GLUTATHIONE CONJUGATES AND THEIR SYNTHETIC DERIVATIVES AS INHIBITORS OF GLUTATHIONE-DEPENDENT ENZYMES INVOLVED IN CANCER AND DRUG RESISTANCE

REFERENCES

• Shi Z.Z., Osei F.J., Kala G., Kala S.V., Barrios R.J., Habib G.M., Lukin D.J., Danney C.M., Matzuk M.M., Lieberman M.W. Glutathione Synthesis Is Essential for Mouse Development But Not for Cell Growth in Culture. Proc. Natl Acad. Sci. USA 2000; 97(10)5101–5106
   PubMed Web of Science ®Google Scholar
• Davis W., Jr., Ronai Z., Tew K.D. Cellular Thiols and Reactive Oxygen Species in Drug-Induced Apoptosis. J. Pharmacol. Exp. Ther. 2001; 296(1)1–6
   PubMed Web of Science ®Google Scholar
• Orlowski M., Meister A. The γ-Glutamyl Cycle—A Possible Transport System for Amino Acids. Proc. Natl Acad. Sci. USA 1970; 67: 1248–1255
   PubMed Web of Science ®Google Scholar
• Meister A., Larsson A. Glutathione Synthetase Deficiency and Other Disorders of the γ-Glutamyl Cycle. The Metabolic and Molecular Bases of Inherited Disease, C.F. Scriver, A.L. Beaudet, W.S. Sly, D. Valle. McGraw Hill, New York 1995; 1461–1477
   Google Scholar
• Ristoff E., Larsson A. Patients with Genetic Defects in the Gamma-Glutamyl Cycle. Chem. Biol. Interact. 1998; 111–112: 113–121
   PubMed Web of Science ®Google Scholar
• Hammond C.L., Lee T.K., Ballatori N. Novel Roles for Glutathione in Gene Expression, Cell Death, and Membrane Transport of Organic Solutes. J. Hepatol. 2001; 34(6)946–954
   PubMed Web of Science ®Google Scholar
• Locigno R., Castronovo V. Reduced Glutathione System: Role in Cancer Development, Prevention and Treatment. Int. J. Oncol. 2001; 19(2)221–236
   PubMed Web of Science ®Google Scholar
• Hayes J.D., McLellan L.I. Glutathione and Glutathione-Dependent Enzymes Represent a Co-ordinately Regulated Defence Against Oxidative Stress. Free Radic. Res. 1999; 31(4)273–300
   PubMed Web of Science ®Google Scholar
• Baillie T.A., Kassahum K. Reversibility in Glutathione-Conjugate Formation. Adv. Pharmacol. 1994; 27: 163–181
   PubMedGoogle Scholar
• Diah S.K., Smitherman P.K., Townsend A.J., Morrow C.S. Detoxification of 1-Chloro-2,4-dinitrobenzene in MCF7 Breast Cancer Cells Expressing Glutathione S-Transferase P1-1 and/or Multidrug Resistance Protein 1. Toxicol. Appl. Pharmacol. 1999; 157(2)85–93
   PubMed Web of Science ®Google Scholar
• Morrow C.S., Smitherman P.K., Townsend A.J. Combined Expression of Multidrug Resistance Protein (MRP) and Glutathione S-Transferase P1-1(GSTP1-1) in MCF7 Cells and High Level Resistance to the Cytotoxicities of Ethacrynic Acid But Not Oxazaphosphorines or Cisplatin. Biochem. Pharmacol. 1998; 56(8)1013–1021
   PubMed Web of Science ®Google Scholar
• Morrow C.S., Smitherman P.K., Diah S.K., Schneider E., Townsend A.J. Coordinated Action of Glutathione S-Transferases (GSTs) and Multidrug Resistance Protein 1(MRP1) in Antineoplastic Drug Detoxification. Mechanism of GST A1-1- and MRP1-Associated Resistance to Chlorambucil in MCF7 Breast Carcinoma Cells. J. Biol. Chem. 1998; 273(32)20114–20120
   PubMed Web of Science ®Google Scholar
• Morrow C.S., Smitherman P.K., Townsend A.J. Role of Multidrug-Resistance Protein 2 in Glutathione S-Transferase P1-1-Mediated Resistance to 4-Nitroquinoline 1-Oxide Toxicities in HepG2 Cells. Mol. Carcinog. 2000; 29: 170–178
   PubMed Web of Science ®Google Scholar
• Paumi C.M., Ledford B.G., Smitherman P.K., Townsend A.J., Morrow C.S. Role of Multidrug Resistance Protein 1 (MRP1) and Glutathione S-Transferase A1-1 in Alkylating Agent Resistance. Kinetics of Glutathione Conjugate Formation and Efflux Govern Differential Cellular Sensitivity to Chlorambucil Versus Melphalan Toxicity. J. Biol. Chem. 2001; 276(11)7952–7956
   PubMed Web of Science ®Google Scholar
• Townsend A.J., Fields W.R., Haynes R.L., Doss A.J., Li Y., Doehmer J., Morrow C.S. Chemoprotective Functions of Glutathione S-Transferases in Cell Lines Induced to Express Specific Isozymes by Stable Transfection. Chem. Biol. Interact. 1998; 111–112: 389–407
   PubMed Web of Science ®Google Scholar
• Cnubben N.H., Rommens A.J., Oudshoorn M.J., van Bladeren P.J. Glutathione-Dependent Biotransformation of the Alkylating Drug Thiotepa and Transport of Its Metabolite Monoglutathionylthiotepa in Human MCF-7 Breast Cancer Cells. Cancer Res. 1998; 58(20)4616–4623
   PubMed Web of Science ®Google Scholar
• Ciaccio P.J., Shen H., Jaiswal A.K., Lyttle M.H., Tew K.D. Modulation of Detoxification Gene Expression in Human Colon HT29 Cells by Glutathione-S-transferase Inhibitors. Mol. Pharmacol. 1995; 48(4)639–647
   PubMed Web of Science ®Google Scholar
• Ciaccio P.J., Tew K.D. Adaptive Response to Glutathione S-Transferase Inhibitors. Br. J. Cancer Suppl. 1996; 27: S93–S98
   PubMedGoogle Scholar
• Tew K.D., O'Brien M., Laing N.M., Shen H. Coordinate Changes in Expression of Protective Genes in Drug-Resistant Cells. Chem. Biol. Interact. 1998; 111–112: 199–211
   PubMed Web of Science ®Google Scholar
• Rosario L.A., O'Brien M.L., Henderson C.J., Wolf C.R., Tew K.D. Cellular Response to a Glutathione S-Transferase P1-1 Activated Prodrug. Mol. Pharmacol. 2000; 58(1)167–174
   PubMed Web of Science ®Google Scholar
• O'Brien M., Kruh G.D., Tew K.D. The Influence of Coordinate Overexpression of Glutathione Phase II Detoxification Gene Products on Drug Resistance. J. Pharmacol. Exp. Ther. 2000; 294(2)480–487
   PubMed Web of Science ®Google Scholar
• Tatebe S., Sinicrope F.A., Tien K.M. Induction of Multidrug Resistance Proteins MRP1 and MRP3 and [Gamma]-Glutamylcysteine Synthetase Gene Expression by Nonsteroidal Anti-inflammatory Drugs in Human Colon Cancer Cells. Biochem. Biophys. Res. Commun. 2002; 290(5)1427–1433
   PubMed Web of Science ®Google Scholar
• Perquin M., Oster T., Maul A., Froment N., Untereiner M., Bagrel D. The Glutathione-Related Detoxification Pathway in the Human Breast: A Highly Coordinated System Disrupted in the Tumour Tissues. Cancer Lett. 2000; 158(1)7–16
   PubMed Web of Science ®Google Scholar
• Sagara Y., Dargusch R., Chambers D., Davis J., Schubert D., Maher P. Cellular Mechanisms of Resistance to Chronic Oxidative Stress. Free Radic. Biol. Med. 1998; 24(9)1375–1389
   PubMed Web of Science ®Google Scholar
• Lam B.K., Frank A.K. Leukotriene C4 Synthase. A Pivotal Enzyme in the Biosynthesis of the Cysteinyl Leukotrienes. Am. J. Respir. Crit. Care Med. 2000; 161(2 Pt 2)S16–S19
   PubMed Web of Science ®Google Scholar
• Chiuch C.C., Rauhala P. The Redox Pathway of S-Nitrosoglutathione, Glutathione and Nitric Oxide in Cell to Neuron Communications. Free Radic. Res. 1999; 31(6)641–650
   PubMed Web of Science ®Google Scholar
• Monks T.J., Lau S.S. Glutathione Conjugation as Mechanism for the Transport of Reactive Metabolites. Adv. Pharmacol. 1994; 27: 183–210
   PubMedGoogle Scholar
• Ruscoe J.E., Rosario L.A., Wang T., Gate L., Arifoglu P., Wolf C.R., Henderson C.J., Ronai Z., Tew K.D. Pharmacologic or Genetic Manipulation of Glutathione S-Transferase P1-1(GSTpi) Influences Cell Proliferation Pathways. J. Pharmacol. Exp. Ther. 2001; 298(1)339–345
   PubMed Web of Science ®Google Scholar
• Lucente G., Luisi G., Pinnen F. Design and Synthesis of Glutathione Analogues. Farmaco 1998; 53(12)721–735
   PubMedGoogle Scholar
• Adang A.E., Brussee J., Meyer D.J., Coles B., Ketterer B., van der Gen A., Mulder G.J. Substrate Specificity of Rat Liver Glutathione S-Transferase Isoenzymes for a Series of Glutathione Analogues, Modified at the Gamma-Glutamyl Moiety. Biochem. J. 1988; 255(2)721–724
   PubMed Web of Science ®Google Scholar
• Adang A.E., Brussee J., van der Gen A., Mulder G.J. The Glutathione-Binding Site in Glutathione S-Transferases. Investigation of the Cysteinyl, Glycyl and Gamma-Glutamyl Domains. Biochem. J. 1990; 269(1)47–54
   PubMed Web of Science ®Google Scholar
• Lyttle M.H., Hocker M.D., Hui H.C., Caldwell C.G., Aaron D.T., Engqvist G.A., Flatgaard J.E., Bauer K.E. Isozyme-Specific Glutathione-S-transferase Inhibitors: Design and Synthesis. J. Med. Chem. 1994; 37(1)189–194
   PubMed Web of Science ®Google Scholar
• Flatgaard J.E., Bauer K.E., Kauvar L.M. Isozyme Specificity of Novel Glutathione-S-transferase Inhibitors. Cancer Chemother. Pharmacol. 1993; 33(1)63–70
   PubMed Web of Science ®Google Scholar
• Adang A.E., Brussee J., van der Gen A., Mulder G.J. Inhibition of Rat Liver Glutathione S-Transferase Isoenzymes by Peptides Stabilized Against Degradation by Gamma-Glutamyl Transpeptidase. J. Biol. Chem. 1991; 266(2)830–836
   PubMed Web of Science ®Google Scholar
• Adang A.E., Moree W.J., Brussee J., Mulder G.J., van der Gen A. Inhibition of Glutathione S-Transferase 3-3 by Glutathione Derivatives That Bind Covalently to the Active Site. Biochem. J. 1991; 278(Pt 1)63–68
   PubMedGoogle Scholar
• Ouwerkerk-Mahadevan S., Mulder G.J. Inhibition of Glutathione Conjugation in the Rat In Vivo by Analogues of Glutathione Conjugates. Chem. Biol. Interact. 1998; 111–112: 163–176
   PubMed Web of Science ®Google Scholar
• Murthy N.S., Bakeris T., Kavarana M.J., Hamilton D.S., Lan Y., Creighton D.J. S-(N-Aryl-N-Hydroxycarbamoyl)Glutathione Derivatives Are Tight-Binding Inhibitors of Glyoxalase I and Slow Substrates for Glyoxalase II. J. Med. Chem. 1994; 37(14)2161–2166
   PubMed Web of Science ®Google Scholar
• Kavarana M.J., Kovaleva E.G., Creighton D.J., Wollman M.B., Eiseman J.L. Mechanism-Based Competitive Inhibitors of Glyoxalase I: Intracellular Delivery, In Vitro Antitumor Activities, and Stabilities in Human Serum and Mouse Serum. J. Med. Chem. 1999; 42(2)221–228
   PubMed Web of Science ®Google Scholar
• D'-Silva C., Daunes S., Rock P., Yardley V., Croft S.L. Structure–Activity Study on the In Vitro Antiprotozoal Activity of Glutathione Derivatives. J. Med. Chem. 2000; 43(10)2072–2078
   PubMed Web of Science ®Google Scholar
• Daunes S., D'Silva C., Kendrick H., Yardley V., Croft S.L. QSAR Study on the Contribution of Log P and E(s) to the In Vitro Antiprotozoal Activity of Glutathione Derivatives. J. Med. Chem. 2001; 44(18)2976–2983
   PubMed Web of Science ®Google Scholar
• Brophy P.M., Campbell A.M., van Eldik A.J., Teesdale-Spittle P.H., Liebau E., Wang M.F. Beta-Carbonyl Substituted Glutathione Conjugates as Inhibitors of O. volvulus GST2. Bioorg. Med. Chem. Lett. 2000; 10(9)979–981
   PubMed Web of Science ®Google Scholar
• Kahna A.H., Bundgaard H. Synthesis and Chemical and Enzymatic Hydrolysis Kinetics of Various Mono- and Diester Prodrugs of N-Acetyl Cysteine. Int. J. Pharm. 1990; 62: 193–205
   Google Scholar
• Hobbs M.J., Butterworth M., Cohen G.M., Upshall D.G. Structure–Activity Relationships of Cysteine Esters and Their Effects on Thiol Levels in Rat Lung In Vitro. Biochem. Pharmacol. 1993; 45(8)1605–1612
   PubMed Web of Science ®Google Scholar
• Levy E.J., Andrews P.A., Meister A. Transport of Glutathione Diethyl Ester into Human Cells. Proc. Natl Acad. Sci. USA 1993; 90: 9171–9175
   PubMed Web of Science ®Google Scholar
• Kunze T. Phosphono Analogues of Glutathione as New Inhibitors of Glutathione S-Transferases. Arch. Pharm. Weinheim 1996; 329(11)503–509
   PubMed Web of Science ®Google Scholar
• Kunze T., Heps S. Phosphono Analogs of Glutathione: Inhibition of Glutathione Transferases, Metabolic Stability, and Uptake by Cancer Cells. Biochem. Pharmacol. 2000; 59(8)973–981
   PubMed Web of Science ®Google Scholar
• Chen W.J., Lee D.Y., Armstrong R.N. N4-(Malonyl-d-cysteinyl)-l-2,4-diaminobutyrate: The End-Group Modified Retro-inverso Isomer of Glutathione. J. Org. Chem. 1986; 51(14)2848–2850
   Web of Science ®Google Scholar
• Luisi G., Calcagni A., Pinnen F. Ψ(SO2–NH) Transition State Isosteres of Peptides. Synthesis of the Glutathione Disulfide Analogue [Glu-Ψ(SO2–NH)–cys–gly]2. Tetrahedron Lett. 1993; 34(14)2391–2392
   Web of Science ®Google Scholar
• Calcagni A., Dupre S., Lucente G., Luisi G., Pinnen F., Rossi D. Synthesis and Activity of the Glutathione Analogue Gamma-(l-gamma-azaglutamyl)-l-cysteinyl-glycine. Int. J. Pept. Protein Res. 1995; 46(5)434–439
   PubMedGoogle Scholar
• Calcagni A., Dupre S., Lucente G., Luisi G., Pinnen F., Rossi D., Spirito A. Synthesis and Activity of the Glutathione Analogue Gamma-(l-gamma-oxaglutamyl)-l-cysteinyl-glycine. Arch. Pharm. Weinheim 1996; 329(11)498–502
   PubMed Web of Science ®Google Scholar
• Vince R., Brownell J., Akella L.B. Synthesis and Activity of Gamma-(l-gamma-azaglutamyl)-S-(p-bromobenzyl)-l-cysteinylglycine: A Metabolically Stable Inhibitor of Glyoxalase I. Bioorg. Med. Chem. Lett. 1999; 9(6)853–856
   PubMed Web of Science ®Google Scholar
• Burg D., Filippov D.V., Hermanns R., van der Marel G.A., van Boom J.H., Mulder G.J. Peptidomimetic Glutathione Analogues as Novel γGT Stable GST Inhibitors. Bioorg. Med. Chem. 2002; 10(1)195–205
   PubMed Web of Science ®Google Scholar
• Klotz P., Slaoui H.A., Baneres J.L., Duckert J.F., Rossi J.C., Kerbal A. Synthesis and Glutathione S-Transferase Structure–Affinity Relationships of Nonpeptide and Peptidase-Stable Glutathione Analogues. J. Med. Chem. 1998; 41(13)2278–2288
   PubMed Web of Science ®Google Scholar
• Duckert J.F., Balas L., Rossi J.C. Synthesis of 5-(Mercaptomethyl)-3(E)-undecene-1,11-dioic Acid, a Non-peptide Glutathione Analog. Tetrahedron Lett. 2001; 42: 3709–3711
   Web of Science ®Google Scholar
• Sheehan D., Meade G., Foley V.M., Dowd C.A. Structure, Function and Evolution of Glutathione Transferases—Implications for Classification of Non-mammalian Members of an Ancient Enzyme Superfamily. Biochem. J. 2001; 360: 1–16
   PubMed Web of Science ®Google Scholar
• Whalen R., Boyer T.D. Human Glutathione S-Transferases. Semin. Liver Dis. 1998; 18(4)345–358
   PubMed Web of Science ®Google Scholar
• Hayes J.D., Pulford D.J. The Glutathione S-Transferase Supergene Family: Regulation of GST and the Contribution of the Isoenzymes to Cancer Chemoprotection and Drug Resistance. Crit. Rev. Biochem. Mol. Biol. 1995; 30(6)445–600
   PubMed Web of Science ®Google Scholar
• Board P.G., Coggan M., Chelvanayagam G., Easteal S., Jermiin L.S., Schulte G.K., Danley D.E., Hoth L.R., Griffor M.C., Kamath A.V., Rosner M.H., Chrunyk B.A., Perregaux D.E., Gabel C.A., Geoghegan K.F., Pandit J. Identification, Characterization, and Crystal Structure of the Omega Class Glutathione Transferases. J. Biol. Chem. 2000; 275: 24798–24806
   PubMed Web of Science ®Google Scholar
• Pemble S.E., Wardle A.F., Taylor J.B. Glutathione S-Transferase Class Kappa-Characterization by the Cloning of Rat Mitochondrial GST and Identification of a Human Homologue. Biochem. J. 1996; 319: 749–754
   PubMed Web of Science ®Google Scholar
• Board P.G., Baker R.T., Chelvanayagam G., Jermiin L.S. Zeta, a Novel Class of Glutathione Transferases in a Range of Species from Plants to Human. Biochem. J. 1997; 328: 929–935
   PubMed Web of Science ®Google Scholar
• Jakobsson P.J., Morgenstern R., Mancini J., Ford-Hutchinson A., Persson B. Membrane-Associated Proteins in Eicosanoid and Glutathione Metabolism (MAPEG). A Widespread Protein Superfamily. Am. J. Respir. Crit. Care Med. 2000; 161(2 Pt 2)S20–S24
   PubMed Web of Science ®Google Scholar
• Pettigrew N.E., Colman R.F. Heterodimers of Glutathione S-Transferase Can Form Between Isoenzyme Classes Pi and Mu. Arch. Biochem. Biophys. 2001; 396(2)225–230
   PubMed Web of Science ®Google Scholar
• Gardner J.L., Gallagher E.P. Development of a Peptide Antibody Specific to Human Glutathione S-Transferase Alpha 4-4 (hGSTA4-4) Reveals Preferential Localization in Human Liver Mitochondria. Arch. Biochem. Biophys. 2001; 390(1)19–27
   PubMed Web of Science ®Google Scholar
• Quondamatteo F., Schulz T.G., Bunzel N., Hallier E., Herken R. Immunohistochemical Localization of Glutathione S-Transferase-T1 in Murine Kidney, Liver, and Lung. Histochem. Cell Biol. 1998; 110(4)417–423
   PubMed Web of Science ®Google Scholar
• Landi S. Mammalian Class Theta GST and Differential Susceptibility to Carcinogens: A Review. Mutat. Res. 2000; 463(3)247–283
   PubMed Web of Science ®Google Scholar
• Ali-Osman F., Brunner J.M., Kutluk T.M., Hess K. Prognostic Significance of Glutathione S-Transferase Pi Expression and Subcellular Localization in Human Gliomas. Clin. Cancer Res. 1997; 3(12 Pt 1)2253–2261
   PubMed Web of Science ®Google Scholar
• van Lieshout E.M., van Haelst U.J., Wobbes T., Peters W.H. Immunohistochemical Localization of Glutathione S-Transferase Alpha and Pi in Human Esophageal Squamous Epithelium, Barrett's Epithelium and Carcinoma. Jpn. J. Cancer Res. 1999; 90(5)530–535
   PubMedGoogle Scholar
• Chen Y.K., Lin L.M. Immunohistochemical Demonstration of Epithelial Glutathione S-Transferase Isoenzymes in Normal, Benign, Premalignant and Malignant Human Oral Mucosa. J. Oral Pathol. Med. 1995; 24(7)316–321
   PubMed Web of Science ®Google Scholar
• Goto S., Ihara Y., Urata Y., Izumi S., Abe K., Koji T., Kondo T. Doxorubicin-Induced DNA Intercalation and Scavenging by Nuclear Glutathione S-Transferase Pi. FASEB J. 2001; 15(14)2702–2714
   PubMed Web of Science ®Google Scholar
• Yu L.G., Fernig D.G., White M.R., Spiller D.G., Appleton P., Evans R.C., Grierson I., Smith J.A., Davies H., Gerasimenko O.V., Petersen O.H., Milton J.D., Rhodes J.M. Edible Mushroom (Agaricus bisporus) Lectin, Which Reversibly Inhibits Epithelial Cell Proliferation, Blocks Nuclear Localization Sequence-Dependent Nuclear Protein Import. J. Biol. Chem. 1999; 274(8)4890–4899
   PubMed Web of Science ®Google Scholar
• Armstrong R.N. Structure, Catalytic Mechanism, and Evolution of the Glutathione Transferases. Chem. Res. Toxicol. 1997; 10(1)2–18
   PubMed Web of Science ®Google Scholar
• Boyer T.D., Vessay D.A., Holcomb C., Saley N. Studies of the Relationship Between the Catalytic Activity and Binding of Nonsubstrate Ligands by Glutathione S-Transferases. Biochem. J. 1984; 217: 179–185
   PubMed Web of Science ®Google Scholar
• Listowski I., Abramovitz M., Homma H., Niitsu Y. Intracellular Binding and Transport of Hormones and Xenobiotics by Glutathione S-Transferases. Drug Metab. Rev. 1988; 19: 305–318
   PubMed Web of Science ®Google Scholar
• Mannervik B., Danielson U.H. Glutathione Transferases—Structure and Catalytic Activity. CRC Crit. Rev. Biochem. 1988; 23(3)283–337
   PubMed Web of Science ®Google Scholar
• Oakley A.J., LoBello M., Nuccetelli M., Mazzetti A.P., Parker M.W. The Ligandin (Non-substrate) Binding Site of Human Pi Class Glutathione Transferase Is Located in the Electrophile Binding Site (H-Site). J. Mol. Biol. 1999; 291(4)913–926
   PubMed Web of Science ®Google Scholar
• Bello M.L., Nuccetelli M., Caccuri A.M., Stella L., Parker M.W., Rossjohn J., McKinstry W.J., Mozzi A.F., Federici G., Polizio F., Pedersen J.Z., Ricci G. Human Glutathione Transferase P1-1 and Nitric Oxide Carriers; a New Role for an Old Enzyme. J. Biol. Chem. 2001; 276(45)42138–42145
   PubMed Web of Science ®Google Scholar
• Adler V., Yin Z., Fuchs S.Y., Benezra M., Rosario L., Tew K.D., Pincus M.R., Sardana M., Henderson C.J., Wolf C.R., Davis R.J., Ronai Z. Regulation of JNK Signaling by GSTp. EMBO J. 1999; 18(5)1321–1334
   PubMed Web of Science ®Google Scholar
• Monaco R., Friedman F.K., Hyde M.J., Chen J.M., Manolatus S., Adler V., Ronai Z., Koslosky W., Pincus M.R. Identification of a Glutathione-S-transferase Effector Domain for Inhibition of Jun Kinase, by Molecular Dynamics. J. Protein Chem. 1999; 18(8)859–866
   PubMedGoogle Scholar
• Wang T., Arifoglu P., Ronai Z., Tew K.D. Glutathione S-Transferase P1-1 (GSTP1-1) Inhibits c-Jun N-Terminal Kinase (JNK1) Signaling Through Interaction with the C-Terminus. J. Biol. Chem. 2001; 276(24)20999–21003
   PubMed Web of Science ®Google Scholar
• Barr R.K., Bogoyevitch M.A. The c-Jun N-Terminal Kinase Family of Mitogen-Activated Protein Kinases (JNK MAPKs). Int. J. Biochem. Cell Biol. 2001; 33: 1047–1063
   PubMed Web of Science ®Google Scholar
• Bernardini S., Bernassola F., Cortese C., Ballerini S., Melino G., Motti C., Bellincampi L., Iori R., Federici G. Modulation of GST P1-1 Activity by Polymerization During Apoptosis. J. Cell Biochem. 2000; 77(4)645–653
   PubMed Web of Science ®Google Scholar
• Yin Z., Ivanov V.N., Habelhah H., Tew K., Ronai Z. Glutathione S-Transferase p Elicits Protection Against H2O2-Induced Cell Death via Coordinated Regulation of Stress Kinases. Cancer Res. 2000; 60(15)4053–4057
   PubMed Web of Science ®Google Scholar
• Van Haaften R.I., den Hartog G.J., Evelo C.T., Haenen G.R., Bast A. Hypochlorous Acid Is a Potent Inhibitor of Gst P1-1. Chem. Biol. Interact. 2001; 138(1)77–83
   PubMed Web of Science ®Google Scholar
• Villafania A., Anwar K., Amar S., Chie L., Way D., Chung D.L., Adler V., Ronai Z., Brandt-Rauf P.W., Yamaizumii Z., Kung H.F., Pincus M.R. Glutathione-S-transferase as a Selective Inhibitor of Oncogenic Ras-p21-Induced Mitogenic Signaling Through Blockade of Activation of Jun by Jun-N-terminal Kinase. Ann. Clin. Lab. Sci. 2000; 30(1)57–64
   PubMed Web of Science ®Google Scholar
• Cho S.G., Lee Y.H., Park H.S., Ryoo K., Kang K.W., Park J., Eom S.J., Kim M.J., Chang T.S., Choi S.Y., Shim J., Kim Y., Dong M.S., Lee M.J., Kim S.G., Ichijo H., Choi E.J. Glutathione S-Transferase Mu Modulates the Stress-Activated Signals by Suppressing Apoptosis Signal-Regulating Kinase 1. J. Biol. Chem. 2001; 276(16)12749–12755
   PubMed Web of Science ®Google Scholar
• Dulhunty A., Gage P., Curtis S., Chelvanayagam G., Board P. The Glutathione Transferase Structural Family Includes a Nuclear Chloride Channel and a Ryanodine Receptor Calcium Release Channel Modulator. J. Biol. Chem. 2001; 276(5)3319–3323
   PubMed Web of Science ®Google Scholar
• Kampranis S.C., Damianova R., Atallah M., Toby G., Kondi G., Tsichlis P.N., Makris A.M. A Novel Plant Glutathione S-Transferase/Peroxidase Suppresses Bax Lethality in Yeast. J. Biol. Chem. 2000; 275(38)29207–29216
   PubMed Web of Science ®Google Scholar
• Buller A.L., Clapper M.L., Tew K.D. Glutathione S-Transferases in Nitrogen Mustard-Resistant and Sensitive Cell Lines. Mol. Pharmacol. 1987; 31: 575–580
   PubMed Web of Science ®Google Scholar
• Yang W.Z., Begleiter A., Johnston J.B., Israels L.G., Mowat M.R. Role of Glutathione and Glutathione S-Transferases in Chlorambucil Resistance. Mol. Pharmacol. 1992; 41: 625–630
   PubMed Web of Science ®Google Scholar
• Berhane K., Hao X.Y., Egyhåzy S., Hansson J., Ringborg U., Mannervik B. Contribution of Glutathione S-Transferase M3-3 to 1,3-Bis(2-Chloroethyl)-1-nitrosourea Resistance in a Human Non-small Cell Lung Cancer Cell Line. Cancer Res. 1993; 53: 4257–4261
   PubMed Web of Science ®Google Scholar
• Skalski V., Yarosh B.D., Batist G., Gros P., Feindel W., Kopriva D., Panasci L.C. Mechanisms of Resistance to (2-Chloroethyl)-3-sarcosinamide-1-nitrosurea (sarCNU) in Sensitive and Resistant Human Glioma Cells. Mol. Pharmacol. 1990; 38: 299–305
   PubMed Web of Science ®Google Scholar
• Dirven H.A., Megens L., Oudshoorn M.J., Dingemanse M.A., van Ommen B., van Bladeren P.J. Glutathione Conjugation of the Cytostatic Drug Ifosfamide and the Role of Human Glutathione S-Transferases. Chem. Res. Toxicol. 1995; 8: 979–986
   PubMed Web of Science ®Google Scholar
• Dirven H.A., Dictus E.L., Broeders N.L., van Ommen B., van Bladeren P.J. The Role of Human Glutathione S-Transferase Isoenzymes in the Formation of Glutathione Conjugates of the Alkylating Cytostatic Drug Thiotepa. Cancer Res. 1995; 55(8)1701–1706
   PubMed Web of Science ®Google Scholar
• Tsuchida S., Sato K. Glutathione Transferases and Cancer. Crit. Rev. Biochem. Mol. Biol. 1992; 27(4–5)337–384
   PubMed Web of Science ®Google Scholar
• Tew K.D. Glutathione-Associated Enzymes in Anticancer Drug Resistance. Cancer Res. 1994; 54(16)4313–4320
   PubMed Web of Science ®Google Scholar
• Tew K., Monks A., Barone L., Rosser D., Akerman G., Montali J.A., Wheatley J.B., Schmidt D.E. Glutathione-Associated Enzymes in the Human Cell Lines of the National Cancer Institute Drug Screening Program. Mol. Pharmacol. 1996; 50: 149–159
   PubMed Web of Science ®Google Scholar
• Morrow C.S., Cowan K.H. Antineoplastic Drug Resistance and Breast Cancer. Ann. NY Acad. Sci. 1993; 698: 289–312
   PubMed Web of Science ®Google Scholar
• Niitsu Y., Takahashi Y., Ban N., Takayama T., Saito T., Katahira T., Umetsu Y., Nakajima T., Ohi M., Kuga T., Sakamaki S., Matsunaga T., Hirayama Y., Kuroda H., Homma H., Kato J., Kogawa K. A Proof of Glutathione S-Transferase-pi-related Multidrug Resistance by Transfer of Antisense Gene to Cancer Cells and Sense Gene to Bone Marrow Stem Cell. Chem. Biol. Interact. 1998; 111–112: 325–332
   PubMed Web of Science ®Google Scholar
• Nakagawa K., Saijo N., Tsuchida S., Sakai M., Tsunokawa Y., Yokota J., Muramatsu M., Sato K., Terada M., Tew K.D. Glutathione-S-transferase Pi as a Determinant of Drug Resistance in Transfectant Cell Lines. J. Biol. Chem. 1990; 265(8)4296–4301
   PubMed Web of Science ®Google Scholar
• Harbottle A., Daly A.K., Atherton K., Campbell F.C. Role of Glutathione S-Transferase P1, P-Glycoprotein and Multidrug Resistance-Associated Protein 1 in Acquired Doxorubicin Resistance. Int. J. Cancer 2001; 92: 777–783
   PubMed Web of Science ®Google Scholar
• Asakura T., Hashizume Y., Tashiro K., Searashi Y., Ohkawa K., Nishihira J., Sakai M., Shibasaki T. Suppression of GST-P by Treatment with Glutathione–Doxorubicin Conjugate Induces Potent Apoptosis in Rat Hepatoma Cells. Int. J. Cancer 2001; 94(2)171–177
   PubMed Web of Science ®Google Scholar
• Gaudiano G., Koch T.H., LoBello M., Nuccetelli M., Ravagnan G., Serafino A., Sinibaldi-Vallebona P. Lack of Glutathione Conjugation to Adriamycin in Human Breast Cancer MCF-7/DOX Cells. Inhibition of Glutathione S-Transferase P1-1 by Glutathione Conjugates from Anthracyclines. Biochem. Pharmacol. 2000; 60: 1915–1923
   PubMed Web of Science ®Google Scholar
• Sinha B.K., Mimnaugh E.G. Free Radicals and Anticancer Drug Resistance-Oxygen Free Radicals in the Mechanism of Drug Cytotoxicity and Resistance by Certain Tumors. Free Radic. Biol. Med. 1990; 8: 567–581
   PubMed Web of Science ®Google Scholar
• Datta K., Kulkarni A.P. Inhibition of Mammalian Hepatic Glutathione S-Transferases by Acetylenic Fatty Acids. Toxicol. Lett. 1994; 73(2)157–165
   PubMed Web of Science ®Google Scholar
• Mitra A., Govindwar S., Joseph P., Kulkarni A. Inhibition of Human Term Placental and Fetal Liver Glutathione-S-transferases by Fatty Acids and Fatty Acid Esters. Toxicol. Lett. 1992; 60(3)281–288
   PubMed Web of Science ®Google Scholar
• Kulkarni A.A., Kulkarni A.P. Retinoids Inhibit Mammalian Glutathione Transferases. Cancer Lett. 1995; 91(2)185–189
   PubMed Web of Science ®Google Scholar
• Van Haaften R.I., Evelo C.T., Haenen G.R., Bast A. Alpha-Tocopherol Inhibits Human Glutathione S-Transferase Pi. Biochem. Biophys. Res. Commun. 2001; 280(3)631–633
   PubMed Web of Science ®Google Scholar
• Van Haaften R.I., Evelo C.T., Penders J., Eijnwachter M.P., Haenen G.R., Bast A. Inhibition of Human Glutathione S-Transferase P1-1 by Tocopherols and Alpha-Tocopherol Derivatives. Biochim. Biophys. Acta 2001; 1548(1)23–28
   PubMed Web of Science ®Google Scholar
• Listowski I. High Capacity Binding by Glutathione S-Transferases and Glucocorticoid Resistance. Structure and Function of Glutathione Transferases, K.D. Tew, C.B. Pickett, T.J. Mantle, B. Mannervik, J.D. Hayes. CRC Press, Boca Raton 1999; 199–209
   Google Scholar
• Ploemen J.H., van Ommen B., van Bladeren P.J. Inhibition of Rat and Human Glutathione S-Transferase Isoenzymes by Ethacrynic Acid and Its Glutathione Conjugate. Biochem. Pharmacol. 1990; 40(7)1631–1635
   PubMed Web of Science ®Google Scholar
• Meyer D.J. Significance of an Unusually Low Km for Glutathione in Glutathione Transferases of the α, μ, and π Classes. Xenobiotica 1993; 23(8)823–834
   PubMed Web of Science ®Google Scholar
• Ouwerkerk-Mahadevan S., van Boom J.H., Dreef T.M., Ploemen J.H., Meyer D.J., Mulder G.J. Glutathione Analogues as Novel Inhibitors of Rat and Human Glutathione S-Transferase Isoenzymes, as Well as of Glutathione Conjugation in Isolated Rat Hepatocytes and in the Rat In Vivo. Biochem. J. 1995; 308(Pt 1)283–290
   PubMedGoogle Scholar
• Ouwerkerk-Mahadevan S., Tirona R.G., Ripping R.A., Ploemen J.H., van Bladeren P.J., Pang K.S., van Boom J.H., Mulder G.J. Inhibition of Glutathione Conjugation by Glutathione Analogues in the Perfused Rat Liver. Effect of Esterification on the Potency of Gamma-l-glutamyl-alpha-(d-2-aminoadipyl)-N-2-heptylamine. Drug Metab. Dispos. 1997; 25(10)1137–1143
   PubMed Web of Science ®Google Scholar
• Ouwerkerk-Mahadevan S., van Boom J.H., Mulder G.J. Isoenzyme-Selective Inhibition of Glutathione Conjugation In Vivo: Selective Inhibition of the Conjugation of S-2-Bromoisovalerylurea in the Rat. J. Pharmacol. Exp. Ther. 1996; 276(3)923–928
   PubMed Web of Science ®Google Scholar
• Koehler R.T., Villar H.O., Bauer K.E., Higgins D.L. Ligand-Based Protein Alignment and Isozyme Specificity of Glutathione S-Transferase Inhibitors. Proteins 1997; 28(2)202–216
   PubMed Web of Science ®Google Scholar
• Morgan A.S., Ciaccio P.J., Tew K.D., Kauvar L.M. Isozyme-Specific Glutathione S-Transferase Inhibitors Potentiate Drug Sensitivity in Cultured Human Tumor Cell Lines. Cancer Chemother. Pharmacol. 1996; 37(4)363–370
   PubMed Web of Science ®Google Scholar
• Chen Y.R., Wang X., Templeton D., Davis R.J., Tan T.H. The Role of c-Jun N-Terminal Kinase (JNK) in Apoptosis Induced by Ultraviolet C and Gamma Radiation. Duration of JNK Activation May Determine Cell Death and Proliferation. J. Biol. Chem. 1996; 271(50)31929–31936
   PubMed Web of Science ®Google Scholar
• van der Kolk D.M., Vellenga E., Muller M., de Vries E.G. Multidrug Resistance Protein MRP1, Glutathione, and Related Enzymes. Their Importance in Acute Myeloid Leukemia. Adv. Exp. Med. Biol. 1999; 457: 187–198
   PubMed Web of Science ®Google Scholar
• Satoh K. Weak Electrophile Selective Characteristics of the Rat Preneoplastic Marker Enzyme Glutathione S-Transferase P-Form, GST-P(7-7): A Theory of Linear Free Energy Relationships for Evaluation of the Active Site Hydrophobicity of Isoenzymes. Carcinogenesis 1998; 19(9)1665–1671
   PubMed Web of Science ®Google Scholar
• Satoh K., Sato R., Takahata T., Suzuki S., Hayakari M., Tsuchida S., Hatayama I. Quantitative Differences in the Active-Site Hydrophobicity of Five Human Glutathione S-Transferase Isoenzymes: Water-Soluble Carcinogen-Selective Properties of the Neoplastic GSTP1-1 Species. Arch. Biochem. Biophys. 1999; 361(2)271–276
   PubMed Web of Science ®Google Scholar
• Berhane K., Widersten M., Engstrom A., Kozarich J.W., Mannervik B. Detoxication of Base Propenals and Other Alpha, Beta-Unsaturated Aldehyde Products of Radical Reactions and Lipid Peroxidation by Human Glutathione Transferases. Proc. Natl Acad. Sci. USA 1994; 91(4)1480–1484
   PubMed Web of Science ®Google Scholar
• Smith G.C.M., Jackson S.P. The DNA-Dependent Protein Kinase. Gen. Dev. 1999; 13: 916–934
   PubMed Web of Science ®Google Scholar
• Lees-Miller S.P. The DNA-Dependent Protein Kinase, DNA-PK: 10 Years and No Ends in Sight. Biochem. Cell. Biol. 1996; 74(4)503–512
   PubMed Web of Science ®Google Scholar
• Park S.J., Oh E.J., Yoo M.A., Lee S.H. Involvement of DNA-Dependent Protein Kinase in Regulation of Stress-Induced JNK Activation. DNA Cell. Biol. 2001; 20(10)637–645
   PubMed Web of Science ®Google Scholar
• Hammersten O., Chu G. DNA-Dependent Protein Kinase–DNA Binding and Activation in Absence of Ku. Proc. Natl Acad. Sci. USA 1998; 95: 525–530
   PubMed Web of Science ®Google Scholar
• D'Arpa P., Liu L.F. Topoisomerase Targeting Antitumor Drugs. Biochim. Biophys. Acta 1989; 989: 163–177
   PubMed Web of Science ®Google Scholar
• Shen H., Schultz M., Kruh G.D., Tew K.D. Increased Expression of DNA-Dependent Protein Kinase Confers Resistance to Adriamycin. Biochim. Biophys. Acta 1998; 1381(2)131–138
   PubMed Web of Science ®Google Scholar
• Kim S.H., Um J.H., Dong-Won B., Kwon B.H., Kim D.W., Chung B.S., Kang C.D. Potentiation of Chemosensitivity in Multidrug-Resistant Human Leukemia CEM Cells by Inhibition of DNA-Dependent Protein Kinase Using Wortmannin. Leuk. Res. 2000; 24(11)917–925
   PubMed Web of Science ®Google Scholar
• Martin N.M. DNA Repair Inhibition and Cancer Therapy. J. Photochem. Photobiol. B 2001; 63(1–3)162–170
   PubMed Web of Science ®Google Scholar
• Izzard R.A., Jackson S.P., Smith G.C. Competitive and Noncompetitive Inhibition of the DNA-Dependent Protein Kinase. Cancer Res. 1999; 59(11)2581–2586
   PubMed Web of Science ®Google Scholar
• Rozenzweig K.E., Youmell M.B., Palayoor S.T., Price B.D. Radiosensitization of Human Tumor Cells by the PI 3-Kinase Inhibitors Wortmannin and Ly294002 Correlates with Inhibition of DNA-Dependent Protein Kinase and Prolonged G2-M Delay. Clin. Cancer Res. 1997; 3: 1149–1156
   PubMed Web of Science ®Google Scholar
• Take Y., Kumano M., Hamano Y., Fukatsu H., Teraoka H., Nishimura S., Okuyama A. OK-1035 a Selective Inhibitor of DNA-Dependent Protein Kinase. Biochem. Biophys. Res. Commun. 1995; 215(1)41–47
   PubMed Web of Science ®Google Scholar
• Take Y., Kumano M., Teraoka H., Nishimura S., Okuyama A. DNA-Dependent Protein Kinase Inhibitor (OK-1035) Suppresses p21 Expression in HCT116 Cells Containing Wild-Type p53 Induced by Adriamycin. Biochem. Biophys. Res. Commun. 1996; 221(2)207–212
   PubMed Web of Science ®Google Scholar
• Stockley M., Clegg W., Fontana G., Golding B.T., Martin N., Rigoreau L.J., Smith G.C., Griffin R.J. Synthesis, Crystal Structure Determination, and Biological Properties of the DNA-Dependent Protein Kinase (DNA-PK) Inhibitor 3-Cyano-6-hydrazonomethyl-5-(4-pyridyl)pyrid-[1H]-2-one(OK-1035). Bioorg. Med. Chem. Lett. 2001; 11(21)2837–2841
   PubMed Web of Science ®Google Scholar
• Eriksson A., Yachnin J., Lewensohn R., Nilsson A., Nilsso A. DNA-Dependent Protein Kinase Is Inhibited by Trifluoperazine. Biochem. Biophys. Res. Commun. 2001; 283(4)726–731
   PubMed Web of Science ®Google Scholar
• Shen H., Schultz M.P., Tew K.D. Glutathione Conjugate Interactions with DNA-Dependent Protein Kinase. J. Pharmacol. Exp. Ther. 1999; 290(3)1101–1106
   PubMed Web of Science ®Google Scholar
• Jin S., Kharbanda S., Mayers B., Kufe D., Weaver D.T. Binding of Ku and c-Abl at the Kinase Homology Region of DNA-Dependent Protein Kinase Catalytic Subunit. J. Biol. Chem. 1997; 272: 24763–24766
   PubMed Web of Science ®Google Scholar
• Kumar S., Pandey P., Bharti A., Jin S., Weichselbaum R., Weaver D., Kufe D., Kharbanda S. Regulation of DNA-Dependent Protein Kinase by the Lyn Tyrosine Kinase. J. Biol. Chem. 1998; 273: 25654–25658
   PubMed Web of Science ®Google Scholar
• Thornalley P.J. Advances in Glyoxalase Research. Glyoxalase Expression in Malignancy, Anti-proliferative Effects of Methylglyoxal, Glyoxalase I Inhibitor Diesters and S-d-Lactoylglutathione, and Methylglyoxal-Modified Protein Binding and Endocytosis by the Advanced Glycation Endproduct Receptor. Crit. Rev. Oncol. Hematol. 1995; 20: 99–128
   PubMed Web of Science ®Google Scholar
• Thornalley P.J. Glutathione-Dependent Detoxification of Alpha-Oxoaldehydes by the Glyoxalase System: Involvement in Disease Mechanisms and Antiproliferative Activity of Glyoxalase I Inhibitors. Chem. Biol. Interact. 1998; 111–112: 137–151
   PubMed Web of Science ®Google Scholar
• Larsen K., Aronsson A.C., Marmstal E., Mannervik B. Immunological Comparison of Glyoxalase I from Yeast and Mammals and Quantitative Determination of the Enzyme in Human Tissues by Radioimmunoassay. Comp. Biochem. Physiol. B 1985; 82(4)625–638
   PubMed Web of Science ®Google Scholar
• Mannervik B., Ridderstrom M. Catalytic and Molecular Properties of Glyoxalase I. Biochem. Soc. Trans. 1993; 21(2)515–517
   PubMed Web of Science ®Google Scholar
• Vander Jagt D.L. Glyoxalase II: Molecular Characteristics, Kinetics and Mechanism. Biochem. Soc. Trans. 1993; 21(2)522–527
   PubMed Web of Science ®Google Scholar
• Castro V.M., Siderstrom M., Carlberg I., Widersten M., Platz A., Mannervik B. Differences Among Human Tumor Cell Lines in the Expression of Glutathione Transferase and Other Glutathione-Linked Enzymes. Carcinogenesis 1990; 11: 1569–1576
   PubMed Web of Science ®Google Scholar
• Ayoub F.M., Zaman M.A., Thornalley P.J. Glyoxalase Activity in Human Tumour Cell Lines In Vitro. Biochem. Soc. Trans. 1993; 21: 176S
   PubMedGoogle Scholar
• Ranganathan S., Tew K. Analysis of Glyoxalase I from Normal and Tumour Tissue from Human Colon. Biochim. Biophys. Acta 1994; 1170: 17–24
   Google Scholar
• Sakamoto H., Mashima T., Kizaki A., Dan S., Hashimoto Y., Naito M., Tsuruo T. Glyoxalase I Is Involved in Resistance of Human Leukemia Cells to Antitumor Induced Apoptosis. Blood 2000; 95: 3214–3218
   PubMed Web of Science ®Google Scholar
• Dills W.L. Nutritional and Physiological Consequences of Tumour Glycolysis. Parasitology 1993; 107: S177–S186
   PubMed Web of Science ®Google Scholar
• Vince R., Wadd W.B. Glyoxalase Inhibitors as Potential Anticancer Agents. Biochem. Biophys. Res. Commun. 1969; 35: 593–598
   PubMed Web of Science ®Google Scholar
• Ayoub F.M., Zaman M.A., Thornalley P.J. Glyoxalase Activities in Human Tumour Cell Lines In Vitro. Anticancer Res. 1993; 13: 151–156
   PubMed Web of Science ®Google Scholar
• Vince R., Daluge S., Wadd W.B. Studies on the Inhibition of Glyoxalase I by S-Substituted Glutathiones. J. Med. Chem. 1971; 14(5)402–404
   PubMed Web of Science ®Google Scholar
• Lo T.W.C., Thornalley P.J. Inhibition of Proliferation of Human Leukemia 60 Cells by Diethyl Esters of Glyoxalase Inhibitors In Vitro. Biochem. Pharmacol. 1992; 44: 2357–2363
   PubMed Web of Science ®Google Scholar
• Conroy P.J. Carcinostatic Activity of Methylglyoxal and Related Substances in Tumour Bearing Mice. Ciba Found. Symp. 1979; 67: 271–298
   Google Scholar
• Thornalley P.J., Ladan M.J., Ridgway S.J., Kang Y. Antitumor Activity of S-(p-Bromobenzyl)Glutathione Diesters In Vitro: A Structure–Activity Study. J. Med. Chem. 1996; 39(17)3409–3411
   PubMed Web of Science ®Google Scholar
• Thornalley P.J., Edwards L.G., Kang Y., Wyatt C., Davies N., Ladan M.J., Double J. Antitumour Activity of S-p-Bromobenzylglutathione Cyclopentyl Diester In Vitro and In Vivo. Inhibition of Glyoxalase I and Induction of Apoptosis. Biochem. Pharmacol. 1996; 51(10)1365–1372
   PubMed Web of Science ®Google Scholar
• Doweyko A.M. The Hypothetical Active Site Lattice. An Approach to Modelling Active Sites from Data on Inhibitor Mechanism. J. Med. Chem. 1988; 31: 1396–1406
   PubMed Web of Science ®Google Scholar
• Klopman G., Dimayuga M.L. Computer Automated Structure Evaluation of Flavonoids and Other Structurally Related Compounds as Glyoxalase I Enzyme Inhibitors. Mol. Pharmacol. 1988; 34: 218–222
   PubMed Web of Science ®Google Scholar
• Thomson C., Higgins D., Edge C. Theorectic Studies of the Electrostatic Potential of Some Enzyme Inhibitors Using Computer Graphics Techniques. J. Mol. Graphics 1988; 6: 171–177
   Google Scholar
• Thomson C., Brandt R. Theoretical Investigations of the Structure of Potential Inhibitors of the Enzyme Glyoxalase I. Int. J. Quantum Chem. 1983; 10: 357–373
   Google Scholar
• Cameron A.D., Olin B., Ridderstrom M., Mannervik B., Jones T.A. Crystal Structure of Human Glyoxalase I—Evidence for Gene Duplication and 3D Domain Swapping. EMBO J. 1997; 16: 3386–3395
   PubMed Web of Science ®Google Scholar
• Johansson A.S., Ridderstrom M., Mannervik B. The Human Glutathione Transferase P1-1 Specific Inhibitor TER 117 Designed for Overcoming Cytostatic-Drug Resistance Is Also a Strong Inhibitor of Glyoxalase I. J. Pharmacol. Exp. Ther. 2000; 57: 619–624
   Google Scholar
• Ridderstrom M., Cameron A.D., Jones T.A., Mannervik B. Mutagenesis of Residue 157 in the Active Site of Human Glyoxalase I. Biochem. J. 1997; 328: 231–235
   PubMed Web of Science ®Google Scholar
• Ridderstrom M., Jemth P., Cameron A.D., Mannervik B. The Active-Site Residue Tyr-175 in Human Glyoxalase II Contributes to Binding of Glutathione Derivatives. Biochim. Biophys. Acta 2000; 1481(2)344–348
   PubMed Web of Science ®Google Scholar
• Cameron A.D., Ridderstrom M., Olin B., Kavarana M.J., Creighton D.J., Mannervik B. Reaction Mechanism of Glyoxalase I Explored by an X-Ray Crystallographic Analysis of the Human Enzyme in Complex with a Transition State Analogue. Biochemistry 1999; 38: 13480–13490
   PubMed Web of Science ®Google Scholar
• Hamilton D.S., Creighton D.J. Inhibition of Glyoxalase I by the Enediol Mimic S-(N-Hydroxy-N-methylcarbamoyl)Glutathione. The Possible Basis of a Tumor-Selective Anticancer Strategy. J. Biol. Chem. 1992; 267(35)24933–24936
   PubMed Web of Science ®Google Scholar
• Kalsi A., Kavarana M.J., Lu T., Whalen D.L., Hamilton D.S., Creighton D.J. Role of Hydrophobic Interactions in Binding S-(N-Aryl/Alkyl-N-hydroxycarbamoyl) Glutathiones to the Active Site of the Antitumor Target Enzyme Glyoxalase I. J. Med. Chem. 2000; 43: 3981–3986
   PubMed Web of Science ®Google Scholar
• Sharkey E.M., O'Neill H.B., Kavarana M.J., Wang H., Creighton D.J., Sentz D.L., Eiseman J.L. Pharmacokinetics and Antitumor Properties in Tumor-Bearing Mice of an Enediol Analogue Inhibitor of Glyoxalase I. Cancer Chemother. Pharmacol. 2000; 46(2)156–166
   PubMed Web of Science ®Google Scholar
• Lo T.W., Thornalley P.J. Inhibition of Proliferation of Human Leukaemia 60 Cells by Diethyl Esters of Glyoxalase Inhibitors In Vitro. Biochem. Pharmacol. 1992; 44(12)2357–2363
   PubMed Web of Science ®Google Scholar
• Al Timari A., Douglas K.T. Inhibition by Glutathione Derivatives of Bovine Liver Glyoxalase II (Hydroxyacylglutathione Hydrolase) as a Probe of the N- and S-Sites for Substrate Binding. Biochim. Biophys. Acta 1986; 870(2)219–225
   PubMed Web of Science ®Google Scholar
• Lo T.W., Thornalley P.J. Inhibition of Human Leukaemia 60 Cell Growth by Diethyl Esterification of the Glyoxalase II Inhibitor S-p-Nitrobenzoxycarbonylglutathione In Vitro. Biochem. Soc. Trans. 1993; 21(2)159S
   PubMedGoogle Scholar
• Thornalley P.J., Tisdale M.J. Inhibition of Proliferation of Human Promyelocytic Leukemia HL60 Cells by S-d-Lactoyl-glutathione. Leuk. Res. 1988; 12: 897–904
   PubMed Web of Science ®Google Scholar
• Edwards L.G., Clelland J.D., Thornalley P.J. Characteristics of the Inhibition of Human Promyelocytic Leukemia HL60 Cell-Growth by S-D-Lactoylglutathione In Vitro. Leuk. Res. 1993; 17(4)305–310
   PubMed Web of Science ®Google Scholar
• Reeves M.E., Thornalley P.J. The Hydrolysis of S-d-Latoyl-glutathione. Biochem. Soc. Trans. 1993; 21: 169S
   PubMedGoogle Scholar
• Christopherson R.I., Schmalzl K.J., Szabados E., Goodridge R.J., Harsanyi M.C., Sant M.E., Algar E.M., Anderson J.E., Armstrong A., Sharma S.C. Mercaptan and Dicarboxylate Inhibitors of Hamster Dihydroorotase. Biochemistry 1989; 28(2)463–470
   PubMed Web of Science ®Google Scholar
• Edwards L.G., Thornalley P.J. Prevention of S-d-Lactoylglutathione-induced Inhibition of Human Leukaemia 60 Cell Growth by Uridine. Leuk. Res. 1994; 18(9)717–722
   PubMed Web of Science ®Google Scholar
• Edwards L.G., Adesida A., Thornalley P.J. Inhibition of Human Leukaemia 60 Cell Growth by S-d-Lactoylglutathione In Vitro. Mediation by Metabolism to N-d-Lactoylcysteine and Induction of Apoptosis. Leuk. Res. 1996; 20(1)17–26
   PubMed Web of Science ®Google Scholar
• Witz G. Biological Interactions of a,b-Unsaturated Aldehydes. J. Free Radic. Biol. Med. 1989; 7: 333–349
   Google Scholar
• Ploemen J.H., Van Schanke A., van Ommen B., van Bladeren P.J. Reversible Conjugation of Ethacrynic Acid with Glutathione and Human Glutathione S-Transferase P1-1. Cancer Res. 1994; 54(4)915–919
   PubMed Web of Science ®Google Scholar
• Ishikawa T., Kobayashi K., Sogame Y., Hayashi K. Evidence for Leukotriene C4 Transport Mediated by an ATP-Dependent Glutathione S-Conjugate Carrier in Rat Heart and Liver Plasma Membranes. FEBS Lett. 1989; 29(1)95–98
   Google Scholar
• Ishikawa T. The ATP-Dependent Glutathione S-Conjugate Export Pump. Trends Biochem. Sci. 1992; 17(11)463–468
   PubMed Web of Science ®Google Scholar
• Leier I., Jedlitschky G., Buchholz U., Cole S.P., Deeley R.G., Keppler D. The MRP Gene Encodes an ATP Dependent Export Pump for Leukotriene C4 and Structurally Related Conjugates. J. Biol. Chem. 1994; 269(45)27807–27810
   PubMed Web of Science ®Google Scholar
• Martinoia E., Grill E., Tommassini R., Kreuz K., Amrhein N. ATP-Dependent Glutathione S-Conjugate “Export” Pump in Vacuolar Membrane of Plants. Nature 1993; 364: 247–249
   Web of Science ®Google Scholar
• Muller M., Meijer C., Zaman G.J., Borst P., Scheper R.J., Mulder N.H., de Vries E.G., Jansen P.L. Overexpression of the Gene Encoding the Multidrug Resistance-Associated Protein Results in Increased ATP-Dependent Glutathione S-Conjugate Transport. Proc. Natl Acad. Sci. USA 1994; 91(26)13033–13037
   PubMed Web of Science ®Google Scholar
• Jedlitschky G., Leier I., Buchholz U., Center M., Keppler D. ATP-Dependent Transport of Glutathione S-Conjugates by the Multidrug Resistance-Associated Protein. Cancer Res. 1994; 54(18)4833–4836
   PubMed Web of Science ®Google Scholar
• Ishikawa T., Tien Kuo M., Furuta K., Suzuki M. The Human Multidrug Resistance-Associated Protein (MRP) Gene Family: From Biological Function to Drug Molecular Design. Clin. Chem. Lab. Med. 2000; 38(9)893–897
   PubMed Web of Science ®Google Scholar
• Borst P., Evers R., Kool M., Wijnholds J. A Family of Drug Transporters: The Multidrug Resistance-Associated Proteins. J. Natl Cancer Inst. 2000; 92(16)1295–1302
   PubMed Web of Science ®Google Scholar
• Renes J., de Vries E.G., Jansen P.L., Muller M. The (Patho)Physiological Functions of the MRP Family. Drug Resist. Updat. 2000; 3(5)289–302
   PubMed Web of Science ®Google Scholar
• Leslie E.M., Deeley R.G., Cole S.P. Toxicological Relevance of the Multidrug Resistance Protein 1. MRP1 (ABCC1) and Related Transporters. Toxicology 2001; 167(1)3–23
   PubMed Web of Science ®Google Scholar
• Rappa G., Lorico A., Flavell R.A., Sartorelli A.C. Evidence That the Multidrug Resistance Protein (MRP) Functions as a Co-transporter of Glutathione and Natural Product Toxins. Cancer Res. 1997; 57(23)5232–5237
   PubMed Web of Science ®Google Scholar
• Loe D.W., Deeley R.G., Cole S.P. Characterization of Vincristine Transport by the M(r) 190,000 Multidrug Resistance Protein (MRP): Evidence for Cotransport with Reduced Glutathione. Cancer Res. 1998; 58(22)5130–5136
   PubMed Web of Science ®Google Scholar
• Zaman G.J., Lankelma J., van Tellingen O., Beijnen J., Dekker H., Paulusma C., Oude Elferink R.P., Baas F., Borst P. Role of Glutathione in the Export of Compounds from Cells by the Multidrug-Resistance-Associated Protein. Proc. Natl Acad. Sci. USA 1995; 92(17)7690–7694
   PubMed Web of Science ®Google Scholar
• Paulusma C.C., van-Geer M.A., Evers R., Heijn M., Ottenhoff R., Borst P., Oude E.R. Canalicular Multispecific Organic Anion Transporter/Multidrug Resistance Protein 2 Mediates Low-Affinity Transport of Reduced Glutathione. Biochem. J. 1999; 338(Pt 2)393–401
   PubMed Web of Science ®Google Scholar
• Leier I., Jedlitschky G., Buchholz U., Center M., Cole S.P., Deeley R.G., Keppler D. ATP-Dependent Glutathione Disulphide Transport Mediated by the MRP Gene-Encoded Conjugate Export Pump. Biochem. J. 1996; 314(Pt 2)433–437
   PubMed Web of Science ®Google Scholar
• Heijn M., Hooijberg J.H., Scheffer G.L., Szabo G., Westerhoff H.V., Lankelma J. Anthracyclines Modulate Multidrug Resistance Protein (MRP) Mediated Organic Anion Transport. Biochim. Biophys. Acta 1997; 1326(1)12–22
   PubMed Web of Science ®Google Scholar
• König J., Nies A.T., Cui Y., Leier I., Keppler D. Conjugate Export Pumps of the Multidrug Resistance Protein (MRP) Family: Localization, Substrate Specificity, and MRP2-Mediated Drug Resistance. Biochim. Biophys. Acta 1999; 1461(2)377–394
   PubMed Web of Science ®Google Scholar
• Loe D.W., Deeley R.G., Cole S.P.C. Biology of the Multidrug Resistance-Associated Protein, MRP. Eur. J. Cancer 2002; 32A: 945–957
   Google Scholar
• Flens M.J., Zaman G.J., van der Valk P., Izquierdo M.A., Schroeijers A.B., Scheffer G.L., de Haas M., Meijer C.J.L.M., Scheper R.J. Tissue Distribution of the Multidrug Resistance Associated Protein. Am. J. Pathol. 1996; 148: 1237–1247
   PubMed Web of Science ®Google Scholar
• Deeley R.G., Cole S.P.C. Function, Evolution and Structure of the Multidrug Resistance Protein (MRP). Semin. Cancer Biol. 1997; 8: 193–204
   PubMed Web of Science ®Google Scholar
• Keppler D., König J. Expression and Localization of the Conjugate Export Pump Encoded by the MRP2 (cMRP/CMOAT) Gene in Liver. FASEB J. 1997; 11: 509–516
   PubMed Web of Science ®Google Scholar
• Schaub T.P., Kartenbeck J., Konig J., Vogel O., Witzgall R., Kriz W., Keppler D. Expression of the Conjugate Export Pump Encoded by the MRP2 Gene in the Apical Membrane of Kidney Proximal Tubules. J. Am. Soc. Nephrol. 1997; 8: 1213–1221
   PubMed Web of Science ®Google Scholar
• Jansen P.L.M., Peters W.H., Lamers W.H. Hereditary Chronic Conjugated Hyperbilirubinemia in Mutant Rats Caused by Defective Hepatic Anion Transport. Hepatology 1985; 5: 573–579
   PubMed Web of Science ®Google Scholar
• Mikami T., Nozaki T., Tagaya O. The Characteristics of a New Mutant in Rats with Hyperbilirubinurea Syndrome. Congenital Anom. 1986; 26: 250–251
   Google Scholar
• Paulusma C.C., Kool M., Bosma P.J., Scheffer G.L., Ter Borg F., Scheper R.J., Tytgat G.N., Borst P., Baas F., Oude Elferink R.P. A Mutation in the Human Canalicular Multispecific Organic Anion Transporter Gene Causes the Dubin-Johnson Syndrome. Hepatology 1997; 25: 1539–1542
   PubMed Web of Science ®Google Scholar
• Gottesman M.M., Pastan I. Biochemistry of Multidrug Resistance Mediated by the Multidrug Transporter. Annu. Rev. Biochem. 1993; 62: 385–427
   PubMed Web of Science ®Google Scholar
• McGrath T., Center M.S. Adriamycin Resistance in HL60 Cells in the Absence of Detectable P-Glycoprotein. Biochem. Biophys. Res. Commun. 1987; 145: 1171–1176
   PubMed Web of Science ®Google Scholar
• Mirski S.E., Gerlach J.H., Cole S.P.C. Multidrug Resistance in a Human Small Cell Lung Cancer Cell Line Selected in Adriamycin. Cancer Res. 1987; 47: 2594–2598
   PubMed Web of Science ®Google Scholar
• Cole S.P.C., Bhardwaj G., Gerlach J.H. Overexpression of a Transporter Gene in a Multidrug-Resistant Human Lung Cancer Cell Line. Science 1992; 258: 1650–1654
   PubMed Web of Science ®Google Scholar
• Hipfner D.R., Deeley R.G., Cole S.P. Structural, Mechanistic and Clinical Aspects of MRP1. Biochim. Biophys. Acta 1999; 1461(2)359–376
   PubMed Web of Science ®Google Scholar
• Litman T., Druley T.E., Stein W.D., Bates S.E. From MDR to MXR: New Understanding of Multidrug Resistance Systems, Their Properties and Clinical Significance. Cell. Mol. Life Sci. 2001; 58(7)931–959
   PubMed Web of Science ®Google Scholar
• Ota E., Abe Y., Oshika Y., Ozeki Y., Iwasaki M., Inoue H., Yamazaki H., Ueyama Y., Takagi K., Ogata T., Tamaoki N., Nakamura M. Expression of the Multidrug Resistance-Associated Protein (MRP) Gene in Non-small Cell Lung Cancer. Br. J. Cancer 1995; 72: 550–554
   PubMed Web of Science ®Google Scholar
• Nooter K., Brutel De La Riviere G., Klijn J., Stoter G., Foekens J. Multidrug Resistance Protein in Recurrent Breast Cancer. Lancet 1997; 349: 1885–1886
   PubMed Web of Science ®Google Scholar
• Filipits M., Stranzl T., Pohl G., Suchomel R.W., Zochbauer S., Brunner R. MRP Expression in Acute Myeloid Leukemia, an Update. Adv. Exp. Med. Biol. 1999; 457: 141–150
   PubMed Web of Science ®Google Scholar
• Arts H.J., Katsaros D., de Vries E.G., Massobrio M., Genta F., Danese S., Arisio R., Scheper R.J., Kool M., Scheffer G.L., Willemse P.H., van der Zee A.G., Suurmeijer A.J. Drug Resistance-Associated Markers P-Glycoprotein, Multidrug Resistance-Associated Protein 1, Multidrug Resistance-Associated Protein 2, and Lung Resistance Protein as Prognostic Factors in Ovarian Carcinoma. Clin. Cancer Res. 1999; 5(10)2798–2805
   PubMed Web of Science ®Google Scholar
• Yokoyama Y., Sato S., Fukushi Y., Sakamoto T., Futagami M., Saito Y. Significance of Multi-drug-resistant Proteins in Predicting Chemotherapy Response and Prognosis in Epithelial Ovarian Cancer. J. Obstet. Gynaecol. Res. 1999; 25(6)387–394
   PubMedGoogle Scholar
• Lorico A., Nesland J., Emilsen E., Fodstad O., Rappa G. Role of the Multidrug Resistance Protein 1 Gene in the Carcinogenicity of Aflatoxin B1: Investigations Using MRP1-Null Mice. Toxicology 2002; 171(2–3)201–205
   PubMed Web of Science ®Google Scholar
• Koike K., Kawabe T., Tanaka T., Toh S., Uchiumi T., Wada M. A Canalicular Multispecific Organic Anion Transporter (cMOAT) Antisense cDNA Enhances Drug Sensitivity in Human Hepatic Cancer Cells. Cancer Res. 1997; 57: 5475–5479
   PubMed Web of Science ®Google Scholar
• Cui Y., Konig J., Buchholz J.K., Spring H., Leier I., Keppler D. Drug Resistance and ATP Dependent Conjugate Transport Mediated by the Apical Multidrug Resistance Protein. MRP2, Permanently Expressed in Human and Canine Cells. Mol. Pharmacol. 1999; 55: 929–937
   PubMed Web of Science ®Google Scholar
• Hooijberg J.H., Broxterman H.J., Kool M., Assaraf Y.G., Peters G.J., Noordhuis P., Scheper R.J., Borst P., Pinedo H.M., Jansen G. Antifolate Resistance Mediated by the Multidrug Resistance Proteins MRP1 and MRP2. Cancer Res. 1999; 59: 2532–2535
   PubMed Web of Science ®Google Scholar
• Schaub T.P., Kartenbeck J., König J., Spring H., Dörsam J., Staeler G., Störkel S., Thon W.F., Keppler D. Expression of the MRP2 Gene-Encoded Conjugate Export Pump in Human Kidney Proximal Tubules and in Renal Cell Carcinoma. J. Am. Soc. Nephrol. 1999; 10: 1159–1169
   PubMed Web of Science ®Google Scholar
• Kim H.S., Min Y.D., Choi C.H. Double-Edged Sword of Chemosensitizer: Increase of Multidrug Resistance Protein (MRP) in Leukemic Cells by an MRP Inhibitor Probenecid. Biochem. Biophys. Res. Commun. 2001; 283(1)64–71
   PubMed Web of Science ®Google Scholar
• Ford J.M., Yang J.M., Hait W.N. Effect of Buthionine Sulfoximine on Toxicity of Verapamil and Doxorubicin to Multidrug Resistant Cells and to Mice. Cancer Res. 1991; 51: 67–72
   PubMed Web of Science ®Google Scholar
• O'Dwyer P.J., Hamilton T.C., LaCreta F.P., Gallo J.M., Kilpatrick D., Halbherr T., Brennan J., Bookman M.A., Hoffman J., Young R.C., Comis R.L., Ozols R.F. Phase I Trial of Buthionine Sulfoximine in Combination with Melphalan in Patients with Cancer. J. Clin. Oncol. 1996; 14(1)249–256
   PubMed Web of Science ®Google Scholar
• Bailey H.H., Mulcahy R.T., Tutsch K.D., Arzoomanian R.Z., Alberti D., Tombes M.B., Wilding G., Pomplun M., Spriggs D.R. Phase I. Clinical Trial of Intravenous l-Buthionine Sulfoximine and Melphalan: An Attempt at Modulation of Glutathione. J. Clin. Oncol. 1994; 12(1)194–205
   PubMed Web of Science ®Google Scholar
• Leslie E.M., Mao Q., Oleschuk C.J., Deeley R.G., Cole S.P. Modulation of Multidrug Resistance Protein 1 (MRP1/ABCC1) Transport and Atpase Activities by Interaction with Dietary Flavonoids. Mol. Pharmacol. 2001; 59(5)1171–1180
   PubMed Web of Science ®Google Scholar
• Hooijberg J.H., Broxterman H.J., Heijn M., Fles D.L.A., Lankelma J., Pinedo H.M. Modulation by (Iso)Flavonoids of the Atpase Activity of the Multidrug Resistance Protein. FEBS Lett. 1997; 413: 344–348
   PubMed Web of Science ®Google Scholar
• Hooijberg J.H., Broxterman H.J., Scheffer G.L., Vrasdonk C., Heijn M., de Jong M.C., Scheper R.J., Lankelma J., Pinedo H.M. Potent Interaction of Flavopiridol with MRP1. Br. J. Cancer 1999; 81(2)269–276
   PubMed Web of Science ®Google Scholar
• Walgren R.A., Karnaky K.J., Jr., Lindenmayer G.E., Walle T. Efflux of Dietary Flavonoid Quercetin 4′-Beta-Glucoside Across Human Intestinal Caco-2 Cell Monolayers by Apical Multidrug Resistance-Associated Protein-2. J. Pharmacol. Exp. Ther. 2000; 294(3)830–836
   PubMed Web of Science ®Google Scholar
• Walle U.K., Galijatovic A., Walle T. Transport of the Flavonoid Chrysin and Its Conjugated Metabolites by the Human Intestinal Cell Line Caco-2. Biochem. Pharmacol. 1999; 58(3)431–438
   PubMed Web of Science ®Google Scholar
• Hollo Z., Homolya L., Hegedus T., Sarkadi B. Transport Properties of the Multidrug Resistance-Associated Protein (MRP) in Human Tumour Cells. FEBS Lett. 1996; 383(1–2)99–104
   PubMed Web of Science ®Google Scholar
• Payen L., Courtois A., Campion J.P., Guillouzo A., Fardel O. Characterization and Inhibition by a Wide Range of Xenobiotics of Organic Anion Excretion by Primary Human Hepatocytes. Biochem. Pharmacol. 2000; 60: 1967–1975
   PubMed Web of Science ®Google Scholar
• Gollapudi S., Thadepalli F., Kim C.H., Gupta S. Difloxacin Reverses Multidrug Resistance in HL-60/AR Cells That Overexpress the Multidrug Resistance-Related Protein (MRP) Gene. Oncol. Res. 1995; 7(5)213–225
   PubMed Web of Science ®Google Scholar
• Courtois A., Payen L., Vernhet L., de Vries E.G., Guillouzo A., Fardel O. Inhibition of Multidrug Resistance-Associated Protein (MRP) Activity by Rifampicin in Human Multidrug-Resistant Lung Tumor Cells. Cancer Lett. 1999; 139: 97–104
   PubMed Web of Science ®Google Scholar
• Terashi K., Oka M., Soda H., Fukuda M., Kawabata S., Nakatomi K., Shiozawa K., Nakamura T., Tsukamoto K., Noguchi Y., Suenaga M., Tei C., Kohno S. Interactions of Ofloxacin and Erythromycin with the Multidrug Resistance Protein (MRP) in MRP-Overexpressing Human Leukemia Cells. Antimicrob. Agents Chemother. 2000; 44(6)1697–1700
   PubMed Web of Science ®Google Scholar
• Klokouzas A., Barrand M.A., Hladky S.B. Effects of Clotrimazole on Transport Mediated by Multidrug Resistance Associated Protein 1 (MRP1) in Human Erythrocytes and Tumour Cells. Eur. J. Biochem. 2001; 268(24)6569–6577
   PubMedGoogle Scholar
• Gekeler V., Ise W., Sanders K.H., Ulrich W.R., Beck J. The Leukotriene LTD4 Receptor Antagonist MK571 Specifically Modulates MRP Associated Multidrug Resistance. Biochem. Biophys. Res. Commun. 1995; 208(1)345–352
   PubMed Web of Science ®Google Scholar
• Nakano R., Oka M., Nakamura T., Fukuda M., Kawabata S., Terashi K., Tsukamoto K., Noguchi Y., Soda H., Kohno S. A Leukotriene Receptor Antagonist, ONO-(1078) Modulates Drug Sensitivity and Leukotriene C4 Efflux in Lung Cancer Cells Expressing Multidrug Resistance Protein. Biochem. Biophys. Res. Commun. 1998; 251(1)307–312
   PubMed Web of Science ®Google Scholar
• Evers R., Kool M., Smith A.J., van Deemter L., de Haas M., Borst P. Inhibitory Effect of the Reversal Agents V-104, GF120918 and Pluronic L61 on MDR1 Pgp-, MRP1- and MRP2-Mediated Transport. Br. J. Cancer 2000; 83(3)366–374
   PubMed Web of Science ®Google Scholar
• Miller D.W., Batrakova E.V., Kabanov A.V. Inhibition of Multidrug Resistance-Associated Protein (MRP) Functional Activity with Pluronic Block Copolymers. Pharm. Res. 1999; 16(3)396–401
   PubMed Web of Science ®Google Scholar
• Payen L., Delugin L., Courtois A., Trinquart Y., Guillouzo A., Fardel O. The Sulphonylurea Glibenclamide Inhibits Multidrug Resistance Protein (MRP1) Activity in Human Lung Cancer Cells. Br. J. Pharmacol. 2001; 132: 778–784
   PubMed Web of Science ®Google Scholar
• Ren X.Q., Furukawa T., Aoki S., Nakajima T., Sumizawa T., Haraguchi M., Chen Z.S., Kobayashi M., Akiyama S. Glutathione-Dependent Binding of a Photoaffinity Analog of Agosterol A to the C-Terminal Half of Human Multidrug Resistance Protein. J. Biol. Chem. 2001; 276(25)23197–23206
   PubMed Web of Science ®Google Scholar
• Chen Z.S., Aoki S., Komatsu M., Ueda K., Sumizawa T., Furukawa T., Okumura H., Ren X.Q., Belinsky M.G., Lee K., Kruh G.D., Kobayashi M., Akiyama S. Reversal of Drug Resistance Mediated by Multidrug Resistance Protein (MRP) 1 by Dual Effects of Agosterol A on MRP1 Function. Int. J. Cancer 2001; 93(1)107–113
   PubMed Web of Science ®Google Scholar
• Chen Z.S., Furukawa T., Sumizawa T., Ono K., Ueda K., Seto K., Akiyama S.I. ATP-Dependent Efflux of CPT-11 and SN-38 by the Multidrug Resistance Protein (MRP) and Its Inhibition by PAK-104P. Mol. Pharmacol. 1999; 55(5)921–928
   PubMed Web of Science ®Google Scholar
• Chuman Y., Chen Z.S., Seto K., Sumizawa T., Furukawa T., Tani A., Haraguchi M., Niwa K., Yamada K., Aikou T., Akiyama S. Reversal of MRP-Mediated Vincristine Resistance in KB Cells by Buthionine Sulfoximine in Combination with PAK-104P. Cancer Lett. 1998; 129(1)69–76
   PubMed Web of Science ®Google Scholar
• Sumizawa T., Chen Z.S., Chuman Y., Seto K., Furukawa T., Haraguchi M., Tani A., Shudo N., Akiyama S.I. Reversal of Multidrug Resistance-Associated Protein-Mediated Drug Resistance by the Pyridine Analog PAK-104P. Mol. Pharmacol. 1997; 51(3)399–405
   PubMed Web of Science ®Google Scholar
• Norman B.H., Dantzig A.H., Kroin J.S., Law K.L., Tabas L.B., Shepard R.L., Palkowitz A.D., Hauser K.L., Winter M.A., Sluka J.P., Starling J.J. Reversal of Resistance in Multidrug Resistance Protein (MRP1)-Overexpressing Cells by LY329146. Bioorg. Med. Chem. Lett. 1999; 9(23)3381–3386
   PubMed Web of Science ®Google Scholar
• Seelig A., Blatter X.L., Wohnsland F. Substrate Recognition by P-Glycoprotein and the Multidrug Resistance-Associated Protein MRP1: A Comparison. Int. J. Clin. Pharmacol. Ther. 2000; 38(3)111–121
   PubMed Web of Science ®Google Scholar
• Ishikawa T. ATP/Mg2+-Dependent Cardiac Transport System for Glutathione S-Conjugates. A Study Using Rat Heart Sarcolemma Vesicles. J. Biol. Chem. 1989; 264(29)17343–17348
   PubMed Web of Science ®Google Scholar
• Ito K., Olsen S.L., Qiu W., Deeley R.G., Cole S.P. Mutation of a Single Conserved Tryptophan in Multidrug Resistance Protein 1 (MRP1/ABCC1) Results in Loss of Drug Resistance and Selective Loss of Organic Anion Transport. J. Biol. Chem. 2001; 276(19)15616–15624
   PubMed Web of Science ®Google Scholar
• Furuta K., Tomokiyo K., Tien Kuo M., Ishikawa T., Suzuki M. Molecular Design of Glutathione-Derived Biochemical Probes Targeting the GS-X Pump. Tetrahedron 1999; 55: 7529–7540
   Web of Science ®Google Scholar
• Leslie E.M., Ito K., Upadhyaya P., Hecht S.S., Deeley R.G., Cole S.P.C. Transport of the b-O-Glucuronide Conjugate of the Tobacco-Specific Carcinogen 4-(Methylnitrosamino)-1-(3-pyridyl)-1-butanol (NNAL) by the Multidrug Resistance Protein 1 (MRP1). J. Biol. Chem. 2001; 276(30)27846–27854
   PubMed Web of Science ®Google Scholar
• O'Brien M.L., Vulevic B., Freer S., Boyd J., Shen H., Tew K.D. Glutathione Peptidomimetic Drug Modulator of Multidrug Resistance-Associated Protein. J. Pharmacol. Exp. Ther. 1999; 291(3)1348–1355
   PubMed Web of Science ®Google Scholar
• Meister A., Tate S.S., Ross L.L. Membrane-Bound γ-Glutamyl Transpeptidase. The Enzymes of Biological Membranes, A. Martonosi, 1990; 315–347
   Google Scholar
• Hanigan M.H. Gamma-Glutamyl Transpeptidase, a Glutathionase: Its Expression and Function in Carcinogenesis. Chem. Biol. Interact. 1998; 111–112: 333–342
   PubMed Web of Science ®Google Scholar
• McIntyre T.M., Curthoys N.P. Renal Catabolism of Glutathione—Characterization of a Particulate Rat Renal Dipeptidase That Catalyzes the Hydrolysis of Cysteinylglycine. J. Biol. Chem. 1982; 257: 11915–11921
   PubMed Web of Science ®Google Scholar
• Commandeur J.N., Stijntjes G.J., Vermeulen N.P. Enzymes and Transport Systems Involved in the Formation and Disposition of Glutathione S-Conjugates. Role in Bioactivation and Detoxication Mechanisms of Xenobiotics. Pharmacol. Rev. 1995; 47(2)271–330
   PubMed Web of Science ®Google Scholar
• Hanigan M.H., Frierson H.F. Immunohistochemical Detection of γ-Glutamyl Transpeptidase in Normal Human Tissues. J. Histochem. Cytochem. 1996; 44: 1101–1108
   PubMed Web of Science ®Google Scholar
• Lieberman M.W., Wiseman A.L., Shi Z.Z., Carter B.Z., Barrios R.J., Ou Z.N., Chevez-Barrios P., Wand Y., Habib G.M., Goodman J.C., Huang S.L., Lebovitz R.M., Matzuk M.M. Growth Retardation and Cysteine Deficiency in γ-Glutamyl Transpeptidase-Deficient Mice. Proc. Natl Acad. Sci. USA 1996; 93: 7923–7926
   PubMed Web of Science ®Google Scholar
• Will Y., Fischer K.A., Horton R.A., Kaetzel R.S., Brown M.K., Hedstrom O., Lieberman M.W., Reed D.J. Gamma-Glutamyltranspeptidase-Deficient Knockout Mice as a Model to Study the Relationship Between Glutathione Status, Mitochondrial Function, and Cellular Function. Hepatology 2000; 32(4 Pt 1)740–749
   PubMed Web of Science ®Google Scholar
• Meister A. Mitochondrial Changes Associated with Glutathione Deficiency. Biochim. Biophys. Acta 1995; 1271: 35–42
   PubMed Web of Science ®Google Scholar
• Chen X., Carystinos G.D., Batist G. Potential for Selective Modulation of Glutathione in Cancer Chemotherapy. Chem. Biol. Interact. 1998; 111–112: 263–275
   PubMed Web of Science ®Google Scholar
• Schroder C.P., Godwin A.K., O'Dwyer P.J., Tew K., Hamilton T.C., Ozols R.F. Glutathione and Drug Resistance. Cancer Investig. 1996; 14(2)158–168
   PubMed Web of Science ®Google Scholar
• Komlosh A., Volohonsky G., Porat N., Tuby C., Bluvshtein E., Steinberg P., Oesch F., Stark A.A. γ-Glutamyl Transpeptidase and Glutathione Biosynthesis in Non-tumorigenic and Tumorigenic Rat Liver Oval Cell Lines. Carcinogenesis 2001; 22(12)2009–2016
   PubMed Web of Science ®Google Scholar
• Hanigan M.H. Expression of Gamma-Glutamyl Transpeptidase Provides Tumors with a Selective Growth Advantage of Physiologic Concentrations of Cyst(e)ine. Carcinogenesis 1995; 16: 181–185
   PubMed Web of Science ®Google Scholar
• Selvaraj P., Balasubramanian K.A., Hill P.G. Isolation of Gamma-Glutamyl Transpeptidase from Human Primary Hepatoma and Comparison of Its Kinetic and Catalytic Properties with the Enzyme from Normal Adult and Fetal Liver. Enzyme 1981; 26(2)57–63
   PubMedGoogle Scholar
• Tennenbaum T., Weiner A.K., Belanger A.J., Glick A.B., Hennings H., Yuspa S.H. The Suprabasal Expression of Alpha 6 Beta 4 Integrin Is Associated with a High Risk for Malignant Progression in Mouse Skin Carcinogenesis. Cancer Res. 1993; 53(20)4803–4810
   PubMed Web of Science ®Google Scholar
• Hanigan M.H., Frierson H.F., Swanson P.E., deYoung B.R. Altered Expression of Gamma-Glutamyl Transpeptidase in Human Tumors. Hum. Pathol. 1999; 30: 300–305
   PubMed Web of Science ®Google Scholar
• deYoung B.R., Frierson H.F., Swanson P.E., Hanigan M.H. γ-Glutamyl Transpeptidase Immunoreactivity in Human Neoplasia. Lab. Invest. 1996; 74, meeting abstract 840
   Web of Science ®Google Scholar
• Durham J.R., Frierson H.F., Hanigan M.H. Glutamyl Transpeptidase Immunoreactivity in Benign and Malignant Breast Tissue. Breast Cancer Res. Treat. 1997; 45: 55–62
   PubMed Web of Science ®Google Scholar
• Lewis A.L., Hayes J.D., Wolf C.R. Glutathione and Glutathione Dependent Enzymes in Ovarian Adenocarcinoma Cell Lines Derived from a Patient Before and After the Onset of Drug Resistance: Intrinsic Differences and Cell Cycle Effects. Carcinogenesis 1988; 9: 1283–1287
   PubMed Web of Science ®Google Scholar
• Godwin A.K., Meister A., O'Dwyer P.J., Huang C.S., Hamilton T.C., Anderson M.E. High Resistance to Cisplatin in Human Ovarian Cancer Cell Lines Is Associated with Marked Increase of Glutathione Synthesis. Proc. Natl Acad. Sci. USA 1992; 89: 3070–3074
   PubMed Web of Science ®Google Scholar
• Lau H.M., Lewis A.D., Ehsan M.N., Sikic B.I. Multifactorial Mechanisms Associated with Broad Cross-resistance of Ovarian Cancer Cells Selected by Cyanomorpholino Doxorubicin. Cancer Res. 1991; 51: 5181–5187
   PubMed Web of Science ®Google Scholar
• Ikeda Y., Fujii J., Anderson M.E., Tanaguchi N., Meister A. Involvement of Ser-451 and Ser-452 in the Catalysis of Human γ-Glutamyl Transpeptidase. J. Biol. Chem. 1995; 270: 22223–22228
   PubMed Web of Science ®Google Scholar
• Inoue M., Hiratake J., Suzuki H., Kumagai H., Sakaa L. Identification of Catalytic Nucleophile of E. Coli γ-Glutamyl Transpeptidase by γ-Monofluorophosphono Derivative of Glutamic Acid-N-terminal Thr-391 in Small Subunit Is the Nucleophile. Biochemistry 2000; 39: 7764–7771
   PubMed Web of Science ®Google Scholar
• Neil G.L., Berger A.E., McPartland R.P., Grindley G.B., Bloch A. Biochemical and Pharmacological Effects of the Fermentation-Derived Antitumor Agent, (AlphaS5S)-Alpha-amino-3-chloro-4,5-dihydro-5-isoxazoleacetic Acid (AT-125). Cancer Res. 1979; 39: 852–856
   PubMed Web of Science ®Google Scholar
• Gardell S.J., Tate S.S. Affinity Labeling of Gamma-Glutamyl Transpeptidase by Glutamine Antagonists. Effects of the Gamma-Glutamyl Transferase and Proteinase Activities. FEBS Lett. 1980; 122(2)171–174
   PubMed Web of Science ®Google Scholar
• Capraro M.A., Hughey R.P. Use of Acivicin in the Determination of Rate Constants for Turnover of Rat Renal Gamma-Glutamyltranspeptidase. J. Biol. Chem. 1985; 260(6)3408–3412
   PubMed Web of Science ®Google Scholar
• Elfarra A.A., Anders M.W. Renal Processing of Glutathione Conjugates. Role in Nephrotoxicity. Biochem. Pharmacol. 1984; 33(23)3729–3732
   PubMed Web of Science ®Google Scholar
• Monks T.J., Lau S.S., Highet R.J., Gillette J.R. Glutathione Conjugates of 2-Bromohydroquinone Are Nephrotoxic. Drug Metab. Dispos. 1985; 13(5)553–559
   PubMed Web of Science ®Google Scholar
• Hochwald S.N., Harrison L.E., Rose D.M., Anderson M.E., Burt M.E. γ-Glutamyl Transpeptidase Mediation of Tumor Glutathione Utilization In Vivo. J. Natl Cancer Inst. 1996; 88(3/4)193–197
   PubMed Web of Science ®Google Scholar
• Tate S.S., Meister A. Affinity Labeling of Gamma-Glutamyl Transpeptidase and Location of the Gamma-Glutamyl Binding Site on the Light Subunit. Proc. Natl Acad. Sci. USA 1977; 74(3)931–935
   PubMed Web of Science ®Google Scholar
• Tate S.S., Ross M.E. Human Kidney Gamma-Glutamyl Transpeptidase. Catalytic Properties, Subunit Structure, and Localization of the Gamma-Glutamyl Binding Site on the Light Subunit. J. Biol. Chem. 1977; 252(17)6042–6045
   PubMed Web of Science ®Google Scholar
• Stein R.L., DeCicco C., Nelson D., Thomas B. Slow Binding Inhibition of γ-Glutamyl Transpeptidase by γ-Boroglu. Biochemistry 2001; 40: 5804–5811
   PubMed Web of Science ®Google Scholar
• London R.E., Gabel S.A. Development and Evaluation of a Boronate Inhibitor of Gamma-Glutamyl Transpeptidase. Arch. Biochem. Biophys. 2001; 385(2)250–258
   PubMed Web of Science ®Google Scholar
• Aberkane H., Frank P., Galteau M.M., Wellman M. Acivicin Induces Apoptosis Independently of Gamma-Glutamyltranspeptidase Activity. Biochem. Biophys. Res. Commun. 2001; 285(5)1162–1167
   PubMed Web of Science ®Google Scholar
• Lyons S.D., Sant M.E., Christopherson R.I. Cytotoxic Mechanisms of Glutamine Antagonists in Mouse L1210 Leukemia. J. Biol. Chem. 1990; 265(19)11377–11381
   PubMed Web of Science ®Google Scholar
• Bluvshtein E., Glass G.A., Volohonsky G., Yaakubowitz M., Harness E., Smorodinsky N.I., Seidel A., Frank H., Steinberg P., Stark A.A. Inhibition of the Hydrolytic and Transpeptidase Activities of Rat γ-Glutamyl Transpeptidase by Specific Monoclonal Antibodies. Eur. J. Biochem. 1999; 260: 844–854
   PubMedGoogle Scholar
• Chang M., Zhang F., Shen L., Pauss N., Alam I., van Breemen R.B., Blond S.Y., Bolton J.L. Inhibition of Glutathione S-Transferase Activity by the Quinoid Metabolites of Equine Estrogens. Chem. Res. Toxicol. 1998; 11: 758–765
   PubMed Web of Science ®Google Scholar
• Chang M., Shin Y.G., van Breemen R.B., Blond S.Y., Bolton J.L. Structural and Functional Consequences of Inactivation of Human Glutathione S-Transferase P1-1 Mediated by the Catechol Metabolite of Equine Estrogens, 4-Hydroxyequilerin. Biochemistry 2001; 40: 4811–4820
   PubMed Web of Science ®Google Scholar