl analogs of methionine sulfoximine that induce convulsions. J Biol Chem 253 (1978) 2333-2338
    • (1978) J Biol Chem , vol.253 , pp. 2333-2338
    • Griffith, O.W.1    Meister, A.2
  • 57
    • 0018800337 scopus 로고
    • Inhibition of glutathione biosynthesis by prothionine sulfoximine (S-n-propyl homocysteine sulfoximine), a selective inhibitor of gamma-glutamylcysteine synthetase
    • Griffith O.W., Anderson M.E., and Meister A. Inhibition of glutathione biosynthesis by prothionine sulfoximine (S-n-propyl homocysteine sulfoximine), a selective inhibitor of gamma-glutamylcysteine synthetase. J Biol Chem 254 (1979) 1205-1210
    • (1979) J Biol Chem , vol.254 , pp. 1205-1210
    • Griffith, O.W.1    Anderson, M.E.2    Meister, A.3
  • 58
    • 0018666729 scopus 로고
    • Potent and specific inhibition of glutathione synthesis by buthionine sulfoximine (S-n-butyl homocysteine sulfoximine)
    • Griffith O.W., and Meister A. Potent and specific inhibition of glutathione synthesis by buthionine sulfoximine (S-n-butyl homocysteine sulfoximine). J Biol Chem 254 (1979) 7558-7560
    • (1979) J Biol Chem , vol.254 , pp. 7558-7560
    • Griffith, O.W.1    Meister, A.2
  • 59
    • 32944460278 scopus 로고    scopus 로고
    • Inhibition of glutamate cysteine ligase activity sensitizes human breast cancer cells to the toxicity of 2-deoxy-d-glucose
    • Andringa K.K., Coleman M.C., Aykin-Burns N., Hitchler M.J., Walsh S.A., Domann F.E., et al. Inhibition of glutamate cysteine ligase activity sensitizes human breast cancer cells to the toxicity of 2-deoxy-d-glucose. Cancer Res 66 (2006) 1605-1610
    • (2006) Cancer Res , vol.66 , pp. 1605-1610
    • Andringa, K.K.1    Coleman, M.C.2    Aykin-Burns, N.3    Hitchler, M.J.4    Walsh, S.A.5    Domann, F.E.6
  • 61
    • 0027405414 scopus 로고
    • Effect of l-buthionine sulfoximine on the radiation response of human renal carcinoma cell lines
    • Leung S.W., Mitchell J.B., al-Nabulsi I., Friedman N., Newsome J., Belldegrun A., et al. Effect of l-buthionine sulfoximine on the radiation response of human renal carcinoma cell lines. Cancer 71 (1993) 2276-2285
    • (1993) Cancer , vol.71 , pp. 2276-2285
    • Leung, S.W.1    Mitchell, J.B.2    al-Nabulsi, I.3    Friedman, N.4    Newsome, J.5    Belldegrun, A.6
  • 62
    • 0036673665 scopus 로고    scopus 로고
    • Glutathione depletion enforces the mitochondrial permeability transition and causes cell death in Bcl-2 overexpressing HL60 cells
    • Armstrong J.S., and Jones D.P. Glutathione depletion enforces the mitochondrial permeability transition and causes cell death in Bcl-2 overexpressing HL60 cells. FASEB J 16 (2002) 1263-1265
    • (2002) FASEB J , vol.16 , pp. 1263-1265
    • Armstrong, J.S.1    Jones, D.P.2
  • 63
    • 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., et al. 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
  • 64
    • 0023251887 scopus 로고
    • Depletion of tumour versus normal tissue glutathione by buthionine sulfoximine
    • Lee F.Y., Allalunis-Turner M.J., and Siemann D.W. Depletion of tumour versus normal tissue glutathione by buthionine sulfoximine. Br J Cancer 56 (1987) 33-38
    • (1987) Br J Cancer , vol.56 , pp. 33-38
    • Lee, F.Y.1    Allalunis-Turner, M.J.2    Siemann, D.W.3
  • 65
    • 0028157817 scopus 로고
    • Phase I clinical trial of intravenous l-buthionine sulfoximine and melphalan: an attempt at modulation of glutathione
    • Bailey H.H., Mulcahy R.T., Tutsch K.D., Arzoomanian R.Z., Alberti D., Tombes M.B., et al. Phase I clinical trial of intravenous l-buthionine sulfoximine and melphalan: an attempt at modulation of glutathione. J Clin Oncol 12 (1994) 194-205
    • (1994) J Clin Oncol , vol.12 , pp. 194-205
    • Bailey, H.H.1    Mulcahy, R.T.2    Tutsch, K.D.3    Arzoomanian, R.Z.4    Alberti, D.5    Tombes, M.B.6
  • 66
    • 0028892242 scopus 로고
    • Time-dependent pharmacodynamic models in cancer chemotherapy: population pharmacodynamic model for glutathione depletion following modulation by buthionine sulfoximine (BSO) 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., et al. Time-dependent pharmacodynamic models in cancer chemotherapy: population pharmacodynamic model for glutathione depletion following modulation by buthionine sulfoximine (BSO) 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
  • 67
    • 9044254931 scopus 로고    scopus 로고
    • Phase I trial of buthionine sulfoximine in combination with melphalan in patients with cancer
    • O'Dwyer P.J., Hamilton T.C., LaCreta F.P., Gallo J.M., Kilpatrick D., Halbherr T., et al. Phase I trial of buthionine sulfoximine in combination with melphalan in patients with cancer. J Clin Oncol 14 (1996) 249-256
    • (1996) J Clin Oncol , vol.14 , pp. 249-256
    • O'Dwyer, P.J.1    Hamilton, T.C.2    LaCreta, F.P.3    Gallo, J.M.4    Kilpatrick, D.5    Halbherr, T.6
  • 69
    • 0032523026 scopus 로고    scopus 로고
    • The relationship between modulation of MDR and glutathione in MRP-overexpressing human leukemia cells
    • Grech K.V., Davey R.A., and Davey M.W. The relationship between modulation of MDR and glutathione in MRP-overexpressing human leukemia cells. Biochem Pharmacol 55 (1998) 1283-1289
    • (1998) Biochem Pharmacol , vol.55 , pp. 1283-1289
    • Grech, K.V.1    Davey, R.A.2    Davey, M.W.3
  • 70
    • 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., et al. Acceleration of glutathione efflux and inhibition of gamma-glutamyltranspeptidase sensitize metastatic B16 melanoma cells to endothelium-induced cytotoxicity. J Biol Chem 280 (2005) 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
  • 72
    • 34247149458 scopus 로고    scopus 로고
    • Modulation of GSH levels in ABCC1 expressing tumor cells triggers apoptosis through oxidative stress
    • Laberge R.M., Karwatsky J., Lincoln M.C., Leimanis M.L., and Georges E. Modulation of GSH levels in ABCC1 expressing tumor cells triggers apoptosis through oxidative stress. Biochem Pharmacol 73 (2007) 1727-1737
    • (2007) Biochem Pharmacol , vol.73 , pp. 1727-1737
    • Laberge, R.M.1    Karwatsky, J.2    Lincoln, M.C.3    Leimanis, M.L.4    Georges, E.5
  • 73
    • 33744996911 scopus 로고    scopus 로고
    • Flavonoid-induced glutathione depletion: potential implications for cancer treatment
    • Kachadourian R., and Day B.J. Flavonoid-induced glutathione depletion: potential implications for cancer treatment. Free Radic Biol Med 41 (2006) 65-76
    • (2006) Free Radic Biol Med , vol.41 , pp. 65-76
    • Kachadourian, R.1    Day, B.J.2
  • 75
    • 0345688182 scopus 로고    scopus 로고
    • Transcriptional regulation of ABC drug transporters
    • Scotto K. Transcriptional regulation of ABC drug transporters. Oncogene 22 (2003) 7496-7511
    • (2003) Oncogene , vol.22 , pp. 7496-7511
    • Scotto, K.1


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