Advanced search
Publication Cover
Critical Reviews in Biochemistry and Molecular Biology Volume 30, 1995 - Issue 6
Submit an article Journal homepage
4,591
Views
2,465
CrossRef citations to date
0
Altmetric
Research Article

The Glut athione S-Transferase Supergene Family: Regulation of GST and the Contribution of the lsoenzymes to Cancer Chemoprotection and Drug Resistance Part I

John D. Hayes Biomedical Research Centre, Ninewells Hospital and Medical School, University of Dundee, Dundee, DD1 9SY, Scotland, UK
&
David J. Pulford Biomedical Research Centre, Ninewells Hospital and Medical School, University of Dundee, Dundee, DD1 9SY, Scotland, UK
Pages 445-520 | Published online: 26 Sep 2008

References

  • Ames B. N., Profet M., Gold L. S. Dietary pesticides (99.99% all natural). Proc. Natl. Acad. Sci. U.S.A 1990; 87: 7777–7781
  • Profet Ames B. N., Gold L. S. Nature's chemicals and synthetic chemicals: comparative toxicology. Proc. Natl. Acad. Sci. U.S.A 1990; 87: 7782–7786
  • Halliwell B., Gutteridge J. M. C. Free Radicals in Biology and Medicine. Clarendon Press, Oxford 1985
  • Nebert D. W., Petersen D. D., Fornace A. J. Cellular responses to oxidative stress: the [Ah]gene battery as a paradigm. Environ. Health Perspect 1990; 88: 13–25
  • Gottesman M. M., Pastan I. Biochemistry of multidrug resistance mediated by the multidrug transporter. Annu. Rev. Biochem 1993; 62: 385–427
  • Hanna P. M., Kadiiska M. B., Jordan S. J., Mason R. P. Role of metallo-thionein in zinc(II) and chromium(III) mediated tolerance to carbon tetrachloride hepatotoxicity: evidence against a trichloro-methyl radical-scavenging mechanism. Chem. Res. Toxicol 1993; 6: 711–717
  • Satoh M., Kondo Y., Mita M., Naka-gawa I., Naganuma A., Imura N. Prevention of carcinogenicity of anticancer drugs by metallothionein induction. Cancer Res 1993; 53: 4767–4768
  • Jakoby W. B. Enzymatic Basis of Detoxification. Academic Press, San Diego 1980; Vol. I
  • Jakoby W. B. Enzymatic Basis of Detoxification. Academic Press, San Diego 1980; Vol. II
  • Fox M., Roberts J. J. Drug resistance and DNA repair. Cancer Metast. Rev 1987; 6: 261–281
  • Sancar A., Sancar G. B. DNA repair enzymes. Ann. Rev. Biochem 1988; 57: 29–67
  • Tanaka K., Wood R. D. Xeroderma pigmentosum and nucleotide excision repair of DNA. Trends Biol. Sci 1994; 19: 83–86
  • Guengerich F. P. Oxidation of toxic and carcinogenic chemicals by human cyto-chrome P-450 enzymes. Chem. Res. Toxicol 1991; 4: 391–407
  • Cholerton S., Daly A. K., Idle J. R. The role of individual human cytochromes P450 in drug metabolism and clinical response. Trends Pharmacol. Sci 1992; 13: 434–439
  • Korzekwa K. R., Jones J. P. Predicting the cytochrome P450 mediated metabolism of xenobiotics. Pharmacogenetics 1993; 3: 1–18
  • Mannervik B., Danielson U. H. Glu-tathione transferases- structure and catalytic activity. Crit. Rev. Biochem. Mol. Biol 1988; 23: 283–337
  • Bock K. W. Roles of UDP-Glucurono-syltransferases in chemical carcinogenesis. Crit. Rev. Biochem. Mol. Biol 1991; 26: 129–150
  • Falany C. N. Molecular enzymology of human liver cytosolic sulphotransferases. Trends Pharmacol. Sci 1991; 12: 255–259
  • Meijer J., DePierre J. W. Cytosolic epoxide hydrolase. Chem.-Biol. Interact 1988; 64: 207–249
  • Cadenas E. Antioxidant and prooxidant functions of DT-diaphorase in quinone metabolism. Biochem. Pharmacol 1995; 49: 127–140
  • Rosen D. R., Siddique T., Patterson D., Figlewicz D. A., et al. Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis. Nature 1993; 362: 59–62
  • Orr C. W., Sohal R. S. Extension of lifespan by overexpression of superoxide dismutase and catalase i Drosophifa melanogaster. Science 1994; 263: 1128–1130
  • Sies H. Strategies of antioxidant defense. Eur. J. Biochem 1993; 215: 213–219
  • Doroshow J. H., Esworthy R. S., Chu F. F., Akrnan S. Glutathione peroxi-dase and resistance to oxidative stress. Structure and Function of Glutathione Transferases, K. D. Tew, C. B. Pickett, T. J. Mantle, B. Mannervik, J. D. Hayes. CRC Press, Boca Raton, FL 1993; 269–277
  • Lavoie L., Tremblay A., Mirault M.-E. Distinct oxidoresistance phenotype of human T47D cells transfected by rat glutathione S-transferase Yc expression vectors. J. Biol. Chem 1992; 267: 3632–3636
  • Berhane K., Widersten M., Engström A., Kozarich J. W., Mannervik B. Detoxication of base propenals and other α,β-unsaturated aldehyde products of radical reactions and lipid peroxidation by human glutathione transferases. Proc. Natl. Acad. Sci. U.S.A 1994; 91: 1480–1484
  • Canuto R. A., Muzio G., Maggiora M., Biocca M. E., Dianzani M. B. Glu-tathione-S-transferase, alcohol dehydroge-nase and aldehyde reductase activities during diethylnitrosamine-carcinogenesis in rat liver. Cancer Lett 1993; 68: 177–183
  • Robson C. N., Milne A. M., Pappin D. J. C., Hickson I. D. Isolation of cDNA clones encoding an enzyme from bovine cells that repairs oxidative DNA damage in vitro: homology with bacterial repair enzymes. Nucleic Acid Res 1991; 19: 1087–1092
  • Hayes J. D., Wolf C. R. Molecular mechanisms of drug resistance. Biochem. J 1990; 272: 281–295
  • Listowsky I., Abrarnovitz M., Homma H., Niitsu Y. Intracellular binding and transport of hormones and xenobiotics by glutathione S-transferases. Drug Met. Rev 1988; 19: 305–318
  • Pickett C. B., Telakowski-Hopkins C. A., Argenbright L, Lu A. Y. H. Regulation of glutathione S-transferase mRNAs by phenobarbital and 3-methyl-cholanthrene: analysis using cDNA probes. Biochem. Soc. Trans 1984; 12: 71–74
  • Prochaska H. J., Talalay P. Regulatory mechanisms of monofunctional and bifunctional anticarcinogenic enzyme in-ducers in murine liver. Cancer Res 1988; 48: 4776–4782
  • Talalay P., De Long M. J., Prochaska H. J. Identification of a common chemical signal regulating the induction of enzymes that protect against chemical carcinogenesis. Proc. Natl. Acad. Sci. U.S.A 1988; 85: 8261–8265
  • Talalay P., Spencer S. R. Regulation of the induction of glutathione transferases and NAD(P)H:Quinone reductase by glutathione transferase substrates. Glutathione S-Transferases and Drug Resistance, J. D. Hayes, C. B. Pickett, T. J. Mantle. Taylor and Francis, London 1990; 176–185
  • Spencer S. R., Xue L., Klenz E. M., Talalay P. The potency of inducers of NAD(P)H:(quinone-acceptor) oxidoreduc-tase parallels their efficiency as substrates for glutathione transferases. Structural and electronic correlations. Biochem. J 1991; 273: 711–717
  • Hayes J. D., Judah D. J., Neal G. E. Resistance to aflatoxin B, is associated with the expression of a novel aldo-keto reductase which has catalytic activity towards a cytotoxic aldehyde-containing metabolite of the toxin. Cancer Res 1993; 53: 3887–3894
  • Ellis E. M., Judah D. J., Neal G. E., Hayes J. D. An ethoxyquin-inducible aldehyde reductase from rat liver that metabolizes aflatoxin B1defines a subfamily of aldo-keto reductases. Proc. Nail. Acad. Sci. U.S.A 1993; 90: 10350–10354
  • Mandel H. G., Manson M. M., Judah D. J., Simpson J. L., Green J. A., Forrester L. M., Wolf C. R., Neal G. E. Metabolic basis for the protective effect of the antioxidant ethoxyquin on aflatoxin B1hepatocarcinogenesis in the rat. Cancer Res 1987; 47: 5218–5223
  • Davies R., Edwards R. E., Green J. A., Legg R. F., Snowden R. T., Manson M. M. Antioxidants can delay liver cell maturation which in turn affects γ-glutamyltranspeptidase expression. Carcinogenesis 1993; 14: 47–52
  • Borroz K. I., Buetler T. M., Eaton D. L. Modulation of γ-glutamylcysteine synthetase large subunit mRNA expression by butylated hydroxyanisole. Toxicol. Appl. Pharmacol 1994; 126: 150–155
  • Mulcahy R. T., Untawale S., Gipp J. J. Transcriptional up-regulation of γ-glutamylcysteine synthetase gene expression in melphalan-resistant human prostate carcinoma cells. Mol. Pharmacol 1994; 46: 909–914
  • Guthenber gWarholm M., Mannervik B., von Bahr C., Glaumann H. Identification of a new glutathione S-trans-ferase in human liver. Acta Chem. Scand 1980; 34: 607–610
  • Board P., Coggan M., Johnston P., Ross V., Suzuki T., Webb G. Genetic heterogeneity of the human glutathione S-transferases: a complex of gene families. Pharmacol. Ther 1990; 48: 357–369
  • Pemble S., Schroeder K. R., Spencer S. R., Meyer D. J., Hallier E., Bolt H. M., Ketterer B., Taylor J. B. Human glutathione S-transferase Theta (GSTT1): cDNA cloning and the characterization of a genetic polymorphism. Biochem. J 1994; 300: 271–276
  • Dolan C. Regulation of Mouse Hepatic Glutathione S-Transferases. Ph.D. thesis, University of Edinburgh. 1990
  • Armstrong R. N. Glutathione S-transferases: structure and mechanism of an archetypical detoxication enzyme. Adv. Enzymol. Relat. Areas Mol. Biol 1994; 69: 1–44
  • Chen W.-J, Graminski G. F., Armstrong R. N. Dissection of the catalytic mechanism of isoenzyme 4–4 of glutathione S-transferases with alternative substrates. Biochemistry 1988; 27: 647–654
  • Graminski G. F., Kubo Y., Armstrong R. N. Spectroscopic and kinetic evidence for the thiolate anion of glutathione at the active site of glutathione S-transferase. Biochemistry 1989; 28: 3562–3568
  • Graminski G. F., Zhang P., Sesay M. A., Amrnon H. L., Armstrong R. N. Formation of the 1-(S-glutathionyl)-2,4,6-trinitrocyclohexadienate anion at the active site of glutathione S-transferase. Biochemistry 1989; 28: 6252–6258
  • Huskey S., Huskey W. P., Lu A. Y. H. Contributions of thiolate “desolvation” to catalysis by glutathione S-transferase isoenzymes 1–1 and 2–2: evidence from kinetic solvent isotope effects. J. Am. Chem. Soc 1991; 113: 2283–2290
  • Reinemer P., Dirr H. W., Ladenstein R., Schaffer J., Gallay O., Huber R. The three-dimensional structure of class glutathione S-transferase in complex with glutathione sulfonate at 2.3 A resolution. EMBO J 1991; 10: 1997–2005
  • Ji X., Zhang P., Armstrong R. N., Gilliland G. L. The three-dimensional structure of a glutathione S-transferase from the Mu gene class. Structural analysis of the binary complex of isoenzyme 3–3 and glutathione at 2.2 A resolution. Biochemistry 1992; 31: 10169–10184
  • Liu S., Zhang P., Ji X., Johnson W. W., Gilliland G. L., Armstrong R. N. Contribution of tyrosine 6 to the catalytic mechanism of isoenzyme 3–3 of glutathione S-transferase. J. Biol. Chem 1992; 267: 4296–4299
  • Sinning I., Kleywegt G. J., Cowan S. W., Reinemer P., Dirr H. W., Huber R., Gilliland G. L., Armstrong R. N., Ji X., Board P. G., Olin B., Mannervik B., Jones T. A. Structure determination and refinement of human alpha class glutathione transferase Al-l, and a comparison with the mu and pi class enzymes. J. Mol. Biol 1993; 232: 192–212
  • Wilce M. C. J., Board P. G., Feil S. C., Parker M. W. Crystal structure of a theta-class glutathione transferase. EMBO J 1995; 14: 2133–2143
  • Jakoby W. B. The glutathione S-transferases: a group of multifunctional detoxication proteins. Adv. Enzymol 1978; 46: 383–414
  • Adang A. E. P., Meyer D. J., Brussee J., Van derGen A., Ketterer B., Mulder G. J. Interaction of rat glutathione S-transferases 7–7 and 8–8 with gamma-glutamyl- or glycyl-modified glutathione analogues. Biochem. J 1989; 264: 759–764
  • Mannervik B. The isoenzymes of glutathione transferase. Adv. Enzymol. Rel. Areas Mol. Biol 1985; 57: 357–417
  • Chasseaud L. F. The role of glutathione and glutathione S-transferases in the metabolism of chemical carcinogens and other electrophilic agents. Adv. Cancer Res 1979; 29: 175–274
  • Nicholson D. W., Ali A., Vaillancourt J. P., Calaycay J. R., Mumford R. A., Zamboni R. J., Ford-Hutchinson A. W. Purification to homogeneity and the N-terminal sequence of human leukotriene C, synthase: a homodirneric glutathione S-transferase composed of 18-kDa subunits. Proc. Natl. Acad. Sci. U.S.A 1993; 90: 2015–2019
  • Chang M., Hong Y., Burgess J. R., Tu C.-P. D., Reddy C. C. Isozyme specificity of rat liver glutathione S-transferases in the formation of PGF2α and PGE2from PGH2. Arch. Biochem. Biophys 1987; 259: 548–557
  • Urade Y., Fujimoto N., Ujihara M., Hayaishi O. Biochemical and immunological characterization of rat spleen prostaglandin D synthetase. J. Biol. Chem 1987; 262: 3820–3825
  • Clark A. G., Smith J. N., Speir T. W. Cross specificity in some vertebrate and insect glutathione S-transferases with methyl parathion (dimethyl p-nitrophenyl phosphorothionate), l-chloro-2,4-dini-trobenzene and S-crotonyl-N-cysteamine as substrates. Biochem. J 1973; 135: 385–392
  • Habig W. H., Jakoby W. B. Assays for differentiation of glutathione S-transferases. Methods Enzymol 1981; 77: 398–405
  • Ishikawa T. The ATP-dependent glutathione S-conjugate export pump. Trends Biochem. Sci 1992; 17: 463–468
  • Zimniak P., Ziller S. A., Panfil I., Radominska A., Wolters H., Kuipers F., Sharma R., Saxena M., Moslen M. T., Vore M., Vonk R., Awasthi Y. C., Lester R. Identification of an anion-transport ATPase that catalyzes glutathione conjugate-dependent ATP hydrolysis in canalicular plasma membranes from normal rats and rats with conjugated hyperbilirubinernia (GY mutant). Arch. Biochem. Biophys 1992; 292: 534–538
  • Leier I., Jedlitschky G., Buchholz U., Cole S. P. C., Deeley R. G., Keppler D. The MRPgene encodes an ATP-dependent export pump for leukotriene C4and structurally related conjugates. J. Biol. Chem 1994; 269: 27807–27810
  • Martinoia E., Grill E., Tommasini R., Kreuz K., Amrhein N. ATP-dependent glutathione S-conjugate “export” pump in the vacuolar membrane of plants. Nature 1993; 364: 247–249
  • Ishikawa T. ATP/Mg2+-dependent cardiac transport system for glutathione S-conjugates. A study using rat heart sar-colemrna vesicles. J. Biol. Chem 1989; 264: 17343–17348
  • Ishikawa T., Ali-Osman F. Glu-tathione-associatedcis-diamminedichloro-platinum(II) metabolism and ATP-dependent efflux from leukemia cells. J. Biol. Chem 1993; 268: 20116–20125
  • Ishikawa T., Wright C. D., Ishizuka H. GS-Xpump is functionally over expressed in cis-diamminedichloroplatinum (11)-resistant human leukemia HL-60 cells and down-regulated by cell differentiation. J. Biol. Chem 1994; 269: 29085–29093
  • Oude Elferink R. P. J., Ottenhoff R., Liefting W., de Haan J., Jansen P. L. M. Hepatobiliary transport of glu-tathione and glutathione conjugate in rats with hereditary hyperbilirubinemia. J. Clin. Invest 1989; 84: 476–483
  • Heijn M., Oude Elferink R. P. J., Jansen P. L. M. ATP-dependent multi-specific organic anion transport system in rat erythrocyte membrane vesicles. Am. J. Physiol 1992; 262: C104–110
  • Awasthi Y. C., Saxena M., Sharma R., Sharma R., Singhal S. S., Ahmad H. Role of glutathione S-transferase and dinitrophenyl S-glutathione ATPase (Dnp-SG ATPase) in the protection of membranes from xenobiotics and oxidative stress. Int. J. Toxicol. Occup. Environ. Hlth 1992; 1: 77–83
  • Saxena M., Singhal S. S., Awasthi S., Singh S. V., Labelle E. F., Zimniak P., Awasthi Y. C. Dinitrophenyl S-glu-tathione ATPase purified from human muscle catalyses ATP hydrolysis in the presence of leukotrienes. Arch. Biochem. Biophys 1992; 298: 231–237
  • Awasthi S., Singhal S. S., Srivastava S. K., Zimniak P., Bajpai K. K., Saxena M., Sharma R., Ziller I II, Frenkel E. P., Singh S. V., He N. G., Awasthi Y. C. Adenosine triphosphate-dependent transport of doxorubicin, daunomycin, and vinblastine in human tissues by a mechanism distinct from the P-glycoprotein. J. Clin. Invest 1994; 93: 958–965
  • Cole S. P. C., Bhardwaj G., Gerlach J. H., Nlackie J. E., Grant C. E., Almquist K. C., Stewart A. J., Kurz E. U., Duncan A. M. V., Deeley R. G. Overexpression of a transporter gene in a multidrug-resistant human cancer cell line. Science 1992; 258: 1650–1654
  • Grant C. E., Valdimarsson G., Hipfner D. R., Almquist K. C., Cole S. P. C., Deeley R. G. Overexpression of multidrug resistance-associated protein (MRP) increases resistance to natural product drugs. Cancer Res 1994; 54: 357–361
  • Kruh G. D., Chan A., Myers K., Gaughan K., Miki T., Aaronson S. A. Expression complementary DNA library transfer establishes mrpas a multidrug resistance gene. Cancer Res 1994; 54: 1649–1652
  • Jedlitschky G., Leier I., Buchholz U., Center M., Keppler D. ATP-dependent transport of glutathione S-conju-gates by the multidrug resistance-associated protein. Cancer Res 1994; 54: 4833–4836
  • Müller M., Meijer C., Zaman G. J. R., Borst P., Scheper R. J., Mulder N. H., de Vries E. G. E., Jansen P. L. M. Overexpression of the gene encoding the multidrug resistance-associated protein results in increased ATP-dependent glutathione S-conjugate transport. Proc. Natl. Acad. Sci. U.S.A 1994; 91: 13033–13037
  • Ballatori N., Truong A. T. Multiple canalicular transport mechanisms for glutathione S-conjugates. Transport on both ATP- and voltage-dependent carriers. J. Biol. Chem 1995; 270: 3594–3601
  • Saxena M., Henderson G. B. ATP-dependent efflux of 2,4-dinitrophenyl-S-glutathione. Properties of two distinct transport systems in inside-out vesicles from L1210 cells and a variant subline with altered efflux of methotrexate and cholate. J, Biol. Chem 1995; 270: 5312–5319
  • Boyland E., Chasseaud L. F. The role of glutathione and glutathione S-trans-ferases in mercapturic acid biosynthesis. Adv. Enzymol 1969; 32: 173–219
  • Vermeulen N. P. E. Analysis of mercapturic acids as a tool in biotransformation, biomonitoring and toxicological studies. Glutathione S-Transferases and Drug Resistance, J. D. Hayes, C. B. Pickett, T. J. Mantle. Taylor and Francis, London 1990; 141–153
  • Alary J., Bravais F., Cravedi J.-P, Debrauwer L., Reo D., Bories G. Mercapturic acid conjugates as urinary end metabolites of the lipid-peroxidation product 4-hydroxy-2-nonenal in the rat. Chem. Res. Toxicol 1995; 8: 34–39
  • Lyttle M. H., Satyam A., Hocker M. D., Bauer K. E., Caldwell C. G., Hui H. C., Morgan A. S., Mergia A., Kauvar L. M. Glutathione S-transferase activates novel alkylating agents. J. Med. Chem 1994; 37: 1501–1507
  • Keen J. H., Jakoby W. B. Glutathione transferases. Catalysis of nucleo-philic reactions of glutathione. J. Biol. Chem 1978; 253: 5654–5657
  • van Bladeren P. J., van Ommen B., Vos R. M. E. Toxication reactions catalysed by GST: inhibition of GST by reactive conjugates. Glutathione S-Trans-ferases and Drug Resistance, J. D. Hayes, C. B. Pickett, T. J. Mantle. Taylor and Francis, London 1990; 131–140
  • van Bladeren P. J., Scheffer A. G., Vos R. M. E., Bruggeman I. M., Temmink J. H. M. The interaction of allyl and benzyl isothiocyanate and rat liver glutathione S-transferases. Glutathione S-Transferases and Carcino-genesis, T. J. Mantle, C. B. Pickett, J. D. Hayes. Taylor and Francis, London 1987; 235–237
  • Zhang Y., Kolm R. H., Mannervik B., Talalay P. Reversible conjugation of isothiocyanates with glutathione catalysed by human glutathione transferases. Biochem. Biophys. Res. Commun 1995; 206: 748–755
  • Meyer D. J., Crease D. J., Ketterer B. Forward and reverse catalysis and product sequestration by human glutathione S-transferases in the reaction of GSH with dietary aralkyl isothiocyanates. Biochem. J 1995; 306: 565–569
  • Baillie T. A., Kassahun K. Reversibility in glutathione-conjugate formation. Adv. Pharmacol 1994; 27: 163–181
  • Slatter J. G., Rashed M. S., Pearson P. G., Han D.-H., Baillie T. A. Biotransformation of methyl isocyanate in the rat. Evidence for glutathione conjugation as a major pathway of metabolism and implications for isocyanate-mediated toxicities. Chem. Res. Toxicol 1991; 4: 157–161
  • Guest I., Baillie T. A., Varma D. R. Toxicity of the methyl isocyanate metabolite S-(N-methylcarbamoyl)GSH on mouse embryos in culture. Teratology 1992; 46: 61–67
  • Rannug U., Sundvall A., Ramel C. The mutagenic effect of 1,2-dichloro-ethane on Salmonella ryphimurium. I. Activation through conjugation with glutathione in vitro. Chem.-Biol. Interactions 1978; 20: 1–16
  • van Bladeren P. J., van der Gen A., Breimer D. D., Mohn G. R. Stereoselective activation of vicinal dihalo-gen compounds by glutathione conjugation. Biochem. Pharmacol 1979; 28: 2521–2524
  • van Bladeren P. J., Breimer D. D., Rotteveel-Smijs G. M. T., de Knijff P., Mohn van Meeteren-Wa G. R., Ulchli B., Buijs W., van der Gen A. The relation between the structure of vicinal dihalogen compounds and their mutagenic activation via conjugation to glutathione. Carcinogenesis 1981; 2: 499–505
  • Graves R. J., Callander R. D., Green T. The role of formaldehyde and S-chloromethylglutathione in the bacterial mutagenicity of methylene chloride. Mutation Res 1994; 320: 235–243
  • Graves R. J., Coutts C., Eyton-Jones H., Green T. Relationship between hepatic DNA damage and methylene chloride-induced hepatocarcinogenicity in B6C3F1 mice. Carcinogenesis 1994; 15: 991–996
  • Graves R. J., Coutts C., Green T. Methylene chloride-induced liver damage; an interspecies comparison. Carcinogenesis 1995; 16: 1919–1926
  • Bogaards J. J. P., van Ommen B., van Bladeren P. J. Interindividual differences in the in vitroconjugation of methylene chloride with glutathione by cytosolic glutathione S-transferase in 22 human liver samples. Biochem. Pharmacol 1993; 45: 2166–2169
  • Ploemen J. H. T., Wormhoudt L. W., van Ommen B., Commandeur J. N. M., Vermeulen V. P. E., van Bladeren P. J. Polymorphism in the glutathione conjugation activity of human erythrocytes towards ethylene dibromide and 1,2-epoxy-3-(p-nitrophenoxy)propane. Biochim. Biophys. Acta 1995; 1243: 469–476
  • Hallier E., Langhof T., Dannappel D., Leutbecher M., Schroder K., Goergens H. W., Muller A., Bolt H. M. Polymorphism of glutathione conjugation of methyl bromide, ethylene oxide and dichloromethane in human blood: influence on the induction of sister chromatid exchanges (SCE) in lymphocytes. Arch. Toxicol 1993; 67: 173–178
  • Thier R., Taylor J. B., Pemble S. E., Humphreys W. G., Persmark M., Ketterer B., Guengerich F. P. Expression of mammalian glutathione S-trans-ferase 5–5 in Salmonella ryphimuriumTA1535 leads to base-pair mutations upon exposure to dihalomethanes. Proc. Natl. Acad. Sci. U.S.A 1993; 90: 8576–8580
  • Thier R., Miiller M., Taylor J. B., Pemble S. E., Ketterer B., Guengerich F. P. Enhancement of bacterial mutagenicity of bifunctional alkylating agents by expression of mammalian glutathione S-trans-ferase. Chem. Res. Toxicol 1995; 8: 465472
  • Anders M. W., Vamvakas S., Dekant W. Bioactivation of haloalkenes through glutathione conjugation. Glutathione S-Transferases and Drug Resistance, J. D. Hayes, C. B. Pickett, T. J. Mantle. Taylor and Francis, London 1990; 121–130
  • Dekant W., Vamvakas S., Anders M. W. Formation and fate of nephrotoxic and cytotoxic glutathione S-conjugates: cysteine conjugate β-lyase pathway. Adv. Pharmacol 1994; 27: 115–162
  • Anderson C., Mosialou E., Weinander R., Morgenstern R. Enzymology of microsomal glutathione S-transferase. Adv. Pharmacol 1994; 27: 19–35
  • Monks T. J., Lau S. S., Highet R. J., Gillette J. R. Glutathione conjugates of 2-bromohydroquinone are nephrotoxic. Drug Met. Dispos 1985; 13: 553–559
  • Habig W. H. Glutathione S-transferases: versatile enzymes of detoxification. Radioprotectors and Anticarcinogens, O. F. Nygaard, M. G. Simic. Academic Press, San Diego 1983; 169–190
  • Mannervik B. Glutathione and the evolution of enzymes for detoxication of products of oxygen metabolism. Chemica Scripta 1986; 26B: 281–284
  • Mosialou E., Ekstrom G., Adang A. E. P., Morgenstern R. Evidence that rat liver microsomal glutathione trans-ferase is responsible for glutathione-dependent protection against lipid peroxidation. Biochem. Pharmacol 1993; 45: 1645–1651
  • Tan K. H., Meyer D. J., Belin J., Ketterer B. Inhibition of microsomal lipid peroxidation by glutathione and glutathione transferases B and AA. Role of endogenous phospholipase A. Biochem. J 1984; 220: 243–252
  • van Kuijk F. J. G., Sevanian A., Handelman G. J., Dratz E. A. A new role for phospholipase A: protection of membranes from lipid peroxidation damage. Trends Biochem. Sci 1987; 12: 31–34
  • Bora P. S., Spilburg C. A., Lange L. G. Metabolism of ethanol and carcinogens by glutathione transferases. Proc. Natl. Acad. Sci. U.S.A 1989; 86: 44704473
  • Sharma R, Gupta S., Singhal S. S., Ahmad H., Haque A., Awasthi Y. C. Independent segregation of glutathione S-transferase and fatty acid ethyl ester synthase from pancreas and other human tissues. Biochem. J 1991; 275: 507–513
  • Board P., Smith S., Green J., Coggan M., Suzuki T. Evidence against a relationship between fatty acid ethyl ester synthase and the Pi class glutathione S-transferase in humans. J. Biol. Chem 1993; 268: 15655–15658
  • Blocki F. A., Schlievert P. M., Wackett L. P. Rat liver protein linking chemical and immunological detoxification systems. Nature 1992; 360: 269–270
  • Blocki F. A., Logan M. S. P., Baoli C., Wackett L. P. Reaction of rat liver glutathione S-transferases and bacterial dichloromethane dehalogenase with dihalomethanes. J. Biol. Chem 1994; 269: 8826–8830
  • Nishihira J., Kuriyama T., Nishino H., Ishibashi T., Sakai M., Nishi S. Purification and characterization of human macrophage migration inhibitory factor: evidence for specific binding to glutathione and formation of subunit structure. Biochem. Mol. Biol. Int 1993; 31: 841–850
  • Hao X.-Y, Widersten M., Ridderström M., Hellman U., Mannervik B. Covariation of glutathione transferase expression and cytostatic drug resistance in HeLa cells: establishment of class Mu glutathione transferase M3–3 as the dominating isoenzyme. Biochem. J 1994; 297: 59–67
  • Ketterer B., Ross-Mansell P., Whitehead J. K. The isolation of carcinogen-binding protein from livers of rats given 4-dimethylaminoazobenzene. Biochem. J 1967; 103: 316–324
  • Jakoby W. B., Keen J. H. A triple-threat in detoxification: the glutathione S-transferases. Trends Biochem. Sci. 1977; 2: 229–231
  • Litwack G., Ketterer B., Arias I. M. Ligandin: a hepatic protein which binds steroids, bilirubin, carcinogens and a number of exogenous organic anions. Nature 1971; 234: 466–467
  • Phillips M. F., Mantle T. J. Inactivation of mouse liver glutathione S-transferase YfYf (Pi class) by ethacrynic acid and 5,5′-dithiobis-(2-nitrobenzoic acid). Biochem. J 1993; 294: 57–62
  • Ploemen J. H. T., 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: 915–919
  • Kirsch R., Fleischner G., Kamisaka K., Arias I. M. Structural and functional studies of ligandin, a major renal organic anion-binding protein. J. Clin. Invest 1975; 55: 1009–1019
  • Hayes J. D., Chalmers J. Bile acid inhibition of basic and neutral glutathione S-transferases in rat liver. Biochem. J 1983; 215: 581–588
  • Hayes J. D., Mantle T. J. Inhibition of hepatic and extrahepatic glutathione S-transferases by primary and secondary bile acids. Biochem. J 1986; 233: 407–415
  • Listowsky I. High capacity binding by glutathione S-transferases and glucocorti-coid 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, FL 1993; 199–209
  • Ishigaki S., Abramovitz M., Listowsky I. Glutathione S-transferases are major cytosolic thyroid hormone binding proteins. Arch. Biochem. Biophys 1989; 273: 265–272
  • Danger D. P., Baldwin W. S., LeBlanc G. A. Photoaffinity labelling of steroid-hormone-binding glutathione S-transferases with [3H]methyltrienolone. Inhibition of steroid-binding activity by the anticarcinogen indole-3-carbinol. Biochem. J 1992; 288: 361–367
  • Meyer D. J. Significance of an unusually low Kmfor glutathione in glutathione transferases of the α, μ and classes. Xenobiotica 1993; 23: 823–834
  • Meyer D. J., Gilmore K. S., Harris J. M., Hartley J. A., Ketterer B. Chlorambucil-monoglutathiony l conj ugate is sequestered by human alpha class glutathione S-transferases. Br. J. Cancer 1992; 66: 433–438
  • Arca P., Rico M., Brana A. F., Villar C. J., Hardisson C., Suárez J. E. Formation of an adduct between fosfomycin and glutathione: a new mechanism of antibiotic resistance in bacteria, Antimicrob. Agents Chemother 1556; 32: 1552
  • La Roche S. D., Leisinger T. Sequence analysis and expression of the bacterial dichloromethane dehalogenase structural gene, a member of the glutathione S-transferase supergene family. J. Bacteriol 1990; 172: 164–171
  • Orser C. S., Dutton J., Lange C., Jablonski P., Xun L., Hargis M. Characterization of a Flavobacteriumglutathione S-transferase gene involved in reductive dechlorination. J. Bacreriol 1993; 175: 2640–2644
  • Sheehan D., Casey J. P. Microbial glutathione S-transferases. Comp. Biochem. Physiol 1993; 104B: 1–6
  • Mignogna G., Allocati N., Aceto A., Piccolomini R., DiIlio C., Barra D., Martini F. The amino acid sequence of glutathione transferase from Proteus mirabilis, a prototype of a new class of enzymes. Eur. J. Biochem 1993; 211: 421–425
  • Masai E., Katayama Y., Kubota S., Kawai S., Yarnasaki M., Morohoshi N. A bacterial enzyme degrading the model lignin compound β-etherase is a member of the glutathione-S-transferase superfam-ily. FEBS Lett 1993; 323: 135–140
  • Nishida M., Kong K.-H, Inoue H., Takahashi K. Molecular cloning and site-directed mutagenesis of glutathione S-transferase from Escherichia coli. The conserved tyrosyl residue near the N terminus is not essential for catalysis. J. Biol. Chem 1985; 269: 32536
  • Tamaki H., Kumagai H., Tochikura T. Glutathione S-transferase in yeast: induction of mRNA, cDNA cloning and expression in Escherichia coli. Biochem Biophys. Res. Commun. 1990; 172: 669–675
  • Tamaki H., Kumagai H., Tochikura T. Nucleotide sequence of the yeast glutathione S-transferase cDNA. Biochim. Biophys. Acta 1991; 1089: 276–279
  • Saxena M., Allarneh A., Mukerji K. G., Raj H. G. Epoxidation of aflatoxin B, by Aspergillus Flavusmicrosomes in vitro: interaction with DNA and formation of aflatoxin B, -glutathione conjugate. Chem.-Biol. Interactions 1991; 78: 13–22
  • Sheehan D., Casey J. P. Evidence for alpha and mu class glutathione S-transferases in a number of fungal species. Comp. Biochem. Physiol 1993; 104B: 7–13
  • Tomarev S. I., Zinovieva R. D. Squid major lens polypeptides are homologous to glutathione S-transferase subunits. Nature 1988; 336: 86–88
  • Tomarev S. I., Zinovieva R. D., Guo K., Piatigorsky J. Squid glutathione S-transferase. Relationships with other glutathione S-transferases and S-crystallins of cephalopods. J. Biol. Chem 1993; 268: 4534–4542
  • Stenersen J., Kobro S., Bjerke M., Arend U. Glutathione transferases in aquatic and terrestrial animals from nine phyla. Comp. Biochem. Physiol 1987; 86C: 73–82
  • Henkle K. J., Davern K. M., Wright M. D., Ramos A. J., Mitchell G. F. Comparison of the cloned genes of the 26–and 28-kilodalton glutathione S-transferases of Schistosoma japonicumand Schistosoma mansoni. Mol. Biochem. Parasitol 1990; 40: 23–34
  • Xu C.-B, Verwaerde C., Gras-Masse H., Fontaine J., Bossus M., Trottein F., Wolowczuk I., Tartar A., Capron A. Schistosoma mansoni28-kDa glutathione S-transferase and immunity against parasite fecundity and egg viability. J. Immunol 1993; 150: 940–949
  • Liebau E., Walter R. D., Henkle-Duhrsen K. Isolation, sequence and expression of an Onchocerca volvulusglutathione S-transferase cDNA. Mol. Biochem. Parasitol 1994; 63: 305–309
  • Liebau E., Schönberger O. L., Walter R. D., Henkle-Duhrsen K. Molecular cloning and expression of a cDNA encoding glutathione S-transferase from Ascaris mum. Mol. Biochem. Parasitol 1900; 63: 167
  • Di Ilio C., Aceto A., Bucciarelli T., Dragani B., Angelucci S., Miranda M., Poma A., Amicarelli F., Barra D., Federici G. Glutathione transferase isoen-zymes from Bifo bufoembryos at an early developmental stage. Biochem. J 1992; 283: 217–222
  • Clark A. G. The comparative enzymol-ogy of the glutathione S-transferases from non-vertebrate organisms. Comp. Biochem. Physiol 1989; 92B: 419–446
  • Toung Y., Hsieh T.-s., Tu C.-P. D. Drosophilaglutathione S-trans-ferase 1–1 shares a region of homology with the maize glutathione S-transferase III. Proc. Natl. Acad. Sci. U.S.A 1990; 87: 31–35
  • Beall C., Fyrberg C., Song S., Fyrberg E. Isolation of a Drosophilagene encoding glutathione S-transferase. Biochem. Genetics 1992; 30: 515–527
  • Fournier D., Bride J. M., Poirie M., Bergé J.-B., Plapp F. W. Insect glutathione S-transferases. Biochemical characteristics of the major forms from houseflies susceptible and resistant to insecticides. J. Biol. Chem 1992; 267: 1840–1845
  • Toung Y., Hsieh T.-s., Tu C.-P. D. The glutathione S-transferase Dgenes. A divergently organized, intronless gene family in. Drosophila melanogaster. J. Biol. Chem 1993; 268: 9737–9746
  • Grove G., Zarlengo R. P., Li K. P., Tam M. F., Tu C. Characterization and heterospecific expression of cDNA clones of genes in the maize GSH S-transferase multigene family. Nucleic Acid Res 1988; 16: 425–438
  • Dudler R., Hertig C., Rebmann G., Bull J., Mauch F. A pathogen-induced wheat gene encodes a protein homologous to glutathione-S-trans-ferases. Mol. Plant-Microbe Interactions 1991; 4: 14–18
  • Meyer R. C., Goldsbrough P. B., Woodson W. R. An ethylene-responsive flower senescence-related gene from carnation encodes a protein homologous to glutathione S-transferases. Plant Mol. Biol 1991; 17: 277–281
  • Droog F. N. J., Hooykaas P. J. J., Libbenga K. R., van der Zaal E. J. Proteins encoded by an auxinregulated gene family of tobacco share limited but significant homology with glutathione S-transferases and one member indeed shows in vitroGST activity. Plant Mol. Biol 1993; 21: 965–972
  • Zhou J., Goldsbrough P. B. An Arabidopsisgene with homology to glutathione S-transferases is regulated by eth-ylene. Plant Mol. Biol 1993; 22: 517–523
  • Zettl R., Schell J., Palme K. Photoaffinity labeling of Arabidopsis thalianaplasma membrane vesicles by 5-azido-[7-3H]indole-3-acetic acid: identification of a glutathione S-transferase. Proc. Natl. Acad. Sci. U.S.A 1994; 91: 689–693
  • Holt D. C., Lay V., Clarke E. D., Dinsmore A., Jepson I., Bright S. W. J., Greenland A. J. Characterization of the safener-induced glutathione S-transferase isoform II from maize. Planta 1995; 196: 295–302
  • Jepson I., Lay V. J., Holt D. C., Bright S. W. J., Greenland A. J. Cloning and characterization of maize herbicide safener induced cDNAs encoding subunits of glutathione S-transferase isoforms I, II and IV. Plant Mol. Biol 1994; 26: 1855–1866
  • Dominey R. J., Nimmo I. A., Cronshaw A. D., Hayes J. D. The major glutathione S-transferase in Salmonid fish livers is homologous to the mammalian pi-class GST. Comp. Biochem. Physiol 1991; 100: 93–98
  • Leaver M. J., Scott K., George S. G. Cloning and characterization of the major hepatic glutathione S-transferase from a marine teleost flatfish, the plaice (Pleuronectes platessa), with structural similarities to plant, insect and mammalian Theta class isoenzymes. Biochem. J 1993; 292: 189–195
  • George S. G. Enzymology and molecular biology of phase II xenobiotic-conjugating enzymes in fish. Aquatic Toxicology: Molecular, Biochemical and Cellular Perspectives, D. C. Malins, G. K. Ostrander. CRC Press, Boca Raton, FL 1994; 37–85
  • Liu L.-F., Tam M. F. Nucleotide sequence of a class μ glutathioneS-transferase from chicken liver. Biochim. Biophys. Acta 1991; 1090: 343–344
  • Chang L.-H, Fan J.-Y, Liu L.-F, Tsai S.-P., Tam M. F. Cloning and expression of a chick liver glutathioneS-transferase CL3 subunit with the use of a baculovirus expression system. Biochem. J 1992; 281: 545–551
  • Hsiao C.-D, Martsen E. O., Lee J.-Y, Tsai S.-P., Tam M. F. Amino acid sequencing, molecular cloning and modeling of chick liver class-Theta glutathioneS-transferase CL1. Biochem. J 1995; 312: 91–98
  • Buetler T. M., Eaton D. L. GlutathioneS-transferases: amino acid sequence comparison, classification and phylogenetic relationship. Environ. Carcinogen. Ecotoxicol Revs 1992; 10: 181–203
  • Mannervik B., Ålin P., Guthenberg C., Jensson H., Tahir M. K., Warholm M., Jörnvall H. Identification of three classes of cytosolic glutathione transferase common to several mammalian species: correlation between structural data and enzymatic properties. Proc. Natl. Acad. Sci. U.S.A 1985; 82: 7202–7206
  • Meyer D. J., Coles B., Pemble S. E., Gilmore K. S., Fraser G. M., Ketterer B. Theta, a new class of glutathione transferases purified from rat and man. Biochem. J 1991; 274: 409–414
  • Meyer D. J., Thomas M. Characterization of rat spleen prostaglandin-H D-isomerase as a sigma class GSH transferase. Biochem. J 1995; 311: 739–742
  • Telakowski-Hopkins C. A., Rothkopf G. S., Pickett C. B. Structural analysis of a rat liver glutathioneS-transferase Ya gene. Proc. Natl. Acad. Sci. U.S.A 1986; 83: 9393–9397
  • Rothkopf G. S., Telakowski-Hopkins C. A., Stotish R. L., Pickett C. B. Multiplicity of glutathioneS-transferase genes in the rat and association with a type 2 Alu repetitive element. Biochemistry 1986; 25: 993–1002
  • Daniel V., Sharon R., Tichauer Y., Sand S. Mouse glutathioneS-transferase Ya subunit: gene structure and sequence. DNA 1987; 6: 317–324
  • Rozen F., Nguyen T., Pickett C. B. Isolation and characterization of the human glutathioneS-transferase Hal subunit gene. Arch. Biochem. Biophys 1992; 292: 589–593
  • Klone A., Hussnätter R., Sies H. Cloning, sequencing and characterization of the human alpha class glutathioneS-transferase gene corresponding to the cDNA clone pGTH2. Biochem. J 1992; 285: 925–928
  • Suzuki T., Johnston P. N., Board P. G. Structure and organization of the human alpha class glutathioneS-transferase genes and related pseudogenes. Genomics 1993; 18: 680–686
  • Lai H. J., Qian B., Grove G., Tu C.-P. D. Gene expression of rat glutathioneS-transferases. Evidence for gene conversion in the evolution of the Ybmultigene family. J. Biol. Chem 1988; 263: 11389–11395
  • Morton M. R., Bayney R. M., Pickett C. B. Isolation and characterization of the rat glutathioneS-transferase Yb1subunit gene. Arch. Biochem. Biophys 1990; 277: 56–60
  • Reinhart J., Pearson W. R. The structure of two murine class-mu glutathione transferase genes coordinately induced by butylated hydroxyanisole. Arch. Biochem. Biophys 1993; 303: 383–393
  • Pearson W. R., Vorachek W. R., Xu S.-j., Berger R., Hart I., Vannis D., Patterson D. Identification of class-mu glutathione transferase genes GSTM1-GSTMSon human chromosome 1p13. Am. J. Hum. Genet 1993; 53: 220–233
  • Comstock K. E, Johnson K. J, Rifenbery D., Henner W. D. Isolation and analysis of the gene and cDNA for a human mu class glutathioneS-transfease, GSTM4. J. Biol. Chem 1993; 268: 16958–16965
  • Fan W., Trifiletti R., Cooper T., Norris J. S. Cloning of a μ-class glutathioneS-transferase gene and identification of the glucocorticoid regulatory domains in its 5′ flanking sequence. Proc. Natl. Acad. Sci. U.S.A 1992; 89: 6104–6108
  • Okuda A., Sakai M., Muramatsu M. The structure of the rat glutathioneS-transferase P gene and related pseudogenes. J. Biol. Chem 1987; 262: 3858–3863
  • Bammler T. K., Smith C. A. D., Wolf C. R. Isolation and characterization of two mouse Pi-class glutathioneS-transferase genes. Biochem. J 1994; 298: 385–390
  • Xu X., Stambrook P. J. Two mu-rine GSTpi genes are arranged in tandem and are differentially expressed. J. Biol. Chem 1994; 269: 30268–30273
  • Cowell I. G., Dixon K. H., Pemble S. E., Ketterer B., Taylor J. B. The structure of the human glutathioneS-transferase gene. Biochem. J 1988; 255: 79–83
  • Morrow C. S., Cowan K. H., Goldsmith M. E. Structure of the human genomic glutathioneS-transferase-n gene. Gene 1989; 75: 3–11
  • Ogura K., Nishiyama T., Hiratsuka A., Watabe T., Watabe T. Isolation and characterization of the gene encoding rat class theta glutathioneS-transferase subunit Yrs. Biochem. Biophys. Res. Commun 1994; 205: 1250–1256
  • Board P. G., Webb G. C. Isolation of a cDNA clone and localization of human glutathioneS-transferase 2 genes to chromosome band 6p12. Proc. Natl. Acad. Sci. U.S.A 1987; 84: 2377–2381
  • Ross V. L., Board P. G., Webb G. C. Chromosomal mapping of the human mu class glutathioneS-transferases to 1p13. Genomics 1993; 18: 87–91
  • Board P. G., Webb G. C., Coggan M. C. Isolation of a cDNA clone and localization of the human glutathioneS-transferase 3 genes to chromosome bands 11 q 13 and 12q 13–14. Ann. Hum. Genet 1989; 53: 205–213
  • Board P. G., Coggan M., Woodcock D. M. The human pi class glutathione transferase sequence at 12q 13–q14 is a reverse-transcribed pseudogene. Genomics 1992; 14: 470–473
  • Tan K. L., Webb G. C., Baker R. T., Board P. G. Molecular cloning of a cDNA and chromosomal localization of a human theta-class glutathioneS-transferase gene (GSTT2) to chromosome 22. Genomics 1995; 25: 381–387
  • Ali-Osman F., Akande O. Isolation and characterization of cDNAs encoding messenger RNAs of variant human glutathioneS-transferase-pi genes in normal cells and gliomas. Biochim. Biophys. Acta, personal communication
  • Pemble S. E., Taylor J. B. An evolutionary perspective on glutathione transferases inferred from class-Theta glutathione transferase cDNA sequences. Biochem. J. 1992; 287: 957–963
  • Wilce M. C. J., Parker M. W. Structure and function of glutathioneS-transferases. Biochim. Biophys. Acta 1994; 1205: 1–18
  • Ji X. H., von Rosenvinge E. C., Johnson W. W., Tomarev S. I., Piatigorsky J., Armstrong R. N., Gilliland G. L. Three-dimensional structure, catalytic properties and evolution of a sigma class glutathione transferase from squid, a progenitor of the lensS-crystallins of cephalopods. Biochemistry 1995; 34: 5317–5328
  • Morgenstern R., DePierre J. W. Microsomal glutathione transferase. Purification in unactivated form and further characterization of the activation process, substrate specificity and amino acid composition. Eur. J. Biochem 1983; 134: 591–597
  • DeJong J. L., Morgenstern R., Jörnvall H., De Pierre J. W., Tu C.-P. D. Gene expression of rat and human microsomal glutathioneS-transferases. J. Biol. Chem 1988; 263: 8430–8436
  • Lam B. K., Penrose J. F., Freeman G. J., Austen K. F. Expression cloning of a cDNA for human leukotriene C, synthase, an integral membrane protein conjugating reduced glutathione to leukotriene A. Proc. Natl. Acad. Sci. U.S.A 1994; 91: 7663–7667
  • Welsch D. J., Creely D. P., Hauser S. D., Mathis K. J., Krivi G. G., Isakson P. C. Molecular cloning and expression of leukotriene-C, synthase. Proc. Natl. Acad. Sci. U.S.A 1994; 91: 9745–9749
  • DeJong J. L., Mohandas T., Tu C.-P. D. The gene for the microsomal glutathioneS-transferase is on human chromosome 12. Genomics 1990; 6: 379–382
  • Morgenstern R., Lundqvist G., Anderson G., Balk L., DePierre J. W. The tissue distribution of microsomal glutathione transferase among different or-ganelles, different organs, and different organisms. Biochem. Pharmacol 1984; 33: 3609–3614
  • Booth J., Boyland E., Sims P. An enzyme from rat liver catalyzing conjugates with glutathione. Biochem. J 1961; 79: 516–524
  • Combes B., Stakelum G. S. A liver enzyme that conjugates sulfobromophthalein with glutathione. J. Clin. Invest 1961; 40: 981–988
  • Hayes J. D. Rapid purification of glutathioneS-transferases by gradient affinity elution of the glutathione-agarose and theS-hexylglutathione-agarose chromatography matrices. Glutathione S-Transferases and Drug Resistance, J. D. Hayes, C. B. Pickett, T. J. Mantle. Taylor and Francis, London 1990; 17–33
  • Simons P. C., Vander Jagt D. L. Purification of glutathioneS-transferases from human liver by glutathione-affinity chromatography. Anal. Biochem 1977; 82: 334–341
  • Guthenberg C., Mannervik B. Purification of glutathioneS-transferases from rat lung by affinity chromatography, evidence for an enzyme form absent in rat liver. Biochem. Biophys. Res. Commun 1979; 86: 1304–1310
  • Hayes J. D. Purification and physical characterization of glutathioneS-transferase K. Differential use ofS-hexylglutathione and glutathione affinity matrices to isolate a novel glutathioneS-transferase from rat liver. Biochem. J 1986; 233: 789–798
  • McLellan L. I., Hayes J. D. Differential induction of class alpha glutathioneS-transferases in mouse liver by the anticarcinogenic antioxidant, butylated hydroxyanisole. Biochem. J 1989; 263: 393402
  • Hiratsuka A., Sebata N., Kawashima K., Okuda H., Ogura K., Watabe T., Satoh K., Hatayama I., Tsuchida S., Ishikawa T., Sato K. A new class of rat glutathioneS-transferase Yrs-Yrs inactivating reactive sulfate esters as metabolites of carcinogenic arylmethanols. J. Biol. Chem 1990; 265: 11973–11981
  • Main waring G. W., Nash J., Davidson M., Green T. Isolation of a mouse theta glutathioneS-transferase active with methylene chloride. Biochem. J, in press
  • Lopez M. F., Patton W. F., Sawlivich W. B., Erdjument-Bromage H., Barry P., Gmyrek K., Hines T., Tempst P., Skea W. M. A glutathioneS-transferase (GST) isoenzyme from broccoli with significant sequence homology to the mammalian theta-class of GSTs. Biochim. Biophys. Acta 1994; 1205: 29–38
  • Hayes J. D., Coulthwaite R. E., Stockman P. K., Hussey A. J., Mantle T. J., Wolf C. R. GlutathioneS-transferase subunits in the mouse and their catalytic activities towards reactive electrophiles. Arch. Toxicol. Suppl 1987; 10: 136–146
  • Hayes J. D. Selective elution of rodent glutathioneS-transferases and glyoxalase I from theS-hexylglutathione-Sepharose affinity matrix. Biochem. J 1988; 255: 913–922
  • Meyer D. J., Lalor E., Coles B., Kispert A., Ålin P., Mannervik B., Ketterer B. Single-step purification and h.p.1.c. analysis of glutathione transferase 8–8 in rat tissues. Biochem. J 1989; 260: 785–788
  • Toft E., Söderström M., Ahlberg M. B., DePierre J. W. A novel 34 kDa glutathione-binding protein in mature rat ovary. Biochem. Biophys. Res. Commun 1994; 201: 149–154
  • Aronsson A.-C., Mannervik B. Characterization of glyoxalase I purified from pig erythrocytes by affinity chromatography. Biochem. J. 1977; 165: 503–509
  • Takahashi Y., Hirata Y., Burstein Y., Listowsky I. 3,2-Enoyl-CoA isomerase is the protein that copurifies with human glutathioneS-transferases fromS-hexylglutathione affinity matrices. Biochem. J 1994; 304: 849–852
  • Hayes J. D., Mantle T. J. Anomalous electrophoretic behaviour of the glutathioneS-transferase Ya and Yk subunits isolated from man and rodents. Biochem. J 1986; 237: 731–740
  • Hales B. F., Jaeger V., Neims A. H. Isoelectric focusing of glutathioneS-transferases from rat liver and kidney. Biochem. J 1978; 175: 937–943
  • Aceto A., Di Ilio C., Angelucci S., Felaco M., Federici G. GlutathioneS-transferase isoenzymes from human testis. Biochem. Pharmacol 1989; 38: 3653–3660
  • Sherman M., Campbell J. A. H., Titmus S. A., Kew M. C., Kirsch R. E. GlutathioneS-transferase in hepato-cellular carcinoma. Hepatology 1983; 3: 170–176
  • Ostlund Farrants A.-K, Meyer D. J., Coles B., Southan C., Aitken A., Johnson P. J., Ketterer B. The separation of glutathione transferase subunits by using reverse-phase high-pressure liquid chromatography. Biochem. J 1987; 245: 423–428
  • Hsieh C.-H, Wang L.-Y, Tsai S.-P, Hsu H.-Y., Tam M. F. Mass spectrometric analysis of rat liver cytosolic glutathioneS-transferases. Modifications are limited to N-terminal processing. Biochem. J 1995; 308: 69–75
  • Hayes J. D., Mantle T. J. Use of immuno-blot techniques to discriminate between the glutathioneS-transferase Yf, Yk, Ya, Yn/Yb and Yc subunits and to study their distribution in extra-hepatic tissues. Evidence for three immunochemically distinct groups of transferases in the rat. Biochem. J 1986; 233: 779–788
  • Hayes J. D., Gilligan D., Chapman B. J., Beckett G. J. Purification of human hepatic glutathioneS-transferases and the development of a radioimmunoassay for their measurement in plasma. Clin. Chim. Acta 1983; 134: 107–121
  • McCusker F. M. G., Boyce S. J., Mantle T. J. The development of glutathioneS-transferase subunits in rat liver. Sensitive detection of the major subunit forms of rat glutathioneS-transferase by using an e.1.i.s.a. method. Biochem. J 1989; 262: 463–467
  • Peters W. H. M., Kock L., Nagengast F. M., Roelofs H. M. J. Immuno-detection with a monoclonal antibody of glutathione ‘S-transferase mu in patients with and without carcinomas. Biochem. Pharmacol 1990; 39: 591–597
  • Peters W. H. M., Boon C. E. W., Roelofs H. M. J., Wobbes T., Nagengast F. M., Kremers P. G. Expression of drug-metabolising enzymes and P-170 glycoprotein in colorectal carcinoma and normal mucosa. Gastroenterology 1992; 103: 448–455
  • Beckett G. J., Hayes J. D. GlutathioneS-transferases: biomedical applications. Adv. Clin. Chem 1993; 30: 279–378
  • Johnson J. A., Finn K. A., Siegel F. L. Tissue distribution of enzymic methylation of glutathioneS-transferase and its effects on catalytic activity. Methylation of glutathioneS-transferase 11–11 inhibits conjugation activity towards 1-chloro-2, 4-dinitrobenzene. Biochem. J 1992; 282: 279–289
  • Kelley M. K., Engqvist-Goldstein Å, Montali J. A., Wheatley J. B., Schmidt D. E., Kauvar L. M. Variability of glutathioneS-transferase isoenzyme patterns in matched normal and cancer human breast tissue. Biochem. J 1994; 304: 843–848
  • Harris J. M., Meyer D. J., Coles B., Ketterer B. A novel glutathione transferase (13–13) isolated from the matrix of rat liver mitochondria having structural similarity to class Theta enzymes. Biochem.J 1991; 278: 137–141
  • Danielson U. H., Mannervik B. Kinetic independence of the subunits of cytosolic glutathione transferase from the rat. Biochem. J 1985; 231: 263–267
  • Tahir M. K., Mannervik B. Simple inhibition studies for distinction between homodimeric and heterodimeric isoenzymes of glutathione transferase. J. Biol. Chem 1986; 261: 1048–1051
  • Atkins W. M., Wang R. W., Bird A. W., Newton D. J., Lu A. Y. H. The catalytic mechanism of glutathioneS-transferase (GST). Spectroscopic determination of the pKaof Tyr-9 in rat αl-1 GST. J. Biol. Chem 1993; 268: 19188–19191
  • Wang R. W., Newton D. J., Johnson A. R., Pickett C. B., Lu A. Y. H. Site-directed mutagenesis of glutathioneS-transferase YaYa. Mapping the glutathione-binding site. J. Biol. Chem 1993; 268: 23981–23985
  • Widersten M., Kolm R. H., Björnestedt R., Mannervik B. Contribution of five amino acid residues in the glutathione binding site to the function of human glutathione transferase P1–1. Biochem. J 1992; 285: 377–381
  • Board P. G., Coggan M., Wilce M. C. J., Parker M. W. Evidence for an essential serine residue in the active site of the theta class glutathione transferases. Biochem. J 1995; 311: 247–250
  • Kolm R. H., Sroga G. E., Mannervik B. Participation of the phenolic hydroxyl group of Tyr-8 in the catalytic mechanism of human glutathione transferase P1–1. Biochem. J 1992; 285: 537–540
  • Board P. G., Mannervik B. The contribution of the C-terminal sequence to the catalytic activity of GST2, a human alpha-class glutathioneS-transferase. Biochem. J 1991; 275: 171–174
  • Bjömestedt R., Widersten M., Board P. G., Mannervik B. Design of two chimaeric human-rat class alpha glutathioneS-transferases for probing the contribution of C-terminal segments of protein structure to the catalytic properties. Biochem. J 1992; 282: 505–510
  • Widersten M., Björnestedt R., Mannervik B. Contribution of amino acid residue 208 in the hydrophobic binding site to the catalytic mechanism of human glutathione transferase A1–1. Biochemistry 1994; 33: 11717–11723
  • Hoesch R. M., Boyer T. D. Localization of a portion of the active site of two rat liver glutathioneS-transferases using a photo affinity label. J. Biol. Chem 1989; 264: 17712–17717
  • Lee H.-C, Toung Y., Tu Y., Tu C.-P. D. A molecular genetic approach for the identification of essential residues in human glutathioneS-transferase function in Escherichia coli. J. Biol. Chem 1995; 270: 99–109
  • Ricci G., Lo Bello M., Caccuri A. M., Pastore A., Nuccetelli M., Parker M. W., Federici G. Site-directed mutagenesis of human glutathione transferase P1–1. Mutation of cys-47 induces a positive cooperativity in glutathione transferase P1–1. J. Biol. Chem 1995; 270: 1243–1248
  • Mannervik B., Awasthi Y. C., Board P. G., Hayes J. D., Di Ilio C., Ketterer B., Listowsky I., Morgenstern R., Muramatsu M., Pearson W. R., Pickett C. B., Sato K., Widersten M., Wolf C. R. Nomenclature for human glutathione transferases. Biochem. J 1992; 282: 305–306
  • Bass N. M., Kirsch R. E., Tuff S. A., Marks I., Saunders S. J. Ligandin heterogeneity: evidence that two non-identical subunits are the monomers of two distinct proteins. Biochim. Biophys. Acta 1977; 492: 163–175
  • Jakoby W., cterer B., Mannervik B. Glutathione transferases: nomenclature. Biochem. Pharmacol 1984; 33: 2539–2540
  • Mannervik B., Jensson H. Binary combinations of four protein subunits with different catalytic specificities explain the relationship between six basic glutathioneS-transferases in rat cytosol. J. Biol. Chem 1982; 257: 9909–9912
  • Lai H., Li N., Weiss M. J., Reddy C. C., Tu C.-P. D. The nucleotide sequence of a rat liver glutathioneS-transferase subunit cDNA clone. J. Biol. Chem 1984; 259: 5536–5542
  • Hayes J. D., Kerr L. A., Harrison D. J., Cronshaw A. D., Ross A. G., Neal G. E. Preferential over-expression of the class alpha rat Ya2glutathioneS-transferase subunit in livers bearing aflatoxin-induced pre-neoplastic nodules. Biochem. J 1990; 268: 295–302
  • Pickett C. B., Telakowski-Hopkins C. A., Ding G., Argenbright L., Lu A. Y. H. Rat liver glutathioneS-transferases. Complete nucleotide sequence of a glutathioneS-transferase mRNA and the regulation of the Ya, Yb and Yc mRNAs by 3-methylcholanthrene and phenobarbital. J. Biol. Chem 1984; 259: 5182–5188
  • Yamada T., Muramatsu Y., Yasue M., Agui T., Yamada J., Matsumoto K. Chromosomal assignments of genes for rat glutathioneS-transferase Ya and Yc subunits. Cytogenet. Cell Genet 1992; 61: 125–127
  • Habig W. H., Pabst M. J., Jakoby W. B. GlutathioneS-transferase AA from rat liver. Arch. Biochem. Biophys 1976; 175: 710–716
  • Telakowski-Hopkins C. A., Rodkey J. A., Bennett C. D., Lu A. Y. H., Pickett C. B. Rat liver glutathioneS-transferases. Construction of a cDNA clone complementary to a Yc mRNA and prediction of the complete amino acid sequence of a Yc subunit. J. Biol. Chem 1985; 260: 5820–5825
  • Tu C.-P. D., Reddy C. C. On the multiplicity of rat liver glutathioneS-transferases. J. Biol. Chem 1985; 260: 9961–9964
  • Stenberg G., Ridderström M., Engström Å, Pemble S. E., Mannervik B. Cloning and heterologous expression of cDNA encoding class Alpha rat glutathione transferase 8–8, an enzyme with high catalytic activity towards genotoxic α,β-unsat-urated carbonyl compounds. Biochem. J 1992; 284: 313–319
  • Scott T. R., Kirsch R. E. The isolation of a fetal rat liver glutathioneS-transferase isoenzyme with high glutathione peroxidase activity. Biochim. Biophys. Acta 1987; 926: 264–269
  • Meyer D. J., Gilmore K. S., Coles B., Dalton K., Hulbert P. B., Ketterer B. Structural distinction of rat GSH transferase subunit 10. Biochem. J 1991; 274: 619
  • Igarashi T., Tsuchiya T., Shikata Y., Sagami F., Tagaya O., Horie T., Satoh T. Developmental aspects of a unique glutathioneS-transferase subunit Yx in the liver cytosol from rats with hereditary hyperbilirubinuria. Comparison with rat fetal transferase subunit Y fetus. Biochem. J 1992; 283: 307–311
  • Hayes J. D., Nguyen T., Judah D. J., Peterson D. G., Neal G. E. Cloning of cDNAs from fetal rat liver encoding glutathioneS-transferase Yc polypeptides. The Yc2subunit is expressed in adult rat liver resistant to the hepatocarcinogen aflatoxin B1. J. Biol. Chem 1994; 269: 20707–20717
  • Tsuchida S., Sato K. Rat spleen glutathione transferases. A new acidic form belonging to the alpha class. Biochem. J 1990; 266: 461–465
  • Ålin P., Jensson H., Cederlund E., Jornvall H., Mannervik B. Cytosolic glutathione transferases from rat liver. Primary structure of class Alpha glutathione transferase 8–8 and characterization of low-abundance class Mu glutathione transferases. Biochem. J 1989; 261: 531–539
  • Habig W. H., Pabst hl. J., Jakoby W. B. GlutathioneS-transferases. The first enzymatic step in mercapturic acid formation. J. Biol. Chem 1974; 249: 7130–7139
  • Askelöf P., Guthenberg C., Jakobson I., Mannervik B. Purification and characterization of two glutathioneS-aryl-transferase activities from rat liver. Biochem. J 1975; 147: 513–522
  • Ding G. J., Lu A. Y. H., Pickett C. B. Rat liver glutathioneS-transferases. Nucleotide sequence analysis of a Yb, cDNA clone and prediction of the complete amino acid sequence of the Yb, sub-unit. J. Biol. Chem 1985; 260: 13268–13271
  • Lai H., Grove G., Tu C.-P. D. Cloning and sequence analysis of a cDNA for a rat liver glutathioneS-transferase Yb subunit. Nucleic Acids Res 1986; 14: 6101–6114
  • Chang C., Saltzman A. G., Sorensen N. S., Hiipakka R. A., Liao S. Identification of glutathioneS-transferase Yb1mRNA as the androgen-repressed mRNA by cDNA cloning and sequence analysis. J. Bio. Chem 1987; 262: 11901–11903
  • Muramatsu Y., Yamada T., Agui T., Yamada J., Serikawa T., Matsumoto K. Chromosomal assignments of genes for rat glutathioneS-transferase Yb1 and Yb2 subunits. Cytogenet. Cell Genet 1993; 63: 141–143
  • Beale D., Meyer D. J., Taylor J. B., Ketterer B. Evidence that the Yb sub-units of hepatic glutathione transferases represent two different but related families of polypeptides. Eur. J. Biochem 1983; 137: 125–129
  • Hayes J. D. Rat liver glutathioneS-transferases. A study of the structure of the basic YbYb-containing enzymes. Biochem. J 1983; 213: 625–633
  • Lai H., Tu C. Rat glutathioneS-transferases supergene family. Characterization of an anionic Yb subunit cDNA clone. J. Biol. Chem 1986; 261: 13793–13799
  • Hayes J. D. Purification and characterization of glutathioneS-transferases P, S and N. Isolation from rat liver of Yb1Yn protein, the existence of which was predicted by subunit hybridization. in vitro. Biochem. J 1984; 224: 839–852
  • Reddanna P., Thyagaraju K., Reddy C. C., Tu C.-P. D. Expression of glutathioneS-transferases in rat brain. J. Biol. Chem 1986; 261: 7596–7599
  • Abramovitz M., Listowsky I. Selective expression of a unique glutathioneS-transferase Yb3gene in rat brain. J. Biol. Chem 1987; 262: 7770–7773
  • Ishikawa T., Tsuchida S., Satoh K., Sato K. The subunit structure of a major glutathioneS-transferase form, M., in rat testis. Evidence for a heterodimer consisting of subunits with different iso-electric points. Eur. J. Biochem 1988; 176: 551–557
  • Kispert A., Meyer D. J., Lalor E., Coles B., Ketterer B. Purification and characterization of a labile rat glutathione transferase of the mu class. Biochem. J 1989; 260: 789–793
  • Kitahara A., Satoh K., Nishimura K., Ishikawa T., Ruike K., Sato K., Tsuda H., Ito N. Changes in molecular forms of rat hepatic glutathioneS-transferase during chemical hepatocarcinogenesis. Cancer Res 1984; 44: 2698–2703
  • Meyer D. J., Beale D., Tan K. H., Coles B., Ketterer B. Glutathione transferases in primary rat hepatomas: the isolation of a form with GSH peroxidase activity. FEBS Lett 1985; 184: 139–143
  • Jensson H., Eriksson L. C., Mannervik B. Selective expression of glutathione transferase isoenzymes in chemically induced preneoplastic rat hepa-tocyte nodules. FEBS Letr 1985; 187: 115–120
  • Suguoka Y., Kano T., Okuda A., Sakai M., Kitagawa T., Muramatsu M. Cloning and nucleotide sequence of rat glutathioneS-transferase P cDNA. Nucleic Acids Res 1985; 13: 6049–6057
  • Fjellstedt T. A., Allen R. H., Duncan B. K., Jakoby W. B. Enzymatic conjugation of epoxides with glutathione. J. Biol. Chem 1973; 248: 3702–3707
  • Gillham B. The mechanism of the reaction between glutathione and 1-menaphthyl sulphate catalysed by a glutathioneS-transferase from rat liver. Biochem. J 1973; 135: 797–804
  • Ogura K., Nishiyama T., Okada T., Kajita J., Narihata H., Watabe T., Hiratsuka A., Watabe T. Molecular cloning and amino acid sequencing of rat liver class theta glutathioneS-transferase Yrs-Yrs inactivating reactive sulfate esters of carcinogenic arylmethanols. Biochem. Biophys. Res. Commun 1991; 181: 1294–1300
  • Hiratsuka A., Okada T., Nishiyama T., Fujikawa M., Ogura K., Okuda H., Watabe T., Watabe T. Novel theta class glutathioneS-transferases Yrs-Yrs' and Yrs'-Yrs' in rat liver cytosol: their potent activity towards 5-sulfoxymethyl-chrysene, a reactive metabolite of the carcinogen 5-hydroxymethylchrysene. Biochem. Biophys. Res. Commun 1994; 202: 278–284
  • Watabe T. Posttranslational modification of GSTT2 account for differences between Yrs and Yrs', oral communication. ISSX GST Workshop, Amsterdam 1995
  • Taylor J. B. Molecular cloning of rat subunit 13, oral communication. ISSX GST Workshop, Amsterdam 1995
  • Hayes J. D., Strange R. C., Percy-Robb I. W. Identification of two litho-cholic acid-binding proteins: separation of ligandin from glutathioneS-transferase B. Biochem. J 1979; 181: 699–708
  • Scully N. C., Mantle T. J. Tissue distribution and subunit structures of the multiple forms of glutathioneS-transferase in the rat. Biochem. J 1981; 193: 367–370
  • Hayes J. D., Clarkson G. H. D. Purification and characterization of three forms of glutathioneS-transferase A. A comparative study of the major YaYa, YbYb and YcYc-containing glutathione S-transferases. Biochem. J 1982; 207: 459–470
  • Satoh K., Kitahara A., Soma Y., Inaba Y., Hatayama I., Sato K. Purification, induction and distribution of placental glutathione transferase: a new marker enzyme for preneoplastic cells in rat chemical hepatocarcinogenesis. Proc. Natl. Acad. Sci. U.S.A 1985; 82: 3964–3968
  • Hayes J. D., Judah D., Mc Lellan L. I., Kerr L. A., Peacock S. D., Neal G. E. Ethoxyquin-induced resistance to aflatoxin B1in the rat is associated with the expression of a novel alpha class glutathioneS-transferase subunit, Yc2, which possesses high catalytic activity for aflatoxin B1--8, 9-epoxide. Biochem. J 1991; 279: 385–398
  • van Ommen B., Ploemen J. H. T., Bogaards J. J. P., Monks T. J., Gau S. S., van Bladeren P. J. Irreversible inhibition of rat glutathioneS-transferase 1–1 by quinones and their glutathione conjugates: structure-activity relationship and mechanism. Biochem. J 1991; 276: 661–666
  • Alin P., Jensson H., Guthenberg C., Danielson U. H., Tahir M. K., Mannervik B. Purification of major basic glutathione transferase isoenzymes from rat liver by use of affinity chromatography and fast protein liquid chromatofocusing. Analyt. Biochem 1985; 146: 313–320
  • Satoh K., Hatayama I., Tsuchida S., Sato K. Biochemical characteristics of a preneoplastic marker enzyme glutathioneS-transferase P-form (7–7). Arch. Biochem. Biophys 1991; 285: 312–316
  • Coles B., Ketterer B. The role of glutathione and glutathione transferases in chemical carcinogenesis. Crit. Rev. Biochem. Mol. Biol 1990; 25: 47–70
  • Anderson C. Microsomal Glutathione Transferase: Species Characteristics, Catalysis and Topology. Ph.D. thesis, University of Stockholm. 1992
  • Mosialou E. Microsomal Glutathione Transferase and Oxidative Stress. Ph.D. thesis, university of Stockholm. 1993
  • Raney K. D., Meyer D. J., Ketterer B., Harris T. M., Guengerich F. P. Glutathione conjugation of aflatoxin B1exo-and endo-epoxidesby rat and human glutathioneS-transferases. Chem. Res. Toxicol 1992; 5: 470478
  • Robertson I. G. C., Jensson H., Mannervik B., Urn B. Glutathione transferases in rat lung: the presence of transferase 7–7, highly efficient in the conjugation of glutathione with the carcinogenic (+)-7β, 8α-dihydroxy-9a, 10α-oxy-7, 8, 9, 10-tetrahydrobenzo[a]pyrene. Carcinogenesis 1986; 7: 295–299
  • Johnson W. W., Liu S., Ji X., Gilliland G. L., Armstrong R. N. Tyrosine 115 participates both in chemical and physical steps of the catalytic mechanism of a glutathioneS-transferase. J. Biol. Chem 1993; 268: 11508–11511
  • Ji X., Johnson W. W., Sesay M. A., Dickert L., Prasad S. M., Ammon H. L., Armstrong R. N., Gilliland G. L. Structure and function of the xenobiotic substrate binding site of a glutathioneS-transferase as revealed by X-ray crystallo-graphic analysis of product complexes with the diastereomers of 9-(S-glutathionyl)-10-hydroxy-9, 10-dihydrophenanthrene. Biochemistry 1994; 33: 1043–1052
  • Shan S.-o., Armstrong R. N. Rational reconstruction of the active site of a class mu glutathioneS-transferase. J. Biol. Chem 1994; 269: 32373–32379
  • Hiratsuka A., Yokoi A., Sebata N., Watabe T., Satoh K., Hatayama I., Sato K. Glutathione conjugation of the fluorophotometric epoxide substrate, 7-glycidoxycoumarin (GOC), by rat liver glutathione transferase isoenzymes. Biochem. Pharmacol 1989; 38: 2609–2613
  • Dirr H. W., Mann K., Huber R., Ladenstein R., Reinerner P. Class pi glutathioneS-transferase from pig lung. Purification, biochemical characterization, primary structure and crystallization. Eur. J. Biochem 1991; 196: 693–698
  • Taniguchi H., Pyerin W. GlutathioneS-transferase is an in vitrosubstrate of Ca++-phospholipid-dependent protein kinase (protein kinase C). Biochem. Biophys. Res. Commun 1989; 162: 903–907
  • Nicholson D. W. Leukotriene C4synthase. Structure and Function of Glutathione Transferases, K. D. Tew, C. B. Pickett, T. J. Mantle, B. Mannervik, J. D. Hayes. CRC Press, Boca Raton, FL 1993; 47–62
  • Kuzmich S., Vanderveer L. A., Tew K. D. Evidence for a glycoconjugate form of glutathioneS-transferase pi. Int. J. Peptide Protein Res 1991; 37: 565–571
  • Murata T., Hatayarna I., Satoh K., Tsuchida S., Sato K. Activation of rat glutathione transferases in class mu by active oxygen species. Biochem. Biophys. Res. Commun 1990; 171: 845–851
  • Aniya Y., Naito A. Oxidative stress-induced activation of microsomal glutathioneS-transferase in isolated rat liver. Biochem. Pharmacol 1993; 45: 3742
  • Morgenstern R., DePierre J. W., Ernster L. Activation of microsomal glutathione transferase activity by sulfhydryl reagents. Biochem. Biophys. Res. Commun 1979; 87: 657–663
  • Morgenstern R., Lundqvist G., Jörnvall H., DePierre J. W. Activation of rat liver microsomal glutathione transferase by limited proteolysis. Biochem. J 1989; 260: 577–582
  • Miles J. S., Moss J. E., Taylor B. A., Burchell B., Wolf C. R. Mapping genes encoding drug-metabolising enzymes in recombinant inbred mice. Genomics 1991; 11: 309–316
  • McLellan L. I., Kerr L. A., Cronshaw A. D., Hayes J. D. Regulation of mouse glutathioneS-transferases by chemoprotectors. Molecular evidence for the existence of three distinct alpha-class glutathioneS-transferase subunits, Ya1, Ya2and Ya3, in mouse liver. Biochem. J 1991; 276: 461469
  • Pearson W. R., Reinhart J., Sisk S. C., Anderson K. S., Adler P. N. Tissue-specific induction of murine glutathione transferase mRNAs by butylated hydroxyanisole. J. Biol. Chem 1988; 263: 13324–13332
  • Hayes J. D., Judah D. J., Neal G. E., Nguyen T. Molecular cloning and heterologous expression of a cDNA encoding a mouse glutathioneS-transferase Yc subunit possessing high catalytic activity for aflatoxin B1-8, 9+poxide. Biochem. J 1992; 285: 173–180
  • Buetler T. M., Eaton D. L. Complementary DNA cloning, messenger RNA expression, and induction of α-class glutathioneS-transferases in mouse tissues. Cancer Res 1992; 52: 314–318
  • Zimniak P., Eckles M. A., Saxena M., Awasthi Y. C. A subgroup of class α glutathioneS-transferases. Cloning of a cDNA for mouse lung glutathioneS-transferase GST 5.7. FEBS Lett 1992; 313: 173–176
  • McLellan L. I., Harrison D. J., Hayes J. D. Modulation of glutathioneS-transferases and glutathione peroxidase by the anticarcinogen butylated hydroxya-nisole in murine extrahepatic organs. Carcinogenesis 1992; 13: 2255–2261
  • Pearson W. R., Windle J. J., Morrow J. F., Benson A. M., Talalay P. Increased synthesis of glutathioneS-transferases in response to anticarcinogenic antioxidants. Cloning and measurement of messenger RNA. J. Biol. Chem 1983; 258: 2052–2062
  • Townsend A. J., Goldsmith M. E., Pickett C. B., Cowan K. H. Isolation, characterization, and expression in Escherichia coliof two murine mu class glutathioneS-transferase cDNAs homologous to the rat subunits 3 (Yb1) and 4 (Yb2). J. Biol. Chem 1989; 264: 21582–21590
  • Hayes J. D., Kerr L. A., Peacock S. D., Cronshaw A. D., McLellan L. I. Hepatic glutathioneS-transferases in mice fed on a diet containing the anticarcinogenic antioxidant butylated hydroxyanisole. Isolation of mouse glutathioneS-transferase heterodimers by gradient elution of the glutathione-Sephareose affinity matrix. Biochem. J 1991; 277: 501–512
  • Lee C. Y. G. Biochemical and immuno-logical analysis of an abundant form of glutathioneS-transferase in mouse testis. Mol. Cell. Biochem 1982; 49: 161–168
  • Hatayama I., Satoh K., Sato K. A cDNA sequence coding a class pi glutathioneS-transferase of mouse. Nucleic Acid Rex 1990; 18: 4606
  • Mainwaring G., Green T., Tugwood J. Molecular cloning of two murine class theta GST, Poster A12. 14th European Workshop on Drug Metabolism, INSERM 1994
  • Hussey A. J. GlutathioneS-Transferases: Catalytic and Molecular Properties of mu-Class and theta-Class Isoenzymes. Ph.D. thesis, University of Edinburgh. 1992
  • Anderson C., Söderström M., Mannervik B. Activation and inhibition of microsomal glutathione transferase from mouse liver. Biochem. J 1988; 249: 819–823
  • Benson A. M., Batzinger R. P., Ou S., Bueding E., Cha Y.-N., Talalay P. Elevation of hepatic glutathioneS-transferase activities and protection against mutagenic metabolites of benzo[a]pyrene by dietary antioxidants. Cancer Res 1978; 38: 4486–4495
  • Lee C.-Y, Johnson L., Cox R. H., McKinney J. D., Lee S.-M. Mouse liver glutathioneS-transferases. Biochemical and immunological characterization. J. Biol. Chem 1981; 256: 8110–8116
  • Benson A. M., Hunkeler M. J., York J. L. Mouse hepatic glutathione transferase isoenzymes and their differential induction by anticarcinogens. Specificities of butylated hydroxyanisole and bisethylxanthogen as inducers of giutathione transferases in male and female CD-1 mice. Biochem. J 1989; 261: 1023–1029
  • McLellan L. I., Hayes J. D. Sex-specific constitutive expression of the pre-neoplastic marker glutathioneS-transferase, YfYf, in mouse liver. Biochem. J 1987; 245: 399–406
  • Warholm M., Jensson H., Tahir M. K., Mannervik B. Purification and characterization of three distinct glutathione transferases from mouse liver. Biochemistry 1986; 25: 4119–4125
  • Singhal S. S., Saxena M., Ahmad H., Awasthi Y. C. GlutathioneS-transferases of mouse liver: sex-related differences in the expression of various isozymes. Biochim. Biophys. Acta 1992; 1116: 137–146
  • Adarns D. J., Balkwill F. R., Griffin D. B., Hayes J. D., Lewis A. D., Wolf C. R. Induction and suppression of glutathioneS-transferases by interferon in the mouse. J. Biol. Chem 1987; 262: 4888–4892
  • Medh R. D., Saxena M., Singhal S. S., Ahmad H., Awasthi Y. C. Characterization of a novel glutathioneS-trans-ferase isoenzyme from mouse lung and liver having structural similarity to rat glutathioneS-transferase 8–8. Biochem. J 1991; 278: 793–799
  • Bammler T. K., Driessen H., Finnstrom N., Wolf C. R. Amino acid differences at positions 10, 11 and 104 explain the profound catalytic differences between two murine pi-class glutathioneS-transferases. Biochemistry 1995; 34: 9000–9008
  • Zimniak P., Singhal S. S., Srivastava S. K., Awasthi S., Sharma R., Hayden J. B., Awasthi Y. C. Estimation of genomic complexity, heterologous expression, and enzymatic characterization of mouse glutathioneS-transferase mGSTA4–4 (GST 5.7). J. Biol. Chem 1994; 269: 992–1000
  • Kamisaka K., Habig W. H., Ketley J. N., Arias I. M., Jakoby W. B. Multiple forms of human glutathioneS-transferase and their affinity for biliru-bin. Eur. J. Biochem 1975; 60: 153–161
  • Stockman P. K., Beckett G. J., Hayes J. D. Identification of a basic hybrid glutathioneS-transferase from human liver. GlutathioneS-transferase 6 is composed of two distinct subunits (B, and B?). Biochem. J 1985; 227: 457465
  • Soma Y., Satoh K., Sato K. Purification and subunit-structural and immunological characterization of five glutathioneS-transferases in human liver, and the acidic form as a hepatic tumor marker. Biochim. Biophys. Acta 1986; 869: 247–258
  • Tu C.-P. D., Qian B. Human liver glutathioneS-transferases: complete primary sequence of an H, subunit cDNA. Biochem. Biophys. Res. Commun 1986; 141: 229–237
  • Hayes J. D., Kerr L. A., Cronshaw A. D. Evidence that glutathioneS-transferases B1B1and B2B2are the products of separate genes and that their expression in human liver is subject to inter-individual variation. Molecular relationships between the B1and B2subunits and other alpha class glutathioneS-transferases. Biochem. J 1989; 264: 437–445
  • Rhoads D. M., Zarlengo R. P., Tu C.-P. D. The basic glutathioneS-transferases from human livers are products of separate genes. Biochem. Biophys. Res. Commun 1987; 145: 474–481
  • Singhal S. S., Zimniak P., Sharma R., Srivastava S. K., Awasthi S., Awasthi Y. C. A novel glutathioneS-transferase isoenzyme similar to GST 8–8 of rat and mGSTA4–4 (GST 5.7) of mouse is selectively expressed in human tissues. Biochim. Biophys. Acta 1994; 1204: 279–286
  • Singhal S. S., Zimniak P., Awasthi S., Piper J. T., He N., Teng J. I., Petersen D. R., Awasthi Y. C. Several closely related glutathioneS-transferase isoenzymes catalysing conjugation of 4-hydroxynonenal are differentially expressed in human tissues. Arch. Biochem;. Biophys 1994; 311: 242–250
  • Del Boccio G., Iio C., Rlin P., Jörnvall H., Mannervik B. Identification of a novel glutathione transferase in human skin homologous with class alpha glutathione transferase 2–2 in the rat. Biochem. J 1987; 244: 21–25
  • Singhal S. S., Gupta S., Ahmad H., Sharma R., Awasthi Y. C. Characterization of a novel α-class anionic glutathioneS-transferase isoenzyme from human liver. Arch. Biochem. Biophys 1990; 279: 45–53
  • Ahmad H., Singhal S. S., Saxena M., Awasthi Y. C. Characterization of two novel subunits of the α-class glutathioneS-transferases of human liver. Biochim. Biophys. Acta 1993; 1161: 333–336
  • Board P. G. Biochemical genetics of glutathioneS-transferase in man. Am. J. Hum. Genet 1981; 33: 36–43
  • Warholm M., Guthenberg C., Mannervik B. Molecular and catalytic properties of glutathione transferase y from human liver: an enzyme efficiently conjugating epoxides. Biochemistry 1983; 22: 3610–3617
  • Strange R. C., Faulder C. G., Davis B. A., Hume R., Brown J. A. H., Cotton W., Hopkinson D. A. The human glutathioneS-transferases: studies on the tissue distribution and genetic variation of the GST1, GST2 and GST3 isoenzymes. Ann. Hum. Genet 1984; 48: 11–20
  • Tsuchida S., Maki T., Sato K. Purification and characterization of glutathione transferases with an activity towards nitroglycerin from human aorta and hem: multiplicity of the human mu forms. J. Biol. Chem 1990; 265: 7150–7157
  • Seidegård J., Vorachek W. R., Pero R. W., Pearson W. R. Hereditary differences in the expression of the human glutathione transferase active on trans-stil-bene oxide are due to a gene deletion. Proc. Natl. Acad. Sci. U.S.A 1988; 85: 7293–7297
  • Hayes J. D. Purification and characterization of a polymorphic Yb-containing glutathioneS-transferase, GST PS, from human liver. Clin. Chem. Enzyme Commun 1989; 1: 245–264
  • Van Ommen B., Bogaards J. J. P., Peters w H. M., Blaauboer B., van Bladeren P. J. Quantification of human hepatic glutathioneS-transferases. Biochem. J 1990; 269: 609–613
  • Widersten M., Pearson W. R., Engström Å., Mannervik B. Het-erologous expression of the allelic variant Mu-class glutathione transferases μand ψ. Biochem. J 1991; 276: 519–524
  • Hussey A. J., Hayes J. D. Human mu-class glutathioneS-transferases present in liver, skeletal muscle and testicular tissue. Biochim. Biophys. Acta 1993; 1203: 131–141
  • Awasthi Y. C., Dao D. D., Saneto R. P. Interrelationship between anionic and cationic forms of glutathioneS-transferases of human liver. Biochem. J 1980; 191: 1–10
  • DeJong J. L., Chang C., Whang-Peng J., Knutsen T., Tu C.-P. D. The human liver glutathioneS-transferase gene super family: expression and chromosome mappimg of an Hb subunit cDNA. Nucleic Acids Res 1988; 16: 8541–8554
  • Hussey A. J., Kerr L. A., Cronshaw A. D., Harrison D. J., Hayes J. D. Variation in the expression of mu-class glutathioneS-transferase isoenzymes from human skeletal muscle. Evidence for the existence of heterodimers. Biochem. J 1991; 273: 323–332
  • Vorachek W. R., Pearson W. R., Rule G. S. Cloning, expression, and characterization of a class-mu glutathione transferase from human skeletal muscle, the product of the GST4locus. Proc. Natl. Acad. Sci. U.S.A 1991; 88: 444347
  • Suzuki T., Coggan M., Shaw D. C., Board P. G. Electrophoretic and immunological analysis of human glutathioneS-transferase isoenzymes. Ann. Hum. Genet 1987; 51: 95–106
  • Singhal S. S., Ahmad H., Sharma R., Gupta S., Haque A. K., Awasthi Y. C. Purification and characterization of human muscle glutathioneS-transferases: evidence that glutathioneS-transferase corresponds to a locus distinct from GST1, GST2 andGST3. Arch. Biochem. Biophys 1991; 285: 64–73
  • Campbell E., Takahashi Y., Abramovitz M., Peretz M., Listowsky I. A distinct human testis and brain p-class glutathioneS-transferase. Molecular cloning and characterization of a form present even in individuals lacking hepatic type μ isoenzymes. J. Biol. Chem 1990; 265: 9188–9193
  • Ross V. L., Board P. G. Molecular cloning and heterologous expression of an alternatively spliced human mu class glutathioneS-transferase transcript. Biochem. J 1993; 294: 373–380
  • Takahashi Y., Campbell E. A., Hirata Y., Takayama T., Listowsky I. A basis for differentiating among the multiple human Mu-glutathioneS-transferases and molecular cloning of brain GSTM5. J. Biol. Chem 1993; 268: 8893–8898
  • Marcus C. J., Habig W. H., Jakoby W. B. Glutathione transferase from human erythrocytes. Nonidentity with the enzymes from liver. Arch. Biochem. Biophys 1978; 188: 287–293
  • Guthenberg C., Mannervik B. GlutathioneS-transferase (transferase) from human placenta is identical or closely related to glutathioneS-transferase (transferase ρ) from erythrocytes. Biochim. Biophys. Acta 1981; 661: 255–260
  • Tateoka N., Tsuchida S., Soma Y., Sato K. Purification and characterization of glutathioneS-transferases in human kidney. Clin. Chim. Acta 1987; 166: 207–218
  • Kano T., Sakai M., Muramatsu M. Structure and expression of a human class glutathioneS-transferase messenger RNA. Cancer Res 1987; 47: 5626–5630
  • Webb G. C., Board P. G. Mapping of human. GSTTI, unpublished communication.
  • Hussey A. J., Hayes J. D. Characterization of a human class theta glutathioneS-transferase with activity towards 1-men-aphthyl sulphate. Biochem. J 1992; 286: 929–935
  • McLellan L. I., Wolf C. R., Hayes J. D. Human microsomal glutathioneS-transferase: its involvement in the conjugation of hexachloro-1, 3-butadiene with glutathione. Biochem. J 1989; 285: 87–93
  • Mosialou E., Andersson C., Lundqvist G., Andersson G., Bergman T., Joörnvall H., Morgenstern R. Human liver microsomal glutathione transferase. Substrate specificity and important protein sites. FEBS Lett 1993; 315: 77–80
  • Stockman P. K., Hayes J. D. Identification of a Yb-containing glutathioneS-transferase (GST ϕ) in human liver with an acidic PI. Glutathione S-Transferases and Carcinogenesis, T. J. Mantle, C. B. Pickett, J. D. Hayes. Francis and Taylor, London 1987; 4142
  • Harada S., Abei M., Tanaka N., Agarwal D. P., Goedde H. W. Liver glutathioneS-transferase polymorphism in Japanese and its pharmacogenetic importance. Hum. Genet 1987; 75: 322–325
  • Davies M. H., Elias E., Acharya S., Cotton W., Faulder G. C., Fryer A. A., Strange R. C. GSTM1 null polymorphism at the glutathioneS-transferase M1 locus: phenotype and genotype studies in patients with primary biliary cirrhosis. Gut 1993; 34: 549–553
  • Stockman P. K., McLellan L., Hayes J. D. Characterization of the basic glutathioneS-transferase B1and B2sub-units from human liver. Biochem. J 1987; 244: 55–61
  • Koskelo K. Isoelectric focusing of glutathioneS-transferases: comparison of the acidic transferases from human liver, kidney, lung, spleen, and placenta. Scand. J. Clin. Lab. Invest 1983; 43: 133–139
  • Weinander R., Anderson C., Morgenstern R. Identification of N-acetylcysteine as a new substrate for rat liver microsomal glutathione transferase. J. Biol. Chem 1994; 269: 71–76
  • Andersson C., Morgenstern R. Chemical modification of rat liver microsomal glutathione transferase defines residues of importance for catalytic function. Biochem. J 1990; 272: 479–484
  • Metters K. M., Sawyer N., Nicholson D. W. Microsomal glutathioneS-transferase is the predominant leukotriene C4binding site in cellular membranes. J. Biol. Chem 1994; 269: 12816–12823
  • Andersson C., Weinander R., Lundqvist G., De Pierre J. W., Morgenstern R. Functional and structural membrane topology of rat liver microsomal glutathione transferase. Biochim. Biophys. Acta 1994; 1204: 298–304
  • Lin D., Meyer D. J., Ketterer B., Lang N. P., Kadlubar F. F. Effects of human and rat glutathioneS-transferases on the covalent DNA binding of the N-acetoxy derivatives of heterocyclic amine carcinogens in vitro: a possible mechanism of organ specificity in their carcinogenesis. Cancer Res 1994; 54: 49204926
  • Buetler T. M., Slone D., Eaton D. L. Comparison of the aflatoxin B, -8, 9-epoxide conjugating activities of two bacterially expressed alpha class glutathioneS-transferase isoenzymes from mouse and rat. Biochem. Biophys. Res. Commun 1992; 188: 597–603
  • Gopalan-Kriczky P., Jensen D. E., Lotlikar P. D. Conjugation of microsome generated and synthetic aflatoxin B1--8, 9-epoxide and styrene oxide to glutathione by purified glutathioneS-transferases from hamster and mouse livers. Cancer Lett 1994; 86: 83–90
  • Nemoto N., Gelboin H. V., Habig W. H., Jakoby W. B. K-region benzo[a]pyrene-4, 5-oxide is conjugated by homogeneous glutathioneS-transferases. Nature 1975; 255: 512
  • Robertson I. G. C., Guthenberg C., Mannervik B., Jernström B. Differences in stereo selectivity and catalytic efficiency of three human glutathione transferases in the conjugation of glutathione with 7β, 8α-dihydroxy-9α, 10α-oxy-7, 8, 9, 10-tetrahydrobenzo[a]pyrene. Cancer Res 1986; 46: 2220–2224
  • Robertson I. G. C., Jernström B. The enzymatic conjugation of glutathione with bay-region diol-epoxides of benzo [a]pyrene, benz[a]anthracene and chrysene. Carcinogenesis 1986; 7: 1633–1636
  • Glatt H., Friedberg T., Grover P. L., Sims P., Oesch F. Inactivation of a diol-epoxide and a K-region epoxide with high efficiency by glutathioneS-transferase X. Cancer Res 1983; 43: 5713–5717
  • Csanády G. A., Guengerich F. P., Bond J. A. Comparison of the biotrans-formation of 1.3-butadiene and its metabolite, butadiene monoepoxide, by hepatic and pulmonary tissues from humans, rats and mice. Carcinogenesis 1992; 13: 1143–1153
  • Jensen D. E., Stelman G. J. Evidence for cytosolic glutathione transferase mediated denitrosation of nitrosocimetidine and 1-methyl-2-nitro-1-nitrosoguanidine. Carcinogenesis 1987; 8: 1791–1800
  • Djurić Z., Coles B., Fifer E. K., Ketterer B., Beland F. A. In vivoand in vitroformation of glutathione conjugates from the K-region epoxides of 1-nitropyrene. Carcinogenesis 1987; 8: 1781–1786
  • Stanley J. S., Benson A. M. The conjugation of 4-nitroquinoline 1-oxide, a potent carcinogen, by mammalian glutathione transferases. 4-nitroquinoline 1-oxide conjugation by human, rat and mouse liver cytosols, extrahepatic organs of mice and purified mouse glutathione transferase isoenzymes. Biochem. J 1988; 256: 303–306
  • Aceto A., Di Ilio C., Lo Bello M., Bucciarelli T, Angelucci S., Federici G. Differential activity of human, rat, mouse and bacterial glutathione transferase isoenzymes towards 4-nitroquinoline 1-oxide. Carcinogenesis 1990; 11: 2267–2269
  • Singh S. V., Srivastava S. K., Awasthi Y. C. Binding of benzo[a]pyrene to rat lung glutathioneS-transferases in vivo. FEBS Lett 1985; 179: 111–114
  • Singh S. V., Creadon G., Das M., Mukhtar H., Awasthi Y. C. GlutathioneS-transferases of mouse lung. Selective binding of benzo[a]pyrene metabolites by the subunits which are preferentially induced by t-butylated hydroxyanisole. Biochem. J 1987; 243: 351–358
  • Ohmi N., Bhargava M., Arias I. M. Binding of 3′-methyl-N, N-dimethyl-4aminoazobenzene metabolites to rat liver cytosol proteins and ligandin subunits. Cancer Res 1981; 41: 3461–3464
  • Sarrif A. M., McCarthy K. L., Nesnow S., Heidelberger C. Separation of glutathioneS-transferase activities with epoxides from the mouse liver h-protein, a major polycyclic hydrocarbon-binding protein. Cancer Res 1978; 38: 1438–1443
  • Vale Aro D., Pe Arin F., Zajdela F. Binding of 5, g-dimethyl dibenzo[c, g] carbazole, a potent hepatocarcinogen, to mouse hepatic cytosolic proteins. Carcino-genesis 1983; 4: 1333–1340
  • Sarrif A. M., Bertram J. S., Kamarck M., Heidelberger C. The isolation and characterization of polycyclic hydrocarbon-binding proteins from mouse liver and skin cytosols. Cancer Res 1975; 35: 816–824
  • Jablonkai I., Hatzios K. K. Role of glutathione and glutathioneS-transferase in the selectivity of acetochlor in maize and wheat. Pest. Biochem. Physiol 1991; 41: 221–231
  • Frear D. S., Swanson H. R., Mansager E. R. Acifluorfen metabolism in soybean: diphenylether bond cleavage and the formation of homoglutathione, cys-teine, and glucose conjugates. Pest. Biochem. Physiol 1983; 20: 299–310
  • Moore R. E., Davies M. S., O'Connell K. M., Harding E. I., Wiegand R. C., Tiemeier D. C. Cloning and expression of a cDNA encoding a maize glutathioneS-transferase in. E. coli. Nucleic Acids Res 1986; 14: 7227–7235
  • Bull D. L., Whitten C. J. Factors influencing organophosphorus insecticide resistance in tobacco budworms. J. Agric. Food Chem 1972; 20: 561–564
  • Wosnick M. A., Barnett R. W., Carlson J. E. Total chemical synthesis and expression in Escherichia coliof a maize glutathioneS-transferase (GST) gene. Gene 1989; 76: 153–160
  • Gronwald J. W., Andersen R. N., Ye C. Atrazine resistance in velvetleaf (Abutilon theophrasti) biotype due to enhanced glutathioneS-transferase activity. Plant Physiol 1991; 96: 104–109
  • Egaas E., Falls J. G., Dauterman W. C. A study of gender, strain and age-differences in mouse liver glutathioneS-transferases. Comp. Biochem. Physiol. C 1995; 110: 35–40
  • Motoyama N., Rock G. C., Dauterman W. C. Studies on the mechanism of azinphosmethyl resistance in the predaceous mite, Neoseiuhis (T.) fallacis(family: Phytoseiidae). Pest. Biochem. Physiol 1971; 1: 205–215
  • Motoyama N., Dauterman W. C. In vitrometabolism of azinphosmethyl in susceptible and resistant houseflies. Pest. Biochem. Physiol 1972; 2: 113–122
  • Armstrong K. F., Suckling D. M. Correlation of azinphosmethyl resistance with detoxication enzyme activity in the light brown apple moth Epiphyas post-vittana(Lepidoptera: Tortricidae). Pest. Biochem. Physiol 1990; 36: 281–289
  • Dierickx P. J. Soluble glutathione transferase isoenzymes in Daphnia Magnastraus and their interaction with 2, 4-dichloro-phenoxyacetic acid and 1, 4-benzoquinone. Insect Biochem 1987; 17: 1–6
  • Brown H. M., Neighbors S. M. Soybean metabolism of chlorimuron ethyl: physiological basis for soybean selectivity. Pest. Biochem. Physiol 1987; 29: 112–120
  • Clark A. G., Shamaan N. A. Evidence that DDT-dehydrochlorinase from the housefly is a glutathioneS-transferase. Pest. Biochem. Physiol 1984; 22: 249–261
  • Tang A. H., Tu C.-P. D. Biochemical characterization of Drosophila glutathioneS-transferases D1 and D21. J. Biol. Chem 1994; 269: 27876–27884
  • Prapanthadara L. A., Hemingway J., Ketterman A. J. Partial purification and characterization of glutathioneS-transferases involved in DDT resistance from the mosquito Anopheles gambiae. Pest. Biochem. Physiol 1993; 47: 119
  • Lamoureux G. L., Davidson K. L. Mercapturic acid formation in the metabolism of propachlor, CDAA, and fluorodifen in the rat. Pest. Biochem. Physiol 1975; 5: 497–506
  • Clark A. G., Shamaan N. A., Sinclair M. D., Dauterman W. C. Insecticide metabolism by multiple glutathioneS-transferases in two strains of the housefly. Musca domestica(L). Pest. Biochem. Physiol 1986; 25: 169–175
  • Lamoureux G. L., Rusness D. G. Synergism of diazinon toxicity and inhibition of diazinon metabolism in the housefly by tridiphane : inhibition of glutathione S-transferase activity. Pest. Biochem. Physiol 1987; 27: 318–329
  • Griffiths M. H., Moss J. A., Rose J. A., Hathway D. E. The comparative metabolism of 2,6-dichlorothiobenzamide (Prefix) and 2,6-dichlorobenzonitrile in the dog and rat. Biochem. J 1966; 98: 770–781
  • Lamoureux G. L., Rusness D. G. The role of glutathione and glutathione S-transferases in pesticide metabolism, selectivity, and mode of action in plants and insects. Coenzymes and Cofactors 1989; 3B: 153–196
  • Lay M.-M., Casida J. E. Dichloro-acetamide antidotes enhance thiocarbamate sulfoxide detoxification by elevating corn root glutathione content and glutathione S-transferase activity. Pest. Biochem. Physiol 1976; 6: 442–456
  • Hubbell J. P., Casida J. E. Metabolic fate of the N,N-dialkylcarbamoyl moiety of thiocarbamate herbicides in rats and corn. J. Agric. Food Chem 1977; 25: 404–413
  • Motoyama N., Dauterman W. C. Purification and properties of housefly glutathione S-transferase. Insect. Biochem 1977; 7: 361–369
  • Tal A., Romano M. L., Stephenson G. R., Schwan A. L. Glutathione conjugation: a detoxification pathway for fenoxaprop-ethyl in barley, crabgrass, oat, and wheat. Pest. Biochem. Physiol 1993; 46: 190
  • Frear D. S., Swanson H. R. Metabolism of substistuted diphenylether herbicides in plants. 1. Enzymatic cleavage of Fluorodifen in Peas (Pisum sativumL.). Pest. Biochem. Physiol 1973; 3: 473–482
  • Kraus P. Biodegradation of alpha-hexachlorocyclohexane. VI. The dechlorination of α-hexachlorocyclohexane by microsomes of rat liver. Naunyn-Schmiedeberg's Arch. Pharmacol 1975; 291: 79–87
  • Tanaka K., Nakajima M., Kurihara N. The mechanism of resistance to lindane and hexadeuterated lindane in the Third Yumenoshima strain of housefly. Pest. Biochem. Physiol 1981; 16: 149–157
  • Niwa Y., Miyata T., Saito T. In vitrometabolism of malathion by malathion resistant and susceptible strains of house-flies, Musca domestica(L.). J. Pest. Sci 1977; 2: 151–157
  • Kao C.-H., Sun C.-N. In vitrodegradation of some organophosphorus insecticides by susceptible and resistant diamondback moth. Pest. Biochem. Physiol 1991; 41: 132–141
  • Ku C. C., Chiang F. M., Hsin C. Y., Yao Y. E. Glutathione transferase isoenzymes involved in insecticide resistance of diamondback moth larvae. Pest. Biochem. Physiol 1994; 50: 191
  • Zama P., Hatzios K. K. Effects of GCA-92194 on the chemical reactivity of Metolachlor with glutathione and metabolism of Metolachlor in grain sorghum (Sorghum bicolor). Weed Sci 1986; 34: 834–841
  • Goon D., Saxena M., Awasthi Y. C., Ross D. Activity of mouse liver glutathione S-transferases toward trans, trans-muconaldehyde and trans-4-hydroxy-2-nonenal. Toxicol. Appl. Pharmacol 1993; 119: 175–180
  • Yawetz A., Koren B. Purification and properties of the Mediterranian fruit fly. Ceratitis capitata(W.) glutathione S-transferase. Insect Biochem 1984; 14: 663–670
  • Hiratsuka A., Yokoi A., Iwata H., Watabe T., Satoh K., Hatayama I., Sato K. Glutathione conjugation of styrene 7,8-oxide enantiomers by major glutathione transferase isoenzymes isolated from rat livers. Biochem. Pharmacol 1989; 38: 4405–4413
  • Pacifici G. M., Warholm M., Guthenberg C., Mannervik B., Rane A. Detoxification of styrene oxide by human liver glutathione transferase. Human Toxicol 1987; 6: 483–489
  • Oppenoorth F. J., van der Pas L. J. T., Houx N. W. H. Glutathione S-transferase and hydrolytic activity in a tetra chlorvinphos-resistant strain of housefly and their influence on resistance. Pest. Biochem. Physiol 1979; 11: 176–188
  • Seidega Urd J., Guthenberg C., Pero R. W., Mannervik B. The trans-stil-bene oxide-active glutathione transferase in human mononuclear leucocytes is identical with the hepatic glutathione transferase μ. Biochem. J 1987; 246: 783–785
  • Lamoureux G. L., Rusness D. G. Tridiphane [2-(3,5dichlorophenyl)-2-(2,2,2-trichloroethyl)-oxirane], an atrazine synergist: enzymatic conversion to a potent glutathione S-transferase inhibitor. Pest. Biochem. Physiol 1986; 26: 323–342
  • Piccolomini R., Allocati N., Cellini L., Faraone A., Di Cola D., Sacchetta P., Ravagnan G. Preliminary studies on the effect of glutathione S-transferase from Providencia stuartiion the antimicrobial activity of different antibiotics. Chernio-terapia 1987; 6: 324–328
  • Arca P., Hardisson C., Suárez J. E. Purification of a glutathione S-transferase that mediates fosfomycin resistance in bacteria. Antimicrob. Agents Chemother 1990; 34: 844–848
  • Navas J., Lebn J., Arroyo M., Garcia-Lobo J. M. Nucleotide sequence and intracellular location of the product of the fosfomycin resistance gene from transposon Tn. 2921 Antimicrob. Agents Chemother 1990; 34: 2016–2018
  • Smith M. J., Evans C. G., Doane-Setzer P., Castro V. M., Tahir M. K., Mannervik B. Denitrosation of 1,3-Bis(2-chloroethyl)-1-nitrosourea by class mu glutathione transferases and its role in cellular resistance in rat brain tumor cells. Cancer Res 1989; 49: 2621–2625
  • Weber G. F., Waxman D. J. Denitrosation of the anti-cancer drug 1,3-Bis(2-chloroethyl)-1-nitrosourea catalysed by microsomal glutathione S-transferase and cytochrome P450 monooxygenases. Arch. Biochem. Biophys 1993; 307: 369–378
  • Berhane K., Hao X., Egyházi S., Hansson J., Ringborg U., Mannervik B. Contribution of glutathione 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
  • Ciaccio P. J., Tew K. D., LaCreta F. P. The spontaneous and glutathione S-transferase-mediated reaction of chlorambucil with glutathione. Cancer Commun 1990; 2: 279–286
  • Ciaccio P. J., Tew K. D., LaCreta P. P. Enzymatic conjugation of chlorambucil with glutathione by human glutathione S-transferases and inhibition by ethacrynic acid. Biochem. Pharmacol 1991; 42: 1504–1507
  • Dirven H. A. A., van Ommen B., van Bladeren P. J. Involvement of human glutathione S-transferase isoenzymes in the conjugation of cyclophosphamide metabolites with glutathione. Cancer Res 1994; 54: 6215–6220
  • Gulick A. M., Fahl W. E. Forced evolution of glutathione S-transferase to create a more efficient drug detoxication enzyme. Proc., Natl. Acad. Sci. U.S.A 1995; 92: 8140–8144
  • Dulik D. M., Fenselau C., Hilton J. Characterization of melphalan-glutathione adducts whose formation is catalysed by glutathione transferases. Biochem. Pharmacol 1986; 35: 3405–3409
  • Dulik D. M., Fenselau C. Conversion of melphalan to 4-(glutathionyl) phenylalanine. A novel mechanism for conjugation by glutathione S-transferases. Drug Met. Dispos 1987; 15: 195–199
  • Bolton M. G., Colvin O. M., Hilton J. Specificity of isozymes of murine hepatic glutathione S-transferase for the conjugation of glutathione with L-phenylala-nine mustard. Cancer Res 1991; 51: 2410–2415
  • Bolton M. G., Hilton J., Robertson K. D., Streeper R. T., Colvin O. M., Noe D. A. Kinetic analysis of the reaction of melphalan with water, phosphate and glutathione. Drug. Met. Dispos 1993; 21: 986–996
  • Wolf C. R., Macpherson J. S., Smyth J. F. Evidence for the metabolism of mitozantrone by microsomal glutathione transferases and 3-methylcholanthrene-in-ducible glucuronosyl transferases. Biochem. Pharmacol 1986; 35: 1577–1581
  • Tew K. D. Glutathione-associated enzymes in anticancer drug resistance. Cancer Res 1994; 54: 4313–4320
  • Dirven H. A. A., Dictus E. L. J., Broeders N. L. H., van Ommen B., van Bladeren P. J. The role of human glutathione S-transferase isoenzymes in the formation of glutathione conjugates of the aikylating cytostatic drug thiotepa. Cancer Res 1995; 55: 1701–1706
  • Meyer D. J., Ketterer B. 5α, 6α-Epoxy-cholestan-3β-ol (cholesterol α-ox-ide): a specific substrate for rat liver glutathione transferase B. FEBS Lett 1982; 150: 499–502
  • Mosialou E., Morgenstern R. Activity of rat liver microsomal glutathione transferase toward products of lipid peroxidation and studies of the effect of inhibitors on glutathione-dependent protection against lipid peroxidation. Arch. Biochem. Biophys 1989; 275: 289–294
  • Singhal S. S., Saxena M., Ahmad H, Awasthi S., Haque A. K., Awasthi Y. C. Glutathione S-transferases of human lung: characterization and evaluation of the protective role of the α-class isoenzymes against lipid peroxidation. Arch. Biochem. Biophys 1992; 299: 232–241
  • Spearman M. E., Prough R. A., Estabrook R. W., Falck J. R., Manna S., Leibman K. C., Murphy R. C., Capdevila J. Novel glutathione conjugates formed from epoxyeicosatrienoic acids (EETs). Arch. Biochem. Biophys 1985; 242: 225–230
  • Jensson H., Guthenberg C., Ålin P., Mannervik B. Rat glutathione transferase 8–8, an enzyme efficiently detoxifying 4-hydroxyalk-2-enals. FEBS Lett 1986; 203: 207–209
  • Hargus S. J., Fitzsimmons M. E., Aniya Y., Anders M. W. Stereochemistry of the microsomal glutathione S-transferase catalysed addition of glutathione to chlorotrifluoroethene. Biochemistry 1991; 30: 717–721
  • Wolf C. R., Berry P. N., Nash J. A., Green T., Lock E. A. Role of microsomal and cytosolic glutathione S-transferases in the conjugation of hexachloro-1,3-butadiene and its possible relevance to toxicity. J. Pharmacol. Exp. Ther 1984; 228: 202–208
  • Eaton D. L., Gallagher E. P. Mechanisms of aflatoxin carcinogenesis. Annu. Rev. Pharmacol. Toxicol 1994; 34: 135–172
  • Raney K. D., Coles B., Guengerich F. P., Harris T. M. The endo-8,9-epoxide of aflatoxin B1: a new metabolite. Chem. Res. Toxicol 1992; 5: 333–335
  • Iyer R. S., Coles B. F., Raney K. D., Thier R., Guengerich F. P., Harris T. M. DNA adduction by the potent carcinogen aflatoxin B1: mechanistic studies. J. Am. Chem. Soc 1994; 116: 1603–1609
  • Phillips D. H. Fifty years of benzo[a] pyrene. Nature 1983; 303: 468–472
  • Boryslawskyj M., Garrood A. C., Pearson J. T., Woodhead D. Elevation of glutathione S-transferase activity as a stress response to organochlorine compounds, in the freshwater mussel. Sphaerium corneum, Marine Environ. Res 1988; 84: 101–104
  • Dean J. V., Gronwald J. W., Eberlein C. V. Induction of glutathione S-transferase isoenzymes in sorghum by herbicide antidotes. Plant Physiol 1990; 92: 467–473
  • Irzyk G. P., Fuerst E. P. Purification and characterization of a glutathione. S-transferase from benoxacor-treated maize (Zea mays). Plant Physiol 1993; 102: 803–810
  • Gronwald J. W., Fuerst E. P., Eberlein C. V., Egli M. A. Effect of herbicide antidotes on glutathione content and glutathione S-transferase activity of sorghum shoots. Pest. Biochem. Physiol 1987; 29: 66–76
  • Yu S. J. Interactions of allelochemicals with detoxication enzymes of insecticide susceptible and resistant fall Armyworms. Pest. Biochem. Physiol 1984; 22: 60–68
  • Cohen E. Glutathione S-transferase activity and its induction in several strains of. Tribolium castaneum. Entomol. Exp. Appl 1986; 41: 39–44
  • Hayaoka T., Dauterman W. C. The effect of phenobarbital induction on glutathione conjugation of diazinon in susceptible and resistant house flies. Pest. Biochem. Physiol 1983; 19: 344–349
  • Cochrane B. J., LeBlanc G. A. Genetics of xenobiotic metabolism in Drosophila. 1. Genetic and environmental factors affecting glutathione S-transferase in larvae. Biochem. Pharmacol 1986; 35: 1679–1684
  • Dudler R., Hertig C., Rebmann G., Bull J., Mauch F. A pathogen-induced wheat gene encodes a protein homologous to glutathione S-transferases. Mol. Plant-Microbe Interact 1991; 4: 14–18
  • Levine A., Tenhaken R., Dixon R., Lamb C. H2O2from the oxidative burst orchestrates the plant hypersensitive disease resistance response. Cell 1994; 79: 583–593
  • Arthur J. R., Morrice P. C., Nocol F., Beddows S. E., Boyd R., Hayes J. D., Beckett G. J. The effects of selenium and copper deficiencies on glutathione S-transferase and glutathione peroxidase in rat liver. Biochem. J 1987; 248: 539–544
  • Lubet R. A., Dragnev K. H., Chauhan D. P., Nims R. W., Diwan B. A., Ward J. M., Jones C. R., Rice J. M., Miller M. S. A pleiotropic response to phenobarbital-type enzyme inducers in the F344/NCr rat. Effects of chemicals of varied structure. Biochem. Pharmacol 1992; 43: 1067–1078
  • Adams D. J., Carmichael J., Wolf C. R. Altered mouse bone marrow glutathione and glutathione transferase levels in response to cytotoxins. Cancer Res 1985; 45: 1669–1673
  • Agius C., Gidari A. S. Effect of streptozotocin on the glutathione S-transferases of mouse liver cytosol. Biochem. Pharmacol 1985; 34: 811–819
  • Yamauchi A., Yamazaki H., Kakiuchi Y. Changes in the composition of glutathione transferase subunits in rat liver after oral administration of benzo[a] pyrene. Toxicol. Environ. Chem 1991; 33: 111–119
  • Kaplowitz N., Kuhlenkamp J., Clifton G. Drug induction of hepatic glutathione S-transferases in male and female rats. Biochem. J 1975; 146: 351–356
  • Clifton G., Kaplowitz N. The glutathione S-transferases of the small intestine in the rat. Cancer Res 1977; 37: 788–791
  • Benson A. M., Barretto P. B. Effects of disulfiram, diethyldithiocarbamate, bisethylxanthogen, and benzylisothio-cyanate on glutathione transferase activities in mouse organs. Cancer Res 1985; 45: 4219–4223
  • McLellan L. L, Judah D. J., Neal G. E., Hayes J. D. Regulation of aflatoxin B1-metabolising aldehyde reductase and glutathione S-transferase by chemo-protectors. Biochem. J 1994; 300: 117–124
  • Awasthi Y. C., Partridge C. A., Dao D. D. Effect of butylated hydroxytoluene on glutathione S-transferase and glutathione peroxidase activities in rat liver. Biochem. Pharmacol 1983; 32: 1197–1200
  • De Long M. J., Prochaska H. J., Talalay P. Tissue-specific induction patterns of cancer-protective enzymes in mice by tert-butyl-4-hydroxyanisole and related substituted phenols. Cancer Res 1985; 45: 546–551
  • Lam L. K. T., Zheng B. L. Inhibitory effects of 2-n-heptylfuran and 2-n-butylthiophene on benzo[a]pyrene-induced lung and forestomach tumorigenesis in A/J mice. Nutr. Cancer 1992; 17: 19–26
  • Boyce S. J., Mantle T. J. Effect of lead acetate and carbon particles on the expression of glutathione S-transferase YfYf in rat liver. Biochem. J 1993; 294: 301–304
  • Waxman D. J., Sundseth S. S., Srivastava P. K., Lapenson D. P. Gene-specific oligonucleotide probes for a, μ, π, and microsomal rat glutathione S-transferases: analysis of liver transferase expression and its modulation by hepatic enzyme inducers and platinum anticancer drugs. Cancer Res 1992; 52: 5797–5802
  • Younes M., Schlichting R., Siegers C.-P. Glutathione S-transferase activities in rat liver: effect of some factors influencing the metabolism of xenobiotics. Pharmacol. Res. Commun 1980; 12: 115–129
  • Masukawa T., Nishimura T., Iwata H. Tissue-specific induction of intestinal glutathione S-transferases by α,β-unsatur-ated carbonyl compounds. Experientia 1984; 40: 1272–1273
  • Spencer S. R., Milczak C. A., Talalay P. Induction of glutathione transferases and NAD(P)H:Quinone reductase by fumaric acid derivatives in rodent cells and tissues. Cancer Res 1990; 50: 7871–7875
  • Sparnins V. L., Venegas P. L., Wattenberg L. W. Glutathione S-transferase activity: enhancement by compounds inhibiting chemical carcinogenesis and by dietary constituents. J. Natl. Cancer Inst 1982; 68: 493–496
  • Kensler T. W., Egner P. A., Dolan P. M., Groopman J. D., Roebuck B. D. Mechanism of protection against aflatoxin tumorigenicity in rats fed 5-(2-pyrazinyl)-4-methyl-1,2-dithiol-3-thione (oltipraz) and related 1,2-dithiol-3-thiones and 1,2-dithiol-3-ones. Cancer Res 1987; 47: 4271–4277
  • Meyer D. J., Harris J. M., Gilmore K. S., Coles B., Kensler T. W., Ketterer B. Quantitation of tissue- and sex-specific induction of rat GSH transferase subunits by dietary 1,2-dithiole-3-thiones. Carcinogenesis 1993; 14: 567–572
  • Zhang Y., Talalay P., Cho C.-G., Posner G. H. A major inducer of anticarcinogenic protective enzymes from broccoli: isolation and elucidation of structure. Proc. Natl. Acad. Sci. U.S.A 1992; 89: 2399–2403
  • David R. M., Nerland D. E. Induction of mouse liver glutathione S-transferase by ethanol. Biochem. Pharmacol 1983; 32: 2809–2811
  • Makary M., Kim H. L., Safe S., Womack J., Ivie G. W. Induction of glutathione S-transferases in genetically inbred male mice by dietary ethoxyquin hydrochloride. Comp. Biochem. Physiol 1989; 92C: 171–174
  • Kensler T. W., Egner P. A., Davidson N. E., Roebuck B. D., Pikul A., Groopman J. D. Modulation of aflatoxin metabolism, aflatoxin-N7-guanine formation, and hepatic tumorigenesis in rats fed ethoxyquin: role of induction of glutathione S-transferases. Cancer Res 1986; 46: 3924–3931
  • Derbel M., Igarashi T., Satoh T. Differential induction of glutathione S-transferase subunits by phenobarbital, 3-methylcholanthrene and ethoxyquin in rat liver and kidney. Biochim. Biophys. Acts 1993; 1158: 175–180
  • Oesch F., Friedberg T., Herbst M., Paul W., Wilhelm N., Bentley P. Effects of lindane treatment on drug metabolising enzymes and liver weight of CF1 mice in which it evoked hepatomas and in non-susceptible rodents. Chem.-Biol. Interactions 1982; 40: 1–14
  • Vos R. M. E., Snoek M. C., van Berkel W. J. H., Müller F., van Bladeren P. J. Differential induction of rat hepatic glutathione S-transferase isoenzymes by hexachlorobenzene and benzyl isothiocyanate. Comparison with induction by phenobarbital and 3-methylcholanthrene. Biochem. Pharmacol 1988; 37: 1077–1082
  • Kohli K. K., Mukhtar H., Bend J. R., Albro P. W., McKinney J. D. Biochemical effects of pure isomers of hexachlorobiphenyl- hepatic microsomal epoxide hydrolase and cytosolic glutathione S-transferase activities in the rat. Biochem. Pharmacol 1979; 28: 1444–1446
  • Moser R., Oberley T. D., Daggett D. A., Friedman A. L., Johnson J. A., Siegel F. L. Effects of lead administration on developing rat kidney. I. Glutathione S-transferase isoenzymes. Toxicol. Appl. Pharmacol 1995; 131: 85–93
  • Sparnins V. L., Wattenberg L. W. Enhancement of glutathione S-transferase activity of the mouse forestomach by inhibitors of benzo[a]pyrene-induced neoplasia of the forestomach. J. Natl. Cancer Inst 1981; 66: 769–771
  • Di Simplicio P., Jensson H., Mannervik B. Effects of inducers of drug metabolism on basic hepatic forms of mouse glutathione transferase. Biochem. J 1989; 263: 679–685
  • Guthenberg C., Morgenstern R., DePierre J. W., Mannervik B. Induction of glutathione S-transferases A, B and C in rat liver cytosol by trans-stilbene oxide. Biochim. Biophys. Acta 1980; 631: 1–10
  • Clifton G., Kaplowitz N. Effect of dietary phenobarbital, 3,4-benzo[a]pyrene and 3-methylcholanthrene on hepatic, intestinal and renal glutathione S-transferase activities in the rat. Biochem. Pharmacol 1978; 27: 1284–1287
  • Igarashi T., Irokawa N., Ono S., Ohmori S., Ueno K., Kitagawa H. Difference in the effects of phenobarbital and 3-methylcholanthrene treatment on sub-unit composition of hepatic glutathione S-transferase in male and female rats. Xenobiotica 1987; 17: 127–137
  • Ip C., El-Bayoumy K., Upadhyaya P., Ganther H., Vadhanavikit S., Thompson H. Comparative effects of inorganic and organic selenocyanate derivatives in mammary cancer chemoprevention. Carcinogenesis 1994; 15: 187–192
  • Iwata N., Minegishi K., Suzuki K., Ohno Y., Igarashi T., Satoh T., Takahashi A. An unusual profile of musk xylene-induced drug-metabolizing enzymes in rat liver. Biochem. Pharmacol 1993; 45: 1659–1665
  • Ansher S. S., Dolan P., Bueding E. Biochemical effects of dithiolthiones. Fd. Chem. Toxicol 1986; 23: 405–415
  • Lubet R. A., Nims R. W., Dragnev K. H., Jones C. R., Diwan B. A., Devor D. E., Ward J. M., Miller M. S., Rice J. M. A markedly diminished pleiotropic response to phenobarbital and structurally related xenobiotics in Zucker rats in comparison with F344/NCr or DA rats. Biochem. Pharmacol 1992; 43: 1079–1087
  • Guo Z., Smith T. J., Wang E., Eklind K. I., Chung F.-L., Yang C. S. Structure-activity relationships of arylalkyl isothiocyanates for the inhibition of 4-(methylnitrosamino)-1-(3-pyridyl)-1-butanone metabolism and the modulation of xenobiotic-metabolising enzymes in rats and mice. Carcinogenesis 1993; 14: 1167–1173
  • Ito Y., Maeda S., Souno K., Ueda N., Sugiyama T. Induction of hepatic glutathione transferase and suppression of 7,12-dimethylbenz[a]anthracene-induced chromosome aberrations in rat bone marrow cells by Sudan III and related azo dyes. J. Natl. Cancer Inst 1984; 73: 177–183
  • Lee E., Okuno S., Kariya K. Propylthiouracil inducible glutathione transferases. Selective induction of ligandin (glutathione transferase 1-1). Biochem. Pharmacol 1986; 35: 1835–1839
  • Baars A. J., Jansen M., Breimer D. D. The influence of phenobarbital, 3-methylcholanthrene and 2,3,7,8-tetra-chlorodibenzo-p-dioxin on glutathione S-transferase activity of rat liver cytosol. Biochem. Pharmacol 1978; 27: 2487–2494
  • Oesch F., Protié-Sabljié M., Friedberg T., Klimisch H.-J., Glatt H. R. Vinylidene chloride: changes in drug-metabolising enzymes, mutagenicity and relation to its targets for carcinogenesis. Carcinogenesis 1983; 4: 1031–1039
  • Skaare J. U., Solheim E. Studies on the metabolism of the antioxidant ethoxy-quin, 6-ethoxy-2,2,4-trimethyl-1,2-dihydro-quinoline in the rat. Xenobiotica 1979; 9: 649–657
  • Branen A. L. Toxicology and biochemistry of butylated hydroxyanisole and butylated hydroxytoluene. J. Am. Oil Chem. Soc 1975; 52: 59–63
  • Ciaccio P. J., Stuart J. E., Tew K. D. Overproduction of a 37.5-kDa cytosolic protein structurally related to prostaglandin F synthase in ethacrynic acid-resistant human colon cells. Mol. Pharmacol 1993; 43: 845–853
  • Ciaccio P. J., Tew K. D. cDNA and deduced amino acid sequences of a human colon dihydrodiol dehydrogenase. Biochim. Biophys. Acta 1994; 1186: 129–132
  • Ciaccio P. J., Jaiswal A. K., Tew K. D. Regulation of human dihydrodiol dehydrogenase by Michael acceptor xenobiotics. J. Biol. Chem 1994; 269: 15558–15562
  • Fentem J. H., Fry J. R. Metabolism of coumarin by rat, gerbil and human liver microsomes. Xenobiotica 1992; 22: 357–367
  • van Iersel M. L. P., Henderson C. J., Walters D. G., Price R. J., Wolf C. R., Lake B. G. Metabolism of [3-14C] coumarin by human liver microsomes. Xenobiotica 1994; 24: 795–803
  • Clejan L. A., Cederbaum A. I. Role of iron, hydrogen peroxide and reactive oxygen species in microsomal oxidation of glycerol to formaldehyde. Arch. Biochem. Biophys 1991; 285: 83–89
  • Dai Y., Rashba-Step J., Cederbaum A. I. Stable expression of human cytochrome-P4502El in HepG2 cells. Characterization of catalytic activities and production of reactive oxygen intermediates. Biochemistry 1993; 32: 6928–6937
  • Hales B. F., Neims A. H. Developmental aspects of glutathione S-transferase B (ligandin) in rat liver. Biochem. J 1976; 160: 231–236
  • Sharma R., Ahmad H., Singhal S. S., Saxena M., Srivastava S. K., Awasthi Y. C. Comparative studies of the effect of butylated hydroxyanisole on glutathione and glutathione S-transferases in the tissues of male and female CD-1 mice. Comp. Biochem. Physiol 1993; 105C: 31–37
  • Wattenberg L. W. Inhibition of carcinogenesis by minor dietary constituents. Cancer Res 1992; 52: 2085–2091s
  • Verhagen H., van Poppel G., Willems M. I., Bogaards J. J. P., Rompelberg C. J. M., van Bladeren P. J. Cancer prevention by natural food constituents. Int. Food Ingredients 1993; 1/2: 22–29
  • Nijhoff W. A., Groen G. M., Peters w. H. M. Induction of rat hepatic and intestinal glutathione S-transferases and glutathione by dietary naturally occurring anticarcinogens. Int. J. Oncol 1993; 3: 1131–1139
  • Nijhoff W. A., Peters W. H. M. Quantification of induction of rat oesophageal, gastric and pancreatic glutathione and glutathione S-transferases by dietary anticarcinogens. Carcinogenesis 1994; 15: 1769–1772
  • Sparnins V. L., Barany G., Wattenberg L. W. Effects of organosulfur compounds from garlic and onions on benzo[a]pyrene-induced neoplasia and glutathione S-transferase activity in the mouse. Carcinogenesis 1988; 9: 131–134
  • Sparnins V. L., Mott A. W., Barany G., Wattenberg L. W. Effects of allyl methyl trisulfide on glutathione S-transferase activity and BP-induced neoplasia in the mouse. Nutr. Cancer 1986; 8: 211–215
  • Bogaards J. J. P., van Ommen B., Falke H. E., Willems M. I., van Bladeren P. J. Glutathione S-transferase subunit induction patterns of brussels sprouts, allyl isothiocyanate and goitrin in rat liver and small intestinal mucosa: a new approach for the identification of inducing xenobiotics. Fd. Chem. Toxicol 1990; 28: 81–88
  • Zheng G.-Q, Zhang J., Kenney P. M., Lam L. K. T. Stimulation of glutathione S-transferase and inhibition of carcinogenesis in mice by celery seed oil constituents. Food Phytochemicals for Cancer Prevention I: Fruits and Vegetables, M.-T Huang, T. Osawa, C.-T. Ho, R. T. Rosen. American Chemical Society. 1994; 230–238
  • Lam L. K. T., Sparnins V. L., Wattenberg L. W. Effects of derivatives of kahweol and cafestol on the activity of glutathione S-transferase in mice. J. Med. Chem 1987; 30: 1399–1403
  • Lam L. K. T., Sparnins V. L., Wattenberg L. W. Isolation and identification of kahweol palmitate and cafestol palmitate as active constituents of green coffee beans that enhance glutathione S-transferase activity in the mouse. Cancer Res 1982; 42: 1193–1198
  • Sparnins V. L., Wattenberg L. W. Effects of citrus fruit oils on glutathione S-transferase (GST) activity and benzo[a] pyrene (BP) -induced neoplasia. Proc. Am. Assoc. Cancer Res 1985; 26: 123–A487
  • March T., Jeffery E., Wallig M. Cyanohydroxybutene, a cruciferous nitrile induces hepatic and pancreatic glutathione S-transferases in rats. Toxicologist 1995; 15: 264
  • Das M., Bickers D. R., Mukhtar H. Effect of ellagic acid on hepatic and pulmonary xenobiotic metabolism in mice: studies of the mechanism of its anticarcinogenic action. Carcinogenesis 1985; 6: 1409–1413
  • Trela B. A., Carlson G. P. Effect of flavanone on mixed-function oxidase and conjugation reactions in rats. Xenobiotica 1987; 17: 11–16
  • Brouard C., Siess M. H., Vernevaut M. F., Suschetet M. Comparison of the effects of feeding quercetin or flavone on hepatic and intestinal drug-metabolising enzymes of the rat. Fd. Chem. Toxicol 1988; 26: 99–103
  • Wortelboer H. M., van der Linden E. C. M., de Kruif C. A., Noordhoek J., Blaauboer B. J., van Bladeren P. J., Falke H. E. Effects of indole-3-carbinol on biotransformation enzymes in the rat: in vivochanges in liver and small intestinal mucosa in comparison with primary hepatocyte cultures. Fd. Chem. Toxicol 1992; 30: 589–599
  • Lam L. K. T., Hasegawa S. Inhibition of benzo[a]pyrene-induced fore-stomach neoplasia in mice by citrus limonoids. Nutr. Cancer 1989; 12: 43–47
  • Athar M., Khan W. A., Mukhtar H. Effect of dietary tannic acid on epidermal, lung, and forestomach polycyclic aromatic hydrocarbon metabolism and tumor-igenicity in Sencar mice. Cancer Res 1989; 49: 5784–5788
  • Hietanen E., Ahotupa M., Heikela A., Laitinen M. Dietary cholesterol-induced changes of xenobiotic metabolism in liver. II Effects of phenobarbitone and carbon tetrachloride on activities of drug-metabolizing enzymes. Drug-Nutriet Interact 1982; 1: 313–327
  • Bogaards J. J. P., Verhagen H., Willems M. I., van Poppel G., van Bladeren P. J. Consumption of brussels sprouts results in elevated α-class glutathione S-transferase levels in human blood plasma. Carcinogenesis 1994; 15: 1073–1075
  • Nijhoff W. A., Grubben M. J. A. L., Nagengast F. M., Jansen J. B. M. J., Verhagen H., van Poppel G., Peters W. H. M. Effects of consumption of Brussels sprouts on intestinal and lymphocytic glutathione and glutathione S-transferases in humans. Carcinogenesis 1995; 16: 2125–2128
  • Morel F., Fardel O., Meyer D. J., Langouet S., Gilmore K. S., Meunier B., Tu C., Kensler T. W., Ketterer B., Guillouzo A. Preferential increase of glutathione S-transferase class a transcripts in cultured human hepatocytes by phenobarbital, 3-methylcholanthrene, and dithiolethiones. Cancer Res 1993; 53: 231–234
  • Rowe J. D., Angelov I. V., Takayama T., Testori A., Listowsky I. The GSTM4gene contains functional ARE and XRE motifs in its 5′-flanking region, oral communication. ISSX GST Workshop, Amsterdam 1995
  • Rushmore T. H., King R. G., Paulson K. E., Pickett C. B. Regulation of glutathione S-transferase Ya subunit gene expression: Identification of a unique xenobiotic-responsive element controlling inducible expression by planar aromatic compounds. Proc. Natl. Acad. Sci. U.S.A 1990; 87: 3826–3830
  • Rushmore T. H., Morton M. R., Pickett C. B. The antioxidant responsive element. J. Biol. Chem 1991; 266: 11632–11639
  • Rushmore T. H., Nguyen T., Pickett C. B. ARE and XRE mediated induction of glutathione S-transferase Ya subunit gene. Structure and Function of Glutathione Transferases, K. D. Tew, C. B. Pickett, T. J. Mantle, B. Mannervik, J. D. Hayes. CRC Press, Boca Raton, FL 1993; 119–128
  • Liang Q., He J.-S., Fulco A. J. The role of barbie box sequences as cis-acting elements involved in the barbiturate-mediated induction of cytochromes P450BM-1and P450BM-3in, Bacillus megaterium. J. Biol. Chem 1995; 270: 4438–4450
  • Friling R. S., Bensimon A., Tichauer Y., Daniel V. Xenobiotic-inducible expression of murine glutathione S-transferase Ya subunit gene is controlled by an electrophile-responsive element. Proc. Natl. Acad. Sci. U.S.A 1990; 87: 6258–6262
  • Friling R. S., Bergelson S., Daniel V. Two adjacent AP-1-like binding sites form the electrophile-responsive element of the murine glutathione S-transferase Ya subunit gene. Proc. Natl. Acad. Sci. U.S.A 1992; 89: 668–672
  • Sakai M., Okuda A., Muramatsu M. Multiple regulatory elements and phorbol 12-O-tetradecanoate 13-acetate responsiveness of the rat placental glutathione transferase gene. Proc. Natl. Acad. Sci. U.S.A 1988; 85: 9456–9460
  • Ding V. D.-H., Pickett C. B. Transcriptional regulation of rat liver glutathione S-transferase genes by phenobarbital and 3-methylcholanthrene. Arch. Biochem. Biophys 1985; 240: 553–559
  • Telakowski-Hopkins C. A., King R. G., Pickett C. B. Glutathione S-transferase Ya subunit gene; Identification of regulatory elements required for basal level and inducible expression. Proc. Natl. Acad. Sci. U.S.A 1988; 85: 1000–1004
  • Paulson K. E., Darnell J. E., Rushmore T. H., Pickett C. B. Analysis of the upstream elements of the xenobiotic compound-inducible and positionally regulated glutathione S-transferase Ya gene. Mol. Cell Biol 1990; 10: 1841–1852
  • Fujisawa-Sehara A., Sogawa K., Nishi C., Fujii-Kuriyama Y. Regulatory DNA elements localized remotely upstream from the drug-metabolising cytochrome P450c gene. Nucleic Acid Res 1986; 14: 1465–1477
  • Gonzalez F. J., Nebert D. W. Autoregulation plus upstream positive and negative control regions associated with transcriptional activation of the mouse P1-450 gene. Nucleic Acid Res 1985; 13: 7269–7288
  • Neuhold L. A., Shirayoshi Y., Ozato K., Jones J. E., Nebert D. W. Regulation of mouse CYP1A1 gene expression by dioxin: requirement of two cis-acting elements during induction. Mol. Cell. Biol 1989; 9: 2378–2386
  • Swanson H I., Bradfield C. A. The Ah-receptor: genetics, structure and function. Pharmacogenetics 1993; 3: 213–230
  • Reyes H., Reisz-Porszasz S., Hankinson O. Identification of the Ah receptor nuclear translocator protein (Arnt) as a component of the DNA binding form of the Ah receptor. Science 1992; 256: 1193–1195
  • Dolwick K. M., Swanson H. I., Bradfield C. A. In vitroanalysis of Ah receptor domains involved in ligand-activated DNA recognition. Proc. Natl. Acad. Sci. U.S.A 1993; 90: 8566–8570
  • Pollenz R. S., Sattler C. A., Poland A. The aryl hydrocarbon receptor and aryl hydrocarbon receptor nuclear translocator protein show distinct subcellular localizations in Hepa lclc7 cells by immunofluorescence microscopy. Mol. Pharmacol 1994; 45: 428–438
  • Sogawa K., Nakano R., Kobayashi A., Kikuchi Y., Ohe N., Matsushita N., Fujii-Kuriyama Y. Possible function of Ah receptor nuclear translocator (Arnt) homodimer in transcriptional regulation. Proc. Natl. Acad. Sci. U.S.A 1995; 92: 1936–1940
  • Blackwood E. M., Eisenman R. N. Max: a helix-loop-helix zipper protein that forms a sequence-specific DNA-binding complex with Myc. Science 1991; 251: 1211–1217
  • Weintraub H., Davis R., Tapscott S., Thayer M., Krause M., Benezra R., Blackwell T. K., Turner D., Rupp R., Hollenberg S., Zhuang Y., Lassar A. The myoDgene family: nodal point during specification of the muscle cell lineage. Science 1991; 251: 761–766
  • Okey A. B., Riddick D. S., Harper P. A. Molecular biology of the aromatic hydrocarbon (dioxin) receptor. Trends Pharmacol. Sci 1994; 15: 226–232
  • Fujisawa-Sehara A., Sogawa K., Yamane M., Fujii-Kuriyama Y. Characterization of xenobiotic responsive elements upstream from the drug metabolising cytochrome P-450c gene: a similarity to glucocorticoid regulatory elements. Nucleic Acid Res 1987; 15: 4179–4191
  • Denison M. S., Fisher J. M., Whitlock J. P. The DNA recognition site for the dioxin-Ah receptor complex. Nucleotide sequence and functional analysis. J. Biol. Chem 1988; 263: 17221–17224
  • Denison M. S., Fisher J. M., Whitlock J. P. Inducible, receptor-dependent protein-DNA interactions at a dioxin-responsive transcriptional enhancer. Proc. Natl. Acad. Sci. U.S.A 1988; 85: 2528–2532
  • Favreau L. V., Pickett C. B. Transcriptional regulation of the rat NAD(P)H: quinone reductase gene. Identification of regulatory elements controlling basal level expression and inducible expression by planar aromatic compounds and phenolic antioxidants. J. Biol. Chem 1991; 266: 4556–4561
  • Buetler T. M., Bammler T. K., Hayes J. D., Eaton D. L. Oltipraz-mediated changes in aflatoxin B, -biotransformation in rat liver: implications for human chemointervention, submitted.
  • Buetler T. M., Gallagher E. P., Wang C., Stahl D. L., Hayes J. D., Eaton D. L. Induction of phase I and phase II drug metabolizing enzyme mRNA, protein and activity by BHA, ethoxyquin and oltipraz. Toxicol. Appl. Pharmacol, in press
  • Rushmore T. H., Pickett C. B. Transcriptional regulation of the rat glutathione S-transferase Ya subunit gene. Characterization of a xenobiotic-responsive element controlling inducible expression by phenolic antioxidants. J. Biol. Chem 1990; 265: 14648–14653
  • Nguyen T., Rushrnore T. H., Pickett C. B. Transcriptional regulation of a rat liver glutathione S-transferase Ya subunit gene. Analysis of the antioxidant response element and its activation by the phorbol ester 12-O-tetradecanoylphorbol-13-acetate. J. Biol. Chem 1994; 269: 13656–13662
  • Daniel V., Bergelson S., Pinkus R. The role of AP-1 transcription factor in the regulation of glutathione S-transferase Ya subunit gene expression by chemical agents. Structure and Function of Glutathione Transferases, K. D. Tew, C. B. Pickett, T. J Mantle, B. Mannervik, J. D. Hayes. CRC Press, Boca Raton, FL 1993; 129–136
  • Rushmore T. H., Pickett C. B. Transactivation of rat GSTA2by benzan-thracene, di-tert-butylcatechol, fisetin, menadione, naphthoflavone, tert-butyl-hydroquinone, quercetin and TCDD, personal communication.
  • Prestera T., Holtzclaw W. D., Zhang Y., Talalay P. Chemical and molecular regulation of enzymes that detoxify carcinogens. Proc. Natl. Acad. Sci. U.S.A 1993; 90: 2965–2969
  • Angel P., Imagaw M., Chiu R., Stei B., Imbra R. J., Rahmsdorf H. J., Jonat C., Herrlich P., Karin M. Phorbolester-inducible genes contain a common ciselement recognised by a TPA-modulated trans-acting factor. Cell 1987; 49: 729–739
  • Lee W., Mitchell P., Tjian R. Purified transcription factor AP-1 interacts with TPA-inducible enhancer elements. Cell 1987; 49: 741–752
  • Jaiswal A. K. Antioxidant response element. Biochem. Pharmacol 1994; 48: 439–444
  • Okuda A., Imagawa M., Sakai Muramatsu M. Functional cooperativity between two TPA responsive elements in undifferentiated F9 embryonic stem cells. EMBO J 1990; 9: 1131–1135
  • Sakai M., Muramatsu M., Nishi S. Suppression of glutathione transferase P expression by glucocorticoid. Biochem. Biophys. Res. Commun 1992; 187: 976–983
  • Li Y., Jaiswal A. K. Regulation of human NAD(P)H:quinone oxidoreductase gene. Role of AP-1 binding site contained within human antioxidant response element. J. Biol. Chem 1992; 267: 15097–15104
  • Wasserman W. W., Fahl W. E. Protein interactions with the antioxidant responsive element (ARE): multiple ARE binding proteins in human HepG2 hepatoma cells, personal communication.
  • Pinkus R., Bergelson S., Daniel V. Phenobarbital induction of AP-1 binding activity mediates activation of glutathione S-transferase and quinone reductase gene expression. Biochem. J 1993; 290: 637–640
  • Mulcahy R. T., Gipp J. J. Identification of a putative antioxidant response element in the 5′-flanking region of the human γ-glutamylcysteine synthetase heavy subunit gene. Biochem. Biophys. Res. Commun 1995; 209: 227–233
  • Hamilton T. C., Yao K.-S, Godwin A. K., Johnson S. W., Beesley J. S., O'Dwyer P. J., Ozols R. F. The mechanism of upregulation of glutathione in cisplatin resistant ovarian cancer cells. ISSX Workshop on Glutathione S-Transferases. Taylor and Francis, London 1995, in press
  • Tew K. D. The effect of ethacrynic acid on the expression of phase II detoxification enzymes. ISSX Workshop on Glutathione S-Transferases. Taylor and Francis, London 1995, in press.
  • Moffat G. J., Bammler T. K., McLaren A. W., Driessen H., Finnstrom N., Wolf C. R. Transcriptional regulation and structure/function analysis of the human and murine pi class GST genes. ISSX Workshop on Glutathione S-Transferases. Taylor and Francis, London 1995, in press
  • Thanos D., Maniatis T. NF-kB: A lesson in family values. Cell 1995; 80: 529–532
  • Anderson M. T., Staal F. J. T., Gitler C., Henenberg L. A., Herzenberg L. A. Separation of oxidant-initiated and redox-regulated steps in the NF-kB signal transduction pathway. Proc. Natl. Acad. Sci. U.S.A 1994; 91: 11527–11531
  • Naumann M., Scheidereit C. Activation of NF-kB in vivois regulated by multiple phosphorylations. EMBO J 1994; 13: 4597–4607
  • Thompson J. E., Phillips R. J., Erdjument-Bromage H., Tempst P., Ghosh S. IkB-β regulates the persistent response in a biphasic activation of NF-kB. Cell 1995; 80: 573–582
  • Singh S., Aggarwal B. B. Protein-tyrosine phosphatase inhibitors block tumor necrosis factor-dependent activation of the nuclear trancription factor NF-kB. J. Biol. Chem 1995; 270: 10631–10639
  • Schreck R., Rieber P., Baeuerle P. A. Reactive oxygen intermediates as apparently widely used messengers in the activation of the NF-kB transcription factor and HIV-1. EMBO J 1991; 10: 2247–2258
  • Hayashi T., Ueno Y., Okamoto T. Oxidoreductive regulation of nuclear factor k B. Involvement of a cellular reducing catalyst thioredoxin. J. Biol. Chem 1993; 268: 11380–11388
  • Qin J., Clore G. M., Kennedy W. M. P., Huth J. R., Gronenborn A. M. Solution structure of human thioredoxin in a mixed disulfide intermediate complex with its target peptide from the transcription factor NFkB. Structure 1995; 3: 289–297
  • Moffat G. J., McLaren A. W., Wolf C. R. Involvement of Jun and Fos proteins in regulating transcriptional activation of the human pi class glutathione S-transferase gene in multidrug-resistant MCF7 breast cancer cells. J. Biol. Chem 1994; 269: 16397–16402
  • Jantzen H., Strähle U., Gloss B., Stewart F., Schmid W., Boshart M., Miksicek R., Schütz G. Cooper-ativity of glucocorticoid response elements located far upstream of the tyrosine aminotransferase gene. Cell 1987; 49: 29–38
  • Strähle U., Klock G., Schütz G. A DNA sequence of 15 base pairs is sufficient to mediate both glucocorticoid and progesterone induction of gene expression. Proc. Natl. Acad. Sci. U.S.A 1987; 84: 7871–7875
  • Xia C., Taylor J. B., Spencer S. R., Ketterer B. The human glutathione S-transferase P1-1 gene: modulation of expression by retinoic acid and insulin. Biochem. J 1993; 292: 845–850
  • Hatayama I., Yamada Y., Tanaka K., Ichihara A., Sato K. Induction of glutathione S-transferase P-form in primary cultured rat hepatocytes by epidermal growth factor and insulin. Jpn. J. Cancer Rex 1991; 82: 807–814
  • Choi H.-S., Moore D. D. Induction of c-fosand c-jungene expression by phenolic antioxidants. Mol. Endocrinol 1993; 7: 1596–1602
  • Yoshioka K., Deng T., Cavigelli M., Karin M. Antitumor promotion by phenolic antioxidants: inhibition of AP-1 activity through induction of Fra expression. Proc. Natl. Acad. Sci. U.S.A 1995; 92: 4972–4976
  • Nguyen T., Pickett C. B. Regulation of rat glutathione S-transferase Ya subunit gene expression. DNA-protein interaction at the antioxidant responsive element. J. Biol. Chem 1992; 267: 13535–13539
  • Nishizawa M., Kataoka K., Goto N., Fujiwara K. T., Kawai S. v-maf, a viral oncogene that encodes a “leucine zipper” motif. Proc. Natl. Acad. Sci. U.S.A 1989; 86: 7711–7715
  • Swaroop A., Xu J., Pawar H., Jackson A., Skolnick C., Agarwal N. A conserved retina-specific gene encodes a basic motif/leucine zipper domain. Proc. Natl. Acad. Sci. U.S.A 1992; 89: 266–270
  • Kerppola T. K., Curran T. Maf and Nrl can bind to AP-1 sites and form heterodimers with Fos and Jun. Oncogene 1994; 9: 675–684
  • Kerppola T. K., Curran T. A conserved region adjacent to the basic domain is required for recognition of an extended DNA binding site by Maf/Nrl family proteins. Oncogene 1994; 9: 3149–3158
  • Kurschner C., Morgan J. I. The mafproto-oncogene stimulates transcription from multiple sites in a promoter that directs Purkinje neuron-specific gene expression. Mol. Cell. Biol 1995; 15: 246–254
  • Kataoka K., Fujiwara K. T., Noda M., Nishizawa M. MafB, a new Maf family transcription activator that can associate with Maf and Fos but not with Jun. Mol. Cell. Biol 1994; 14: 7581–7591
  • Igarashi K., Itoh K., Motohashi H., Hayashi N., Matuzaki Y., Nakauchi H., Nishizawa M., Yamamoto M. Activity and expression of murine small Maf family protein MafK. J. Biol. Chem 1995; 270: 7615–7624
  • Wang B., Williamson G. Transcriptional regulation of the human NAD(P)H: quinone oxidoreductase (NQO1) gene: AP-1 proteins modulate basal expression but a novel 160 kDa protein mediates induction, unpublished results.
  • Xanthoudakis S., Miao G., Wang F., Pan Y., Curran T. Redox activation of Fos-Jun DNA binding activity is mediated by a DNA repair enzyme. EMBO. J 1992; 11: 3323–3335
  • Abate C., Luk D., Curran T. A ubiquitous nuclear protein stimulates the DNA-binding activity of fos and jun indirectly. Cell Growth Diff 1990; 1: 455–462
  • Abate C., Luk D., Gentz R., Rauscher F. J., Curran T. Expression and purification of the leucine zipper and DNA-binding domains of Fos and Jun: both Fos and Jun contact DNA directly. Proc. Natl. Acad. Sci. U.S.A 1990; 87: 1032–1036
  • Abate C., Patel L., Rauscher F. J., Curran T. Redox regulation of Fos and Jun DNA-binding activity in vitro. Science 1990; 249: 1157–1161
  • Xanthoudakis S., Curran T. Identification and characterization of Ref-1, a nuclear protein that facilitates AP-1 DNA-binding activity. EMBO J 1992; 11: 653–665
  • Smeal T., Binetruy B., Mercola D., Grover-Bardwick A., Heidecker G., Rapp U. R., Karin M. Oncoprotein-mediated signalling cascade stimulates c-Jun activity by phosphorylation of serines 63 and 73. Mol. Cell. Biol 1992; 12: 3507–3513
  • De Arijard B., Hibi M., Wu I.-H, Barrett T., Su B., Deng T., Karin M., Davis R. J. JNK1: a protein kinase stimulated by UV light and Ha-Ras that binds and phosphorylates the c-Jun activation domain. Cell 1994; 76: 1025–1037
  • Seger R., Krebs E. G. The MAPK signaling cascade. FASEB J 1995; 9: 726–735
  • Lander H. M., Ogiste J. S., Teng K. K., Novogrodsky A. p21rasas a common signaling target of reactive free radicals and cellular redox stress. J. Biol. Chem 1995; 270: 21195–21198
  • Lane B. P., Lieber C. S. Effects of butylated hydroxytoluene on the ultrastructure of rat hepatocytes. Lab. Invest 1967; 16: 342–348
  • Babich H. Butylated hydroxytoluene (BHT): a review. Environ. Res 1982; 29: 1–29
  • Ito N., Fukushima S., Tsuda H. Carcinogenicity and modification of the carcinogenic response by BHA, BHT, and other antioxidants. Crit. Rev. Toxicol 1985; 15: 109–150
  • Mankowitz L., Staffas L., Bakke M., Lund J. Adrenocorticotrophic-hor-mone-dependent regulation of a μ-class glutathione transferase in mouse adrenocortical cells. Biochem. J 1995; 305: 111–118
  • Davidson N. E., Egner P. A., Kensler T. W. Transcriptional control of glutathione S-transferase gene expression by the chemoprotective agent 5-(2-Pyrazinyl)-4-methyl-1,2-dithiole-3-thione (Oltipraz) in rat liver. Cancer Res 1990; 50: 2251–2255
  • Koo P., Nagai M. K., Farber E. Multiple sites of control of glutathione S-transferase P1-1 in rat liver. J. Biol. Chem 1994; 269: 14601–14606
  • Morimura S., Suzuki T., Hochi S., Yuki A., Nomura K., Kitagawa T., Nagatsu I., Imagawa M., Muramatsu M. Trans-activation of glutathione transferase P gene during chemical hepato-carcinogenesis of the rat. Proc. Natl. Acad. Sci. U.S.A 1993; 90: 2065–2068
  • Morrow C. S., Chiu J., Cowan K. H. Posttranscriptional control of glutathione S-transferase gene expression in human breast cancer cells. J. Biol. Chern 1992; 267: 10544–10550
  • Shen H., Ranganathan S., Kuzmich S., Tew K. D. The influence of ethacrynic acid on glutathione S-transferase transcript and protein half-lives in human colon cancer cells. Biochem. Pharmacol 1995; 50: 1233–1238
  • Lewis A. D., Hickson I. D., Robson C. N., Harris A. L., Hayes J. D., Griffiths S. A., Manson M. M., Hall A. E., Moss J. E., Wolf C. R. Amplification and increased expression of alpha class glutathione S-transferase-encoding genes associated with resistance to nitrogen mustards. Proc. Natl. Acad. Sci. U.S.A 1988; 85: 8511–8515
  • Moorhouse K. G., Casida J. E. Pesticides as activators of mouse liver microsomal glutathione S-transferase. Pest. Biochem. Physiol 1992; 44: 83
  • Boyer T. D., Vessey D. A., Kempner E. Radiation inactivation of microsomal glutathione S-transferase. J. Biol. Chem 1986; 261: 16963–16968
  • Vessey D. A., Boyer T. D. Differential activation and inhibition of different forms of rat liver glutathione S-transferase by the herbicides 2,4-dichlorophen-oxyacetate (2,4-D) and 2,4,5-trichloro-phenoxyacetate (2,4,5-T). Toxicol. Appl. Pharmacol 1984; 73: 492–499
  • Ricci G., Del Boccio G., Pennelli A., Lo Bello M., Petruzzelli R., Caccuri A. M., Barra D., Federici G. Redox forms of human placenta glutathione transferase. J. Biol. Chem 1991; 266: 21409–21415
  • Tamai K., Shen H., Tsuchida S., Hatayama I., Satoh K., Yasui A., Oikawa A., Sato K. Role of cysteine residues in the activity of rat glutathione transferase P (7–7): elucidation by oligonucleotide site-directed mutagenesis. Biochem. Biophys. Res. Commun 1991; 179: 790–797
  • Nishihira J., Ishibashi T., Sakai M., Nishi S., Kumazaki T., Hatanaka Y., Tsuda S., Hikichi K. Characterization of cysteine residues of glutathione S-transferase P: evidence for steric hindrance of substrate binding by a bulky adduct to cysteine 47. Biochem. Biophys. Res. Commun 1992; 188: 424–432
  • Phillips M. F., Mantle T. J. The initial-rate kinetics of mouse glutathione S-transferase YfYf. Evidence for an allosteric site for ethacrynic acid. Biochem. J 1991; 275: 703–709
  • Fernandes C. L., Dong J.-H, Chisari F. V., Montali J. A., Schmidt D. E., Prochaska H. J. Elevations of NAD(P)H:(quinone-acceptor)oxidoreduc tase, glutathione, and α- and μ-class glutathione S-transferase isoforms in livers of transgenic mice with chronic active hepatitis: a compensatory response to injury, submitted
  • Sato K. Glutathione S-tranferases as markers of preneoplasia and neoplasia. Adv. Cancer. Res 1989; 52: 205–255
  • Sugioka Y., Fujii-Kuriyama Y., Kitagawa T., Muramatsu M. Changes in polypeptide pattern of rat liver cells during chemical hepatocarcinogenesis. Cancer Res 1985; 45: 365–378
  • Rao M. S., Nemali M. R., Usuda N., Scarpelli D. G., Makino T., Pitot H. C., Reddy J. K. Lack of expression of glutathione S-transferase P, γ-glutamyl transpeptidase and a-fetoprotein mRNAs in liver tumors induced by peroxisome proliferators. Cancer Res 1988; 48: 4919–4925
  • Yokoyama Y., Tsuchida S., Hatayama I., Sato K. Lack of peroxisomal enzyme inducibility in rat hepatic preneoplastic lesions induced by mutagenic carcinogens: contrasted expression of glutathione S-transferase P form and enoyl CoA hydratase. Carcinogenesis 1993; 14: 393–398
  • Burt R. K., Garfield S., Johnson K., Thorgeirsson S. S. Transformation of rat liver epithelial cells with v-H-rasor v-rafcauses expression of MDR-1, glutathione S-transferase-P and increased resistance to cytotoxic chemicals. Carcinogenesis 1988; 9: 2329–2332
  • Diccianni M. B., Imagawa M., Muramatsu M. The dyad palindromic glutathione transferase P enhancer binds multiple factors including AP1. Nucleic Acid Res 1992; 20: 5153–5158
  • Imagawa M., Osada S., Okuda A., Muramatsu M. Silencer binding proteins function on multiple cis-elements in the glutathione transferase P gene. Nucleic Acid Res 1991; 19: 5–10
  • Hayes P. C., Harrison D. J., Bouchier I. A. D., McLellan L. I., Hayes J. D. Cytosolic and microsomal glutathione S-transferase isoenzymes in normal human liver and intestinal epithelium. Cut 1989; 30: 854–859
  • Hayes P. C., May L., Hayes J. D., Harrison D. J. Glutathione S-transferases in human liver cancer. Gut 1991; 32: 1546–1549
  • Harrison D. J., May L., Hayes P. C., Haque M. M., Hayes J. D. Glutathione S-transferases in alcoholic liver disease. Gut 1990; 31: 909–912
  • Harrison D. J., Kharbanda R., Bishop D., McLellan L. I., Hayes J. D. Glutathione S-transferase isoenzymes in human renal carcinoma demonstrated by immunohistochemistry. Carcinogenesis 1989; 10: 1257–1260
  • Shiratori Y., Soma Y., Maruyama H., Sato S., Takano A., Sato K. Im-munohistochemical detection of the placental form of glutathione S-transferase in dysplastic and neoplastic human uterine cervix lesions. Cancer Res 1987; 47: 6806–6809
  • Di Ilio C., Del Boccio G., Aceto A., Federici G. Alteration of glutathione transferase isoenzyme concentrations in human renal carcinomas. Carcinogenesis 1987; 8: 861–864
  • Di Ilio C., Del Boccio G., Aceto A., Casaccia R., Mucilli F., Federici G. Elevation of glutathione transferase activity in human lung tumor. Curcinogenesis 1988; 9: 335–340
  • Eimoto H., Tsutsumi M., Nakajima A., Yamamoto K., Takashima Y., Maruyama H., Konishi Y. Expression of the glutathione S-transferase placental form in human lung carcinomas. Carcinogenesis 1988; 9: 2325–2327
  • Shea T. C., Kelley S. L., Henner W. D. Identification of an anionic form of glutathione transferase present in many human tumors and human tumor cell lines. Cancer Res 1988; 48: 527–533
  • Moscow J. A., Fairchild C. R., Madden M. J., Ransom D. T., Wieand H. S., O'Brien E. E., Poplack D. G., Crossman J., Myers C. E., Cowan K. H. Expression of anionic glutathione S-transferase and P-glycoprotein genes in human tissues and tumors. Cancer Res 1989; 49: 1422–1428
  • Peters W. H. M., Nagengast F. M., Wobbes T. Glutathione S-transferases in normal and cancerous human colon tissue. Carcinogenesis 1989; 10: 2371–2374
  • Moscow J. A., Townsend A. J., Goldsmith M E., Peng J., Vickers P. J., Poisson R., Legault-Poisson S., Myers C. E., Cowan K. H. Isolation of the human anionic glutathione S-transferase cDNA and the relation of its gene expression to estrogen-receptor content in primary breast cancer. Proc. Nutl. Acad. Sci. U.S.A 1988; 85: 6518–6522
  • Howie A. F., Miller W. R., Hawkins R. A., Hutchinson A. R., Beckett G. J. Expression of glutathione S-transferase B1, B2, Mu and Pi in breast cancers and their relationship to oestrogen receptor status. Br. J. Cancer 1989; 60: 834–837
  • Gilbert L., Elwood L. J., Merino M., Masood S., Barnes R., Steinberg S. M., Lazarous D. F., Pierce L., Angelo T., Moscow J. A., Townsend A. J., Cowan K. H. A pilot study of π-class glutathione S-transferase expression in breast cancer: correlation with estrogen receptor expression and prognosis in node-negative breast cancer. J. Clin. Oncol 1993; 11: 49–58
  • Grignon D. J., Abdel-Malak M., Mertens W. C., Sakr W. A., Shepherd R. R. Glutathione S-transferase expression in renal cell carcinoma: a new marker of differentiation. Mod. Pathol 1994; 7: 186–189
  • Mulder T. P. J., Verspaget H. W., Sier C. F. M., Roelofs H. M. J., Ganesh S., Griffioen G., Peters W. H. M. Glutathione S-transferase in colorectal tumors is predictive for overall survival. Cancer Res 1995; 55: 2696–2702
  • Green J. A., Robertson L. J., Clark A. H. Glutathione S-transferase expression in benign and malignant ovarian tumours. Br. J. Cancer 1993; 68: 235–239
  • Hamada S.-I, Kamada M., Furumoto H., Hirao T., Aono T. Expression of glutathione S-transferase-π in human ovarian cancer as an indicator of resistance to chemotherapy. Gynecol. Oncol 1994; 52: 313–319
  • Tidefelt U., Elmhorn-Rosenborg A., Paul C., Hoa X.-Y, Mannervik B., Eriksson L. C. Expression of glutathione S-transferase π as a predictor for treatment results at different stages of acute non-lymphoblastic leukemia. Cancer Res 1992; 52: 3281–3285
  • Okuyama T., Maehara Y., Endo K., Baba H., Adachi Y., Kuwano M., Sugimachi K. Expression of glutathione S-transferase-π and sensitivity of human gastric cancer cells to cisplatin. Cancer 1994; 74: 1230–1236
  • Murphy D., McGown A. T., Hall A., Cattan A., Crowther D., Fox B. W. Glutathione S-transferase activity and isoenzyme distribution in ovarian tumour biopsies taken before or after cytotoxic chemotherapy. Br. J. Cancer 1992; 66: 937–942
  • Lee W., Morton R. A., Epstein J I., Brooks J. D., Campbell P. A., Bova G. S., Hsieh W.-S, Isaacs W. B., Nelson W. G. Cytidine methylation of regulatory sequences near the π-class glutathione S-transferase gene accompanies human prostatic carcinogenesis. Proc. Natl. Acad. Sci. U.S.A 1994; 91: 11733–11737
  • Xia C L., Cowell I. G., Dixon K. H., Pemble S. E., Ketterer B., Taylor J. B. Glutathione transferase pi: its minimal promoter and downstream cis-acting element. Biochem. Biophys. Rex Comm 1991; 176: 233–240
  • Hussey A. J., Stockman P. K., Beckett G. J., Hayes J. D. Variations in the glutathione S-transferase subunits expressed in human livers. Biochim. Biophys. Acta 1986; 874: 1–12
  • Listowsky I. Variable expression of skin GST 9.9 in HeLa cells, personal communication
  • Matsumoto K., Gasser D. L. Polymorphism of glutathione S-transferase in laboratory rats. Biochem. Genet 1983; 21: 1209–1215
  • Johnson J. A., Hayward J. J., Kornguth S. E., Siegel F. L. Effects of hyper bilirubinaemia on glutathione S-transferase isoenzyrnes in cerebellar cortex of the Gunn rat. Biochem. J 1993; 291: 453–461
  • Singhal S. S., Saxena M., Awasthi S., Ahmad H., Sharma R., Awasthi Y. C. Gender related differences in the expression and characteristics of glutathione S-transferases of human colon. Biochim. Biophys. Acta 1992; 1171: 19–26
  • Singhal S. S., Saxena M., Awasthi S., Mukhtar H., Zaidi S. I. A., Ahmad H., Awasthi Y. C. Glutathione S-transferases of human skin: qualitative and quantitative differences in men and women. Biochim. Biophys. Acta 1993; 1163: 266–272
  • Srivastava P. K., Waxman D. J. Sex-dependent expression and growth hormone regulation of class alpha and class mu glutathione S-transferase mRNAs in adult rat liver. Biochem. J 1993; 294: 159–165
  • Hatayama I., Satoh K., Sato K. Developmental and hormonal regulation of the major foim of hepatic glutathione S-transferase in male mice. Biochem. Biophys. Res. Commun 1986; 140: 581–588
  • Faulder C. G., Hirrell P. A., Hume R., Strange R. C. Studies of the development of basic, neutral and acidic isoenzymes of glutathione S-transferase in human liver, adrenal, kidney and spleen. Biochem. J 1987; 241: 221–228
  • Strange R. C., Howie A. F., Hume R., Matharoo B., Bell J., Hiley C., Jones P., Beckett G. J. The developmental expression of alpha-, mu- and pi-class glutathione S-transferases in human liver. Biochim. Biophys. Acta 1989; 993: 186–190
  • Tee L. B. G., Gilmore K. S., Meyer D. J., Ketterer B., Vandenberghe Y., Yeoh G. C. T. Expression of glutathione S-transferase during rat liver development. Biochem. J 1992; 282: 209–218
  • Awasthi Y. C., Sharma R., Singhal S. S. Human glutathione S-transferases. Int. J. Biochem 1994; 26: 295–308
  • Peters W. H. M., Wormskamp N. G. M., Thies E. Expression of glutathione S-transferases in normal gastric mucosa and in gastric tumors. Carcinogenesis 1990; 11: 1593–1596
  • Peters W. H. M., Roelofs H. M. J., Nagengast F. M., Van Tongeren J. H. M. Human intestinal glutathione S-transferases. Biochem. J 1989; 257: 471–476
  • Meikle I., Hayes J. D., Walker S. W. Expression of an abundant alphaclass glutathione S-transferase in bovine and human adrenal cortex tissues. J. Endocrinol 1992; 132: 83–92
  • Corrigall A. V., Kirsch R. E. Glutathione S-transferase distribution and concentration in human organs. Biochem. Int 1988; 16: 443–448
  • Grayson D. R., Costa R. H., Xanthopoulos K. G., Darnell J. E. A cell-specific enhancer of the mouse αl-antitrypsin gene has multiple functional regions and corresponding protein-binding sites. Mol. Cell. Biol 1988; 8: 1055–1066
  • Costa R. H., Grayson D. R., Darnell J. E. Multiple hepatocyte-enriched nuclear factors function in the regulation of transthyretin and αl-antitrypsin genes. Mol. Cell. Biol 1989; 9: 1415–1425
  • Herbst R. S., Friedman N., Darnell J. E., Babiss L. E. Positive and negative regulatory elements in the mouse albumin enhancer. Proc. Natl. Acad. Sci. U.S.A 1989; 86: 1553–1557
  • Abramovitz M., Testori A., Angelov I. V., Darmon A., Listowsky I. Brain and testis selective expression of the glutathione S-transferase Yb3subunit is governed by tandem direct repeat octamer motifs in the 5′-flanking region of its gene. Mol. Brain Res 1995; 28: 37–46
  • Maines M. D., Sluss P. M., Iscan M. Cis-platinum-mediated decrease in serum testosterone is associated with depression of luteinizing hormone receptors and cytochrome P-450scc in rat testis. Endocrinology 1990; 126: 2398–2406
  • Farber E. Clonal adaption during carcinogenesis. Biochem. Pharmacol 1990; 39: 1837–1846
  • Lewis A. D., Hayes J. D., Wolf C. R. Glutathione and glutathione-depen-dent 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
  • Wang A. L., Tew K. D. Increased glutathione S-transferase activity in a cell line with acquired resistance to nitrogen mustards. Cancer Treat. Rep 1985; 69: 677–682
  • Puchalski R., Fahl W. E. Expression of recombinant glutathione S-transferases π, Ya or Yb1confers resistance to alkylating agents. Proc. Natl. Acad. Sci. U.S.A 1990; 87: 2443–2447
  • Batist G., Tulpule A., Sinha B. K., Katki A. G., Myers C. E., Cowan K. H. Overexpression of a novel anionic glutathione transferase in multidrug-resistant human ‘breast cancer cells. J. Biol. Chem 1986; 261: 15544–15549
  • Cole S. P. C., Downes H. F., Mirski S. E. L., Clements D. J. Alterations in glutathione and glutathione-related enzymes in a multidrug-resistant small cell lung cancer cell line. Mol. Pharmacol 1990; 37: 192–197
  • Chao C. C., Huang Y.-T, Ma C. M., Chou W., Lin-Chao S. Over-expression of glutathione S-transferase and elevation of thiol pools in a multidrug-resistant human colon cancer cell line. Mol. Pharmacol 1992; 41: 69–75
  • Schisselbauer J. C., Crescimanno M., D'Alessandro N., Clapper M., Toulmond S., Tapiero H., Tew K. D. Glutathione, glutathione S-transferases, and related redox enzymes in adriamycin resistant cell lines with a multidrug resistant phenotype. Cancer Commun 1989; 1: 133–139
  • Singh S. V., Nair S., Ahmad H., Awasthi Y. C., Krishan A. Glutathione S-transferases and glutathione per-oxidases in doxorubicin-resistant murine leukemic P388 cells. Biochem. Pharmacol 1989; 38: 3505–3510
  • Schecter R. L., Woo A., Duong M., Batist G. In vivoand in vitromechanisms of drug resistance in a rat mammary carcinoma model. Cancer Res 1991; 51: 1434–1442
  • Wang H.-F., Lee T.-C. Glutathione S-transferase π facilitates the excretion of arsenic from arsenic-resistant Chinese hamster ovary cells. Biochem. Biophys. Res. Commun 1993; 192: 1093–1099
  • Giaccia A. J., Lewis A. D., Denko N. C., Cholon A., Evans J. W., Waldren C. A., Stamato T. D., Brown J. M. The hypersensitivity of the Chinese hamster ovary variant BL-10 to bleomycin killing is due to lack of glutathione S-transferase-α activity. Cancer Res 1991; 51: 4463–4469
  • Wareing C. J., Black S. M., Hayes J. D., Wolf C. R. Increased levels of alpha and pi class glutathione S-transferases in cell lines resistant to 1-chloro-2,4-dinitrobenzene. Eur. J. Biochem 1993; 217: 671–676
  • Buller A. L., Clapper M. L., Tew K. D. Glutathione S-transferases in nitrogen mustard-resistant and -sensitive cell lines. Mol. Pharmacol 1987; 31: 575–578
  • Robson C. N., Lewis A. D., Wolf C. R., Hayes J. D., Hall A., Proctor S. J., Harris A. L., Hickson I. D. Reduced levels of drug-induced DNA cross-linking in nitrogen mustard-resistant Chinese hamster ovary cells expressing elevated glutathione S-transferase activity. Cancer Res 1987; 47: 6022–6027
  • Yang W. Z., Begleiter A., Johnston J. B., Israels L. G., Mowat M. R. A. Role of glutathione and glutathione S-transferase in chlorambucil resistance. Mol. Pharmacol 1992; 41: 625–630
  • McGown A. T., Fox B. W. A proposed mechanism of resistance to cyclophosphamide and phosphoramide mustard in a Yoshida cell line in vitro. Cancer Chemother. Pharmacol 1986; 17: 223–226
  • Wareing C. J. The Role of the Glutathione S-Transferases in Resistance to Cytotoxic Compounds. Ph.D. thesis, University of Edinburgh. 1990
  • Kuzmich S., Vanderveer L. A., Walsh E., LaCreta F. P., Tew K. D. Increased levels of glutathione S-transferase transcript as a mechanism of resistance to ethacrynic acid. Biochem. J 1992; 281: 219–224
  • Whelan R. D. H., Hosking L. K., Townsend A. J., Cowan K. H., Hill B. T. Differential increases in glutathione S-transferase activities in a range of multidrug-resistant human tumor cell lines. Cancer Commun 1989; 1: 359–365
  • Armstrong D. K., Gordon G. B., Hilton J., Streeper R. T., Colvin O. M., Davidson N. E. Hepsulfam sensitivity in human breast cancer cell lines: the role of glutathione and glutathione S-transferase in resistance. Cancer Res 1992; 52: 1416–1421
  • Gupta V., Singh S. V., Ahmad H., Medh R. D., Awasthi Y. C. Glutathione and glutathione S-transferases in a human plasma cell line resistant to melphalan. Biochem. Pharmacol 1989; 38: 1993–2000
  • Xu B. H., Gupta V., Singh S. V. Mitomycin C sensitivity in human bladder cancer cells: possible role of glutathione and glutathione transferase in resistance. Arch. Biochem. Biophys 1994; 308: 164–170
  • Peters W. H. M., Roelofs H. M. J. Biochemical characterization of resistance to mitoxantrone and adriamycin in Caco-2 human colon adenocarcinoma cells: a possible role for glutathione S-transferases. Cancer Res 1992; 52: 1886–1890
  • Woo A., Tsao M A., Batist G. Drug resistance in cultured rat liver epithelial cells spontaneously and chemically transformed. Carcinogenesis 1992; 13: 1675–1677
  • Chen G., Waxman D. J. Identification of glutathione S-transferase as a determinant of 4-hydroperoxycyclophosphamide resistance in human breast cancer cells. Biochem. Pharmacol 1995; 49: 1691–1701
  • Zhang X., Wang T., Batist G., Tsao M.-S. Transforming growth factor β1 promotes spontaneous transformation of cultured rat liver epithelial cells. Cancer Res 1994; 54: 6122–6128
  • Das M., Bickers D. R., Mukhtar H. Plant phenols as in vitro inhibitors of glutathione S-transferase(s). Biochem. Biophys. Res. Commun 1984; 120: 427–433
  • Bach M. K., Brashler J. R., Johnson M. A. Inhibition by sulfasalazine of LTC synthetase and the rat liver glutathione S-transferases. Biochem. Pharmacol 1985; 34: 2695–2704
  • Tew K. D., Bomber A. M., Hoffman S. J. Ethacrynic acid and piriprost as enhancers of cytotoxicity in drug resistant and sensitive cell lines. Cancer Res 1988; 48: 3622–3625
  • Hall A., Robson C. N., Hickson I. D., Harris A. L., Proctor S. J., Cattan A. R. Possible role of inhibition of glutathione S-transferase in the partial reversal of chlorambucil resistance by indomethacin in a Chinese hamster ovary cell line. Cancer Res 1989; 49: 6265–6268
  • Fehring S. I., Ahokas J. T. Effect of the glutathione S-transferase inhibitor, tienilic acid, on biliary excretion of sulphobromophthalein. Chem.-Biol. Interactions 1989; 69: 23–32
  • Benz C. C., Keniry M. A., Ford J. M., Townsend A. J., Cox F. W., Palayoor S., Matlin S. A., Hait W. N., Cowan K. H. Biochemical correlates of the antitumor and antmitochondrial properties of gossypol enantiomers. Mol. Pharmacol 1990; 37: 840–847
  • Ouwerkerk-Mahadevan S., van Boom J. H., Dreef-Tromp M. C., Ploemen J. H. T. M., Meyer D. J., Mulder G. J. Glutathione analogues as novel inhibitors of rat and human glutathione S-transferase isoenzymes, as well as of glutathione conjugation in isolated rat hepato cytes and in the rat, in vivo. Biochem. J 1995; 308: 283–290
  • Manoharan T. H., Puchalski R. B., Burgess J. A., Pickett C. B., Fahl W. E. Promoter-glutathione S-transferase Ya cDNA hybrid genes. Expression and conferred resistance to an alkylating molecule in mammalian cells. J. Biol. Chem 1987; 262: 3739–3745
  • Manoharan T. H., Welch P. J., Gulick A. M., Puchalski R. B., Lathrop A. L., Fahl W. E. Expression of tandem glutathione S-transferase recombinant genes in COS cells for analysis of efficiency of protein expression and associated drug resistance. Mol. Pharmacol 1991; 39: 461–467
  • Nakagawa K., Saijo N., Tsuchida S., Sakai M., Tsunokawa Y., Yokota J., Muramatsu M., Sato K., Terada M., Tew K. D. Glutathione S-transferase as a determinant of drug resistance in transfectant cell lines. J. Biol. Chem 1990; 265: 4296–4301
  • Black S. M., Beggs J. D., Hayes J. D., Bartoszek A., Muramatsu M., Sakai M., Wolf C. R. Expression of human glutathione S-transferases in S. cerevisiaeconfers resistance to the anticancer drugs adriamycin and chlorambucil. Biochem. J 1990; 268: 309–315
  • Schecter R. L., Alaoui-Jamali M. A., Woo A., Fahl W. E., Batist G. Expression of a rat glutathione S-transferase complementary DNA in rat mammary carcinoma cells: impact upon alkylator-in-duced toxicity. Cancer Res 1993; 53: 4900–4906
  • Greenbaum M., Létourneau S., Assar H., Schecter R. L., Batist G., Cournoyer D. Retrovirus-mediated gene transfer of rat glutathione S-transferase Yc confers alkylating drug resistance in NIH 3T3 mouse fibroblasts. Cancer Res 1994; 54: 4442–4447
  • Fields W. R., Li Y., Townsend A. J. Protection by transfected glutathione S-transferase isoenzymes against carcinogen-induced alkylation of cellular macro molecules in human MCF-7 cells. Carcino-genesis 1994; 15: 1155–1160
  • Moscow J. A., Townsend A. J., Cowan K. H. Elevation of class glutathione S-transferase activity in human breast cancer cells by transfection of the GST gene and its effect on sensitivity to toxins. Mol. Pharmacol 1989; 36: 22–28
  • Leyland-Jones B. R., Townsend A. J., Tu C., Cowan K. H., Goldsmith M. E. Antineoplastic drug sensitivity of human MCF-7 breast cancer cells stably transfected with a human α class glutathione S-transferase gene. Cancer Res 1991; 51: 587–594
  • Townsend A. J., Tu C., Cowan K. H. Expression of human μ or α class glutathione S-transferases in stably transfected human MCF-7 breast cancer cells: effect on cellular sensitivity to cytotoxic agents. Mol. Pharmacol 1992; 41: 230–236
  • Shimabukuro R. H., Frear D. S., Swanson H. R., Walsh W. C. Glutathione conjugation: an enzymatic basis for atrazine resistance in corn. Plant Physiol. 1971; 47: 10–14
  • Marrs K. A., Alfenito M. R., Lloyd A. M., Walbot V. A glutathione S-transferase involved in vacuolar transfer encoded by the maize gen Bronze-2. Nature 1995; 375: 397–400
  • Strange R. C. Glutathione S-transferases and cancer susceptibility. ISSX Workshop on Glutathione S-transferases. Taylor and Francis, London, Amsterdam 1995, in press
  • Wiencke J. K., Kelsey K. T., Lamela R. A., Toscano W. A. Human glutathione S-transferase deficiency as a marker of susceptibility to epoxide-induced cytogenetic damage. Cancer Res 1990; 50: 1585–1590
  • Shields P. G., Bowman E. D., Harrington A. M., Doan V. T., Weston A. Polycyclic aromatic hydrocarbon-DNA adducts in human lung and cancer susceptibility genes. Cancer Res 1993; 53: 3486–3492
  • Liu Y. H., Taylor J., Linko P., Lucier G. W., Thompson C. L. Glutathione S-transferase p in human lymphocyte and liver: role in modulating formation of carcinogen-derived DNA adducts. Carcino-genesis 1991; 12: 2269–2275
  • Seidegård J., Pero R. W., Miller D. G., Beattie E. J. A glutathione transferase in human leukocytes as a marker for the susceptibility to lung cancer. Carcino-genesis 1986; 7: 751–753
  • Brockmöller J., Kerb R., Drakoulis N., Nitz M., Roots I. Genotype and phenotype of glutathione S-transferase class μ isoenzymes μ and ψ in lung cancer patients and controls. Cancer Res 1993; 53: 1004–1011
  • Nazar-Stewart V., Motulsky A. G., Eaton D. L., White E., Hornung S. K., Leng Z.-T, Stapleton P., Weiss N. S. The glutathione S-transferase μ polymorphism as a marker for susceptibility to lung carcinoma. Cancer Res 1993; 53: 2313–2318
  • Zhong S., Howie A. F., Ketterer B., Taylor J. B., Hayes J. D., Beckett G. J., Wathen C. G., Wolf C. R., Spurr N. K. Glutathione S-transferase mu locus: use of genotyping and phenotyping assays to assess association with lung cancer susceptibility. Carcinogenesis 1991; 12: 1533–1537
  • Hirvonen A., Husgafvel-Pursianen K., Anttila S., Vainio H. The GSTM1null genotype as a potential risk modifier for squamous cell carcinoma of the lung. Carcinogenesis 1993; 14: 1479–1481
  • Grinberg-Funes R. A., Singh V. N., Perera F. P., Bell D. A., Young T. L., Dickey C., Wang L. W., Santella R. M. Polycyclic aromatic hydrocarbon-DNA adducts in smokers and their relationship to micronutrient levels and the glutathione S-transferase M1 genotype. Carcinogenesis 1994; 15: 2449–2454
  • Cheng T.-J, Christiani D. C., Xu X., Wain J. C., Wiencke J. K., Kelsey K. T. Glutathione S-transferase μ genotype, diet, and smoking as determinants of sister chromatid exchange frequency in lymphocytes. Cancer Epidemiol. Biomarkers Prev 1995; 4: 535–542
  • Smith C. M., Kelsey K. T., Wiencke J. K., Leyden K., Levin S., Christiani D. C. Inherited glutathione S-transferase deficiency is a risk factor for pulmonary asbestosis. Cancer Epidemiol. Biomarkers Prev 1994; 3: 471–477
  • Daly A. K., Thomas D. J., Cooper J., Pearson W. R., Neal D. E., Idle J. R. Homozygous deletion of gene for glutathione S-transferase M1 in bladder cancer. Br. Med. J 1993; 307: 481–482
  • Bell D. A., Taylor J. A., Paulson D. F., Robertson C. N., Mohler J. L., Lucier G. W. Genetic risk and carcinogen exposure: a common inherited defect of the carcinogen-metabolism gene glutathione S-transferase M1 (GSTM1) that increases susceptibility to bladder cancer. J. Natl. Cancer Inst 1993; 85: 1159–1164
  • Brockmo Uller J., Kerb R., Drakoulis N., Staffeldt B., Roots I. Glutathione S-transferase M1 and its variants A and B as host factors of bladder cancer susceptibility: a case-control study. Cancer Res 1994; 54: 4103–4111
  • Strange R. C., Matharoo B., Faulder G. C., Jones P., Cotton W., Elder J. B., Deakin M. The human glutathione S-transferases: a case-control study of the incidence of the GST1 0 phenotype in patients with adenocarcinoma. Carcino-genesis 1991; 12: 25–28
  • Zhong S., Wyllie A. H., Barnes D., Wolf C. R., Spurr N. K. Relationship between the GSTM1 genetic polymorphism and susceptibility to bladder, breast and colon cancer. Carcinogenesis 1993; 14: 1821–1824
  • Heagerty A. H. M., Fitzgerald D., Smith A., Bowers B., Jones P., Fryer A. A., Zhao L., Alldersea J., Strange R. C. Glutathione S-transferase GSTM1 phenotypes and protection against cutaneous tumours. Lancet 1994; 343: 266–268
  • Wiencke J. K., Pemble S., Ketterer B., Kelsey K. T. Gene deletion of glutathione S-transferase theta- correlation with induced genetic damage and potential role in endogenous mutagenesis. Cancer Epidemiol. Biomarkers Prev 1995; 4: 253–259
  • Warwick A., Sarhanis P., Redman C., Pemble S., Taylor J. B., Ketterer B., Jones P., Alldersea J., Gilford J., Yengi L., Fryer A., Strange R. C. Theta class glutathione S-transferase GSTT1 genotypes and susceptibility to cervical neoplasia: interactions with GSTM1, CYP2D6 and smoking. Carcinogenesis 1994; 15: 2841–2845
  • Chenevix-Trench G., Young J., Coggan M., Board P. Glutathione S-transferase M1 and T1 polymorphisms: susceptibility to colon cancer and age of onset. Carcinogenesis 1995; 16: 1655–1657
  • Hall A. G., Autzen P., Cattan A. R., Malcolm A. J., Cole M., Kernahan J., Reid M. M. Expression of μ class glutathione S-transferase correlates with event-free survival in childhood acute lymphoblastic leukemia. Cancer Res 1994; 54: 5251–5254
  • Nakajima T., Elovaara E., Anttila S., Hirvonen A., Camus A.-M, Hayes J. D., Ketterer B., Vainio H. Expression and polymorphism of glutathione S-transferase in human lungs: risk factors in smoking-related lung cancer. Carcinogenesis 1995; 16: 707–711
  • Idle J. R., Armstrong M., Boddy A. V., Boustead C., Cholerton S., Cooper J., Daly A. K., Ellis J., Gregory W., Hadidi H., Höfer C., Holt J., Leathart J., MeCracken N., Monkman S. C., Painter J. E., Taber H., Walker D., Yule M. The pharmacogenetics of chemical carcinogenesis. Pharmacogenetics 1992; 2: 246–258

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Order Reprints Request Corporate Permissions

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

Request Academic Permissions

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.

Related research

People also read lists articles that other readers of this article have read.

Recommended articles lists articles that we recommend and is powered by our AI driven recommendation engine.

Cited by lists all citing articles based on Crossref citations.
Articles with the Crossref icon will open in a new tab.