Mechanisms of induction of cytosolic and microsomal glutathione transferase (GST) genes by xenobiotics and pro-inflammatory agents

References

• Abramovitz, M., Listowsky, I. (1987) Selective expression of a unique glutathione S-transferase Yb3 gene in rat brain. J Biol Chem 262:7770–7773.
   PubMed Web of Science ®Google Scholar
• Ackerman, W.E., 4th, Summerfield, T.L., Vandre, D.D., Robinson, J.M., Kniss, D.A. (2008) Nuclear factor-κB regulates inducible prostaglandin E synthase expression in human amnion mesenchymal cells. Biol Reprod 78:68–76.
   PubMed Web of Science ®Google Scholar
• Adachi, Y., Nanno, T., Yamashita, M., Ueshima, S., Yamamoto, T. (1985) Induction of rat liver bilirubin-conjugating enzymes and glutathione S-transferase by rifampicin. Gastroenterol Jpn 20:104–110.
   PubMedGoogle Scholar
• Ago, H., Kanaoka, Y., Irikura, D., Lam, B.K., Shimamura, T., Austen, K.F., Miyano, M. (2007) Crystal structure of a human membrane protein involved in cysteinyl leukotriene biosynthesis. Nature 448:609–612.
   PubMed Web of Science ®Google Scholar
• Alander, J., Lengqvist, J., Holm, P.J., Svensson, R., Gerbaux, P., Heuvel, R.H., Hebert, H., Griffiths, W.J., Armstrong, R.N., Morgenstern, R. (2009) Microsomal glutathione transferase 1 exhibits one-third-of-the-sites-reactivity towards glutathione. Arch Biochem Biophys 487:42–48.
   PubMed Web of Science ®Google Scholar
• An, J.H., and Blackwell, T.K. (2003) SKN-1 links C. elegans mesendodermal specification to a conserved oxidative stress response. Genes Dev 17:1882–1893.
   PubMed Web of Science ®Google Scholar
• Armstrong, R.N. (1991) Glutathione S-transferases: reaction mechanism, structure, and function. Chem Res Toxicol 4:131–140.
   PubMed Web of Science ®Google Scholar
• Armstrong, R.N. (1997) Structure, catalytic mechanism, and evolution of the glutathione transferases. Chem Res Toxicol 10:2–18.
   PubMed Web of Science ®Google Scholar
• Atkinson, H.J., and Babbitt, P.C. (2009) Glutathione transferases are structural and functional outliers in the thioredoxin fold. Biochemistry 48:11108–11116.
   PubMed Web of Science ®Google Scholar
• Baars, A.J., Jansen, M., Breimer, D.D. (1978) The influence of phenobarbital, 3-methylcholanthrene and 2,3,7,8-tetrachlorodibenzo-p-dioxin on glutathione S-transferase activity of rat liver cytosol. Biochem Pharmacol 27:2487–2497.
   PubMed Web of Science ®Google Scholar
• Bass, N.M., Kirsch, R.E., Tuff, S.A., Saunders, S.J. (1977) Radioimmunoassay of ligandin. Biochim Biophys Acta 494:131–143.
   PubMed Web of Science ®Google Scholar
• Bass, N.M., Kirsch, R.E., Tuff, S.A., Marks, I., Saunders, S.J. (1977) Ligandin heterogeneity: evidence that the two non-identical subunits are the monomers of two distinct proteins. Biochim Biophys Acta 492:163–175.
   PubMed Web of Science ®Google Scholar
• Beischlag, T.V., Luis Morales, J., Hollingshead, B.D., Perdew, G.H. (2008) The arylhydrocarbon receptor complex and the control of gene expression. Crit Rev Eukaryot Gene Expr 18:207–250.
   PubMed Web of Science ®Google Scholar
• Benson, A.M., Talalay, P., Keen, J.H., Jakoby, W.B. (1977) Relationship between the soluble glutathione-dependent Δ5-3-ketosteroid isomerase and the glutathione S-transferases of the liver. Proc Natl Acad Sci USA 74:158–162.
   PubMed Web of Science ®Google Scholar
• Benson, A.M., Batzinger, R.P., Ou, S.Y., Bueding, E., Cha, Y.N., Talalay, P. (1978) Elevation of hepatic glutathione S-transferase activities and protection against mutagenic metabolites of benzo[a]pyrene by dietary antioxidants. Cancer Res 38:4486–4495.
   PubMed Web of Science ®Google Scholar
• Bloom, D.A., and Jaiswal, A.K. (2003) Phosphorylation of Nrf2 at Ser40 by protein kinase C in response to antioxidants leads to the release of Nrf2 from INrf2, but is not required for Nrf2 stabilization/accumulation in the nucleus and transcriptional activation of antioxidant response element-mediated NAD(P)H:quinone oxidoreductase-1 gene expression. J Biol Chem 278:44675–44682.
   PubMed Web of Science ®Google Scholar
• Board, P.G., Baker, R.T., Chelvanayagam, G., Jermiin, L.S. (1997) Zeta, a novel class of glutathione transferases in a range of species from plants to humans. Biochem J 328:929–935.
   PubMed Web of Science ®Google Scholar
• Board, P.G., Coggan, M., Chelvanayagam, G., Easteal, S., Jermiin, L.S., Schulte, G.K., Danley, D.E., Hoth, L.R., Griffor, M.C., Kamath, A.V., Rosner, M.H., Chrunyk, B.A., Perregaux, D.E., Gabel, C.A., Geoghegan, K.F., Pandit, J. (2000) Identification, characterization, and crystal structure of the Omega class glutathione transferases. J Biol Chem 275:24798–24806.
   PubMed Web of Science ®Google Scholar
• Booth, J., Boyland, E., Sims, P. (1961) An enzyme from rat liver catalysing conjugations with glutathione. Biochem J 79:516–524.
   PubMed Web of Science ®Google Scholar
• Boyland, E., and Chasseaud, L.F. (1969) The role of glutathione and glutathione S-transferases in mercapturic acid biosynthesis. Adv Enzymol Relat Areas Mol Biol 32:173–219.
   PubMedGoogle Scholar
• Branen, A.L. (1975) Toxicology and biochemistry of butylated hydroxyanisole and butylated hydroxytoluene. J Am Oil Chem Soc 52:59–63.
   PubMed Web of Science ®Google Scholar
• Busenlehner, L.S., Alander, J., Jegerscöhld, C., Holm, P.J., Bhakat, P., Hebert, H., Morgenstern, R., Armstrong, R.N. (2007) Location of substrate binding sites within the integral membrane protein microsomal glutathione transferase-1. Biochemistry 46:2812–2822.
   PubMed Web of Science ®Google Scholar
• Chanas, S.A., Jiang, Q., McMahon, M., McWalter, G.K., McLellan, L.I., Elcombe, C.R., Henderson, C.J., Wolf, C.R., Moffat, G.J., Itoh, K., Yamamoto, M., Hayes, J.D. (2002) Loss of the Nrf2 transcription factor causes a marked reduction in constitutive and inducible expression of the glutathione S-transferase Gsta1, Gsta2, Gstm1, Gstm2, Gstm3 and Gstm4 genes in the livers of male and female mice. Biochem J 365:405–416.
   PubMed Web of Science ®Google Scholar
• Chang, C., Smith, D.R., Prasad, V.S., Sidman, C.L., Nebert, D.W., Puga, A. (1993) Ten nucleotide differences, five of which cause amino acid changes, are associated with the Ah receptor locus polymorphism of C57BL/6 and DBA/2 mice. Pharmacogenetics 3:312–321.
   PubMedGoogle Scholar
• Cho, H.Y., Gladwell, W., Wang, X., Chorley, B., Bell, D., Reddy, S.P., Kleeberger, S.R. (2010) Nrf2-regulated PPARγ expression is critical to protection against acute lung injury in mice. Am J Respir Crit Care Med 182:170–182.
   PubMed Web of Science ®Google Scholar
• Clark, A.G., Darby, F.J., Smith, J.N. (1967) Species differences in the inhibition of glutathione S-aryltransferase by phthaleins and dicarboxylic acids. Biochem J 103:49–54.
   PubMed Web of Science ®Google Scholar
• Clark, A.G., Smith, J.N., Speir, T.W. (1973) Cross specificity in some vertebrate and insect glutathione-transferases with methyl parathion (dimethyl p-nitrophenyl phosphorothionate), 1-chloro-2,4-dinitro-benzene and s-crotonyl-N-acetylcysteamine as substrates. Biochem J 135:385–392.
   PubMed Web of Science ®Google Scholar
• Claveau, D., Sirinyan, M., Guay, J., Gordon, R., Chan, C.C., Bureau, Y., Riendeau, D., Mancini, J.A. (2003) Microsomal prostaglandin E synthase-1 is a major terminal synthase that is selectively up-regulated during cyclooxygenase-2-dependent prostaglandin E2 production in the rat adjuvant-induced arthritis model. J Immunol 170:4738–4744.
   PubMed Web of Science ®Google Scholar
• Clifton, G., and Kaplowitz, N. (1978) 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 27:1284–1287.
   PubMed Web of Science ®Google Scholar
• Coggan, M., Whitbread, L., Whittington, A., Board, P. (1998) Structure and organization of the human theta-class glutathione S-transferase and D-dopachrome tautomerase gene complex. Biochem J 334:617–623.
   PubMed Web of Science ®Google Scholar
• Combes, B., and Stakelum, G.S. (1961) A liver enzyme that conjugates sulfobromophthalein sodium with glutathione. J Clin Invest 40:981–988.
   PubMed Web of Science ®Google Scholar
• Darby, F.J., and Grundy, R.K. (1972) Glutathione S-aryltransferase: the effect of treating male and female rats with phenobarbitone on the apparent kinetic parameters for the conjugation of 1,2-dichloro-4-nitrobenzene and 1-chloro-2,4-dinitrobenzene with glutathione. Biochem J 128:175–177.
   PubMed Web of Science ®Google Scholar
• DeJong, J.L., Morgenstern, R., Jörnvall, H., DePierre, J.W., Tu, C.P. (1988) Gene expression of rat and human microsomal glutathione S-transferases. J Biol Chem 263:8430–8436.
   PubMed Web of Science ®Google Scholar
• Díaz-Muñoz, M.D., Osma-García, I.C., Cacheiro-Llaguno, C., Fresno, M., Iñiguez, M.A. (2010) Coordinated up-regulation of cyclooxygenase-2 and microsomal prostaglandin E synthase 1 transcription by nuclear factor κB and early growth response-1 in macrophages. Cell Signal 22:1427–1436.
   PubMed Web of Science ®Google Scholar
• Ding, G.J., Ding, V.D., Rodkey, J.A., Bennett, C.D., Lu, A.Y., Pickett, C.B. (1986) Rat liver glutathione S-transferases. DNA sequence analysis of a Yb2 cDNA clone and regulation of the Yb1 and Yb2 mRNAs by phenobarbital. J Biol Chem 261:7952–7957.
   PubMed Web of Science ®Google Scholar
• Dinkova-Kostova, A.T., Holtzclaw, W.D., Cole, R.N., Itoh, K., Wakabayashi, N., Katoh, Y., Yamamoto, M., Talalay, P. (2002) Direct evidence that sulfhydryl groups of Keap1 are the sensors regulating induction of phase 2 enzymes that protect against carcinogens and oxidants. Proc Natl Acad Sci USA 99:11908–11913.
   PubMed Web of Science ®Google Scholar
• Dinkova-Kostova, A.T., Massiah, M.A., Bozak, R.E., Hicks, R.J., Talalay, P. (2001) Potency of Michael reaction acceptors as inducers of enzymes that protect against carcinogenesis depends on their reactivity with sulfhydryl groups. Proc Natl Acad Sci USA 98:3404–3409.
   PubMed Web of Science ®Google Scholar
• Dinkova-Kostova, A.T., Talalay, P., Sharkey, J., Zhang, Y., Holtzclaw, W.D., Wang, X.J., David, E., Schiavoni, K.H., Finlayson, S., Mierke, D.F., Honda, T. (2010) An exceptionally potent inducer of cytoprotective enzymes: elucidation of the structural features that determine inducer potency and reactivity with Keap1. J Biol Chem 285:33747–33755.
   PubMed Web of Science ®Google Scholar
• Di Simplicio, P., Jensson, H., Mannervik, B. (1989) Effects of inducers of drug metabolism on basic hepatic forms of mouse glutathione transferase. Biochem J 263:679–685.
   PubMed Web of Science ®Google Scholar
• Dixon, D.P., Skipsey, M., Edwards, R. (2010) Roles for glutathione transferases in plant secondary metabolism. Phytochemistry 71:338–350.
   PubMed Web of Science ®Google Scholar
• Dixon, R.A., Diehl, R.E., Opas, E., Rands, E., Vickers, P.J., Evans, J.F., Gillard, J.W., Miller, D.K. (1990) Requirement of a 5-lipoxygenase-activating protein for leukotriene synthesis. Nature 343:282–284.
   PubMed Web of Science ®Google Scholar
• Eggler, A.L., Liu, G., Pezzuto, J.M., van Breemen, R.B., Mesecar, A.D. (2005) Modifying specific cysteines of the electrophile-sensing human Keap1 protein is insufficient to disrupt binding to the Nrf2 domain Neh2. Proc Natl Acad Sci USA 102:10070–10075.
   PubMed Web of Science ®Google Scholar
• Ejiri, N., Katayama, K., Kiyosawa, N., Baba, Y., Doi, K. (2005) Microarray analysis on Phase II drug metabolizing enzymes expression in pregnant rats after treatment with pregnenolone-16α-carbonitrile or phenobarbital. Exp Mol Pathol 79:272–277.
   PubMed Web of Science ®Google Scholar
• Falkner, K.C., Rushmore, T.H., Linder, M.W., Prough, R.A. (1998) Negative regulation of the rat glutathione S-transferase A2 gene by glucocorticoids involves a canonical glucocorticoid consensus sequence. Mol Pharmacol 53:1016–1026.
   PubMed Web of Science ®Google Scholar
• Falkner, K.C., Pinaire, J.A., Xiao, G.H., Geoghegan, T.E., Prough, R.A. (2001) Regulation of the rat glutathione S-transferase A2 gene by glucocorticoids: involvement of both the glucocorticoid and pregnane X receptors. Mol Pharmacol 60:611–619.
   PubMed Web of Science ®Google Scholar
• Favreau, L.V., Pickett, C.B. (1995) The rat quinone reductase antioxidant response element. Identification of the nucleotide sequence required for basal and inducible activity and detection of antioxidant response element-binding proteins in hepatoma and non-hepatoma cell lines. J Biol Chem 270:24468–24474.
   PubMed Web of Science ®Google Scholar
• Frank, C., Gonzalez, M.M., Oinonen, C., Dunlop, T.W., Carlberg, C. (2003) Characterization of DNA complexes formed by the nuclear receptor constitutive androstane receptor. J Biol Chem 278:43299–43310.
   PubMed Web of Science ®Google Scholar
• Frankfurt, O.S., Lipchina, L.P., Bunto, T.V., Emanuél’, N.M. (1967) The effect of 4-methyl-2,6-di-tert.-butylphenol (ionol) on liver tumor induction in rats. Biull Eksp Biol Med (USSR) 64:86–88.
   PubMedGoogle Scholar
• Friling, R.S., Bensimon, A., Tichauer, Y., Daniel, V. (1990) Xenobiotic-inducible expression of murine glutathione S-transferase Ya subunit gene is controlled by an electrophile-responsive element. Proc Natl Acad Sci USA 87:6258–6262.
   PubMed Web of Science ®Google Scholar
• Friling, R.S., Bergelson, S., Daniel, V. (1992) 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 USA 89:668–672.
   PubMed Web of Science ®Google Scholar
• Gong, H., Singh, S.V., Singh, S.P., Mu, Y., Lee, J.H., Saini, S.P., Toma, D., Ren, S., Kagan, V.E., Day, B.W., Zimniak, P., Xie, W. (2006) Orphan nuclear receptor pregnane X receptor sensitizes oxidative stress responses in transgenic mice and cancerous cells. Mol Endocrinol 20:279–290.
   PubMed Web of Science ®Google Scholar
• Goodwin, B., Hodgson, E., Liddle, C. (1999) The orphan human pregnane X receptor mediates the transcriptional activation of CYP3A4 by rifampicin through a distal enhancer module. Mol Pharmacol 56:1329–1339.
   PubMed Web of Science ®Google Scholar
• Grantham, P.H., Weisburger, J.H., Weisburger, E.K. (1973) Effect of the antioxidant butylated hydroxytoluene (BHT) on the metabolism of the carcinogens N-2-fluorenylacetamide and N-hydroxy-N-2-fluorenylacetamide. Food Cosmet Toxicol 11:209–217.
   PubMedGoogle Scholar
• Habig, W.H., Pabst, M.J., Jakoby, W.B. (1974a) Glutathione S-transferases. The first enzymatic step in mercapturic acid formation. J Biol Chem 249:7130–7139.
   PubMed Web of Science ®Google Scholar
• Habig, W.H., Pabst, M.J., Fleischner, G., Gatmaitan, Z., Arias, I.M., Jakoby, W.B. (1974b) The identity of glutathione S-transferase B with ligandin, a major binding protein of liver. Proc Natl Acad Sci USA 71:3879–3882.
   PubMed Web of Science ®Google Scholar
• Habig, W.H., Pabst, M.J., Jakoby, W.B. (1976) Glutathione S-transferase AA from rat liver. Arch Biochem Biophys 175:710–716.
   PubMed Web of Science ®Google Scholar
• Hales, B.F., and Neims, A.H. (1976) Developmental aspects of glutathione S-transferase B (ligandin) in rat liver. Biochem J 160:231–236.
   PubMed Web of Science ®Google Scholar
• Hammock, B.D., and Ota, K. (1983) Differential induction of cytosolic epoxide hydrolase, microsomal epoxide hydrolase, and glutathione S-transferase activities. Toxicol Appl Pharmacol 71:254–265.
   PubMed Web of Science ®Google Scholar
• Han, R., Tsui, S., Smith, T.J. (2002) Up-regulation of prostaglandin E2 synthesis by interleukin-1β in human orbital fibroblasts involves coordinate induction of prostaglandin-endoperoxide H synthase-2 and glutathione-dependent prostaglandin E2 synthase expression. J Biol Chem 277:16355–16364.
   PubMed Web of Science ®Google Scholar
• Hankinson, O. (1995) The aryl hydrocarbon receptor complex. Annu Rev Pharmacol Toxicol 35:307–340.
   PubMed Web of Science ®Google Scholar
• Harris, J.M., Meyer, D.J., Coles, B., Ketterer, B. (1991) A novel glutathione transferase (13-13) isolated from the matrix of rat liver mitochondria having structural similarity to class theta enzymes. Biochem J 278:137–141.
   PubMed Web of Science ®Google Scholar
• Hayes, J.D. (1986) Purification and physical characterization of glutathione S-transferase K. Differential use of S-hexylglutathione and glutathione affinity matrices to isolate a novel glutathione S-transferase from rat liver. Biochem J 233:789–798.
   PubMed Web of Science ®Google Scholar
• Hayes, J.D., and Clarkson, G.H. (1982) Purification and characterization of three forms of glutathione S-transferase A. A comparative study of the major YaYa-, YbYb- and YcYc-containing glutathione S-transferases. Biochem J 207:459–470.
   PubMed Web of Science ®Google Scholar
• Hayes, J.D., and McMahon, M. (2001) Molecular basis for the contribution of the antioxidant response element to cancer chemoprevention. Cancer Lett 174:103–113.
   PubMed Web of Science ®Google Scholar
• Hayes, J.D., and McMahon, M. (2009) NRF2 and KEAP1 mutations: permanent activation of an adaptive response in cancer. Trends Biochem Sci 34:176–188.
   PubMed Web of Science ®Google Scholar
• Hayes, J.D., and Pulford, D.J. (1995) The glutathione S-transferase supergene family: regulation of GST and the contribution of the isoenzymes to cancer chemoprotection and drug resistance. Crit Rev Biochem Mol Biol 30:445–600.
   PubMed Web of Science ®Google Scholar
• Hayes, J.D., Strange, R.C., Percy-Robb, I.W. (1979) Identification of two lithocholic acid-binding proteins. Separation of ligandin from glutathione S-transferase B. Biochem J 181:699–708.
   PubMed Web of Science ®Google Scholar
• Hayes, J.D., Strange, R.C., Percy-Robb, I.W. (1980) Cholic acid binding by glutathione S-transferases from rat liver cytosol. Biochem J 185:83–87.
   PubMed Web of Science ®Google Scholar
• Hayes, J.D., Strange, R.C., Percy-Robb, I.W. (1981) A study of the structures of the YaYa and YaYc glutathione S-transferases from rat liver cytosol. Evidence that the Ya monomer is responsible for lithocholate-binding activity. Biochem J 197:491–502.
   PubMed Web of Science ®Google Scholar
• Hayes, J.D., Judah, D.J., McLellan, L.I., Kerr, L.A., Peacock, S.D., Neal, G.E. (1991a) Ethoxyquin-induced resistance to aflatoxin B1 in the rat is associated with the expression of a novel Alpha-class glutathione S-transferase subunit, Yc2, which possesses high catalytic activity for aflatoxin B1-8,9-epoxide. Biochem J 279:385–398.
   PubMed Web of Science ®Google Scholar
• Hayes, J.D., Judah, D.J., McLellan, L.I., Neal, G.E. (1991b) Contribution of the glutathione S-transferases to the mechanisms of resistance to aflatoxin B1. Pharmacol Ther. 1991;50(3):443–72.
   Google Scholar
• Hayes, J.D., Nguyen, T., Judah, D.J., Petersson, D.G., Neal, G.E. (1994) Cloning of cDNAs from fetal rat liver encoding glutathione S-transferase Yc polypeptides. The Yc2 subunit is expressed in adult rat liver resistant to the hepatocarcinogen aflatoxin B1. J Biol Chem 269:20707–20717.
   PubMed Web of Science ®Google Scholar
• Hayes, J.D., Ellis, E.M., Neal, G.E., Harrison, D.J., Manson, M.M. (1999) Cellular response to cancer chemopreventive agents: contribution of the antioxidant responsive element to the adaptive response to oxidative and chemical stress. Biochem Soc Symp 64:141–168.
   PubMedGoogle Scholar
• Hayes, J.D., Chanas, S.A., Henderson, C.J., McMahon, M., Sun, C., Moffat, G.J., Wolf, C.R., Yamamoto, M. (2000) The Nrf2 transcription factor contributes both to the basal expression of glutathione S-transferases in mouse liver and to their induction by the chemopreventive synthetic antioxidants, butylated hydroxyanisole and ethoxyquin. Biochem Soc Trans 28:33–41.
   PubMed Web of Science ®Google Scholar
• Hayes, J.D., Flanagan, J.U., Jowsey, I.R. (2005) Glutathione transferases. Annu Rev Pharmacol Toxicol 45:51–88.
   PubMed Web of Science ®Google Scholar
• Hayes, J.D., McMahon, M., Chowdhry, S., Dinkova-Kostova, A.T. (2010) Cancer chemoprevention mechanisms mediated through the Keap1-Nrf2 pathway. Antioxid Redox Signal 13:1713–1748.
   PubMed Web of Science ®Google Scholar
• Higgins, L.G., Cavin, C., Itoh, K., Yamamoto, M., Hayes, J.D. (2008) Induction of cancer chemopreventive enzymes by coffee is mediated by transcription factor Nrf2. Evidence that the coffee-specific diterpenes cafestol and kahweol confer protection against acrolein. Toxicol Appl Pharmacol 226:328–337.
   PubMed Web of Science ®Google Scholar
• Higgins, L.G., Kelleher, M.O., Eggleston, I.M., Itoh, K., Yamamoto, M., Hayes, J.D. (2009) Transcription factor Nrf2 mediates an adaptive response to sulforaphane that protects fibroblasts in vitro against the cytotoxic effects of electrophiles, peroxides and redox-cycling agents. Toxicol Appl Pharmacol 237:267–280.
   PubMed Web of Science ®Google Scholar
• Honkakoski, P., and Negishi, M. (1997) Characterization of a phenobarbital-responsive enhancer module in mouse P450 Cyp2b10 gene. J Biol Chem 272:14943–14949.
   PubMed Web of Science ®Google Scholar
• Honkakoski, P., Zelko, I., Sueyoshi, T., Negishi, M. (1998) The nuclear orphan receptor CAR-retinoid X receptor heterodimer activates the phenobarbital-responsive enhancer module of the CYP2B gene. Mol Cell Biol 18:5652–5658.
   PubMed Web of Science ®Google Scholar
• Hsieh, F.H., Lam, B.K., Penrose, J.F., Austen, K.F., Boyce, J.A. (2001) T helper cell type 2 cytokines coordinately regulate immunoglobulin E-dependent cysteinyl leukotriene production by human cord blood-derived mast cells: profound induction of leukotriene C4 synthase expression by interleukin 4. J Exp Med 193:123–133.
   PubMed Web of Science ®Google Scholar
• Huang, H.C., Nguyen, T., Pickett, C.B. (2000) Regulation of the antioxidant response element by protein kinase C-mediated phosphorylation of NF-E2-related factor 2. Proc Natl Acad Sci USA 97:12475–12480.
   PubMed Web of Science ®Google Scholar
• Huang, H.C., Nguyen, T., Pickett, C.B. (2002) Phosphorylation of Nrf2 at Ser-40 by protein kinase C regulates antioxidant response element-mediated transcription. J Biol Chem 277:42769–42774.
   PubMed Web of Science ®Google Scholar
• Hussey, A.J., and Hayes, J.D. (1992) Characterization of a human class-Theta glutathione S-transferase with activity towards 1-menaphthyl sulphate. Biochem J 286:929–935.
   PubMed Web of Science ®Google Scholar
• Ikeda, H., Omoteyama, K., Yoshida, K., Nishi, S., Sakai, M. (2006) CCAAT enhancer-binding protein alpha suppresses the rat placental glutathione S-transferase gene in normal liver. J Biol Chem 281:6734–6741.
   PubMed Web of Science ®Google Scholar
• Jakobsson, P.J., Mancini, J.A., Ford-Hutchinson, A.W. (1996) Identification and characterization of a novel human microsomal glutathione S-transferase with leukotriene C4 synthase activity and significant sequence identity to 5-lipoxygenase-activating protein and leukotriene C4 synthase. J Biol Chem 271:22203–22210.
   PubMed Web of Science ®Google Scholar
• Jakobsson, P.J., Mancini, J.A., Riendeau, D., Ford-Hutchinson, A.W. (1997) Identification and characterization of a novel microsomal enzyme with glutathione-dependent transferase and peroxidase activities. J Biol Chem 272:22934–22939.
   PubMed Web of Science ®Google Scholar
• Jakobsson, P.J., Morgenstern, R., Mancini, J., Ford-Hutchinson, A., Persson, B. (2000) Membrane-associated proteins in eicosanoid and glutathione metabolism (MAPEG). A widespread protein superfamily. Am J Respir Crit Care Med 161:S20–S24.
   PubMed Web of Science ®Google Scholar
• Jakobsson, P.J., Thorén, S., Morgenstern, R., Samuelsson, B. (1999) Identification of human prostaglandin E synthase: a microsomal, glutathione-dependent, inducible enzyme, constituting a potential novel drug target. Proc Natl Acad Sci USA 96:7220–7225.
   PubMed Web of Science ®Google Scholar
• Jakoby, W.B., Ketterer, B., Mannervik, B. (1984) Glutathione transferases: nomenclature. Biochem Pharmacol 33:2539–2540.
   PubMed Web of Science ®Google Scholar
• Jegerschöld, C., Pawelzik, S.C., Purhonen, P., Bhakat, P., Gheorghe, K.R., Gyobu, N., Mitsuoka, K., Morgenstern, R., Jakobsson, P.J., Hebert, H. (2008) Structural basis for induced formation of the inflammatory mediator prostaglandin E2. Proc Natl Acad Sci USA 105:11110–11115.
   PubMed Web of Science ®Google Scholar
• Ji, X., Johnson, W.W., Sesay, M.A., Dickert, L., Prasad, S.M., Ammon, H.L., Armstrong, R.N., Gilliland, G.L. (1994) Structure and function of the xenobiotic substrate binding site of a glutathione S-transferase as revealed by X-ray crystallographic analysis of product complexes with the diastereomers of 9-(S-glutathionyl)-10-hydroxy-9,10-dihydrophenanthrene. Biochemistry 33:1043–1052.
   PubMed Web of Science ®Google Scholar
• Jowsey, I.R., Jiang, Q., Itoh, K., Yamamoto, M., Hayes, J.D. (2003) Expression of the aflatoxin B1-8,9-epoxide-metabolizing murine glutathione S-transferase A3 subunit is regulated by the Nrf2 transcription factor through an antioxidant response element. Mol Pharmacol 64:1018–1028.
   PubMed Web of Science ®Google Scholar
• Jowsey, I.R., Thomson, R.E., Orton, T.C., Elcombe, C.R., Hayes, J.D. (2003) Biochemical and genetic characterization of a murine class Kappa glutathione S-transferase. Biochem J 373:559–569.
   PubMed Web of Science ®Google Scholar
• Kang, K.W., Cho, I.J., Lee, C.H., Kim, S.G. (2003) Essential role of phosphatidylinositol 3-kinase-dependent CCAAT/enhancer binding protein β activation in the induction of glutathione S-transferase by oltipraz. J Natl Cancer Inst 95:53–66.
   PubMed Web of Science ®Google Scholar
• Kaplowitz, N., Kuhlekamp, J., Clifton, G. (1975) Drug induction of hepatic glutathione S-transferases in male and female rats. Biochem J 146:351–356.
   PubMed Web of Science ®Google Scholar
• Kaplowitz, N., Percy-Robb, I.W., Javitt, N.B. (1973) Role of hepatic anion-binding protein in bromsulphthalein conjugation. J Exp Med 138:483–487.
   PubMed Web of Science ®Google Scholar
• Katsuoka, F., Motohashi, H., Engel, J.D., Yamamoto, M. (2005) Nrf2 transcriptionally activates the mafG gene through an antioxidant response element. J Biol Chem 280:4483–4490.
   PubMed Web of Science ®Google Scholar
• Keen, J.H., and Jakoby, W.B. (1978) Glutathione transferases. Catalysis of nucleophilic reactions of glutathione. J Biol Chem 253:5654–5657.
   PubMed Web of Science ®Google Scholar
• Keen, J.H., Habig, W.H., Jakoby, W.B. (1976) Mechanism for the several activities of the glutathione S-transferases. J Biol Chem 251:6183–6188.
   PubMed Web of Science ®Google Scholar
• Kelly, V.P., Ellis, E.M., Manson, M.M., Chanas, S.A., Moffat, G.J., McLeod, R., Judah, D.J., Neal, G.E., Hayes, J.D. (2000) Chemoprevention of aflatoxin B1 hepatocarcinogenesis by coumarin, a natural benzopyrone that is a potent inducer of aflatoxin B1-aldehyde reductase, the glutathione S-transferase A5 and P1 subunits, and NAD(P)H:quinone oxidoreductase in rat liver. Cancer Res 60:957–969.
   PubMed Web of Science ®Google Scholar
• Kensler, T.W., and Wakabayashi, N. (2010) Nrf2: friend or foe for chemoprevention? Carcinogenesis 31:90–99.
   PubMed Web of Science ®Google Scholar
• Kensler, T.W., Egner, P.A., Dolan, P.M., Groopman, J.D., Roebuck, B.D. (1987) 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 47:4271–4277.
   PubMed Web of Science ®Google Scholar
• Kensler, T.W., Wakabayashi, N., Biswal, S. (2007) Cell survival responses to environmental stresses via the Keap1-Nrf2-ARE pathway. Annu Rev Pharmacol Toxicol 47:89–116.
   PubMed Web of Science ®Google Scholar
• Ketterer, B., Ross-Mansell, P., Whitehead, J.K. (1967) The isolation of carcinogen-binding protein from livers of rats given 4-dimethylaminoazobenzene. Biochem J 103:316–324.
   PubMed Web of Science ®Google Scholar
• Kelner, M.J., Bagnell, R.D., Montoya, M.A., Estes, L.A., Forsberg, L., Morgenstern, R. (2000) Structural organization of the microsomal glutathione S-transferase gene (MGST1) on chromosome 12p13.1-13.2. Identification of the correct promoter region and demonstration of transcriptional regulation in response to oxidative stress. J Biol Chem 275:13000–13006.
   PubMed Web of Science ®Google Scholar
• Kelner, M.J., Bagnell, R.D., Morgenstern, R. (2004) Structural organization of the murine microsomal glutathione S-transferase gene (MGST1) from the 129/SvJ strain: identification of the promoter region and a comprehensive examination of tissue expression. Biochim Biophys Acta 1678:163–169.
   PubMed Web of Science ®Google Scholar
• Klaassen, C.D., and Plaa, G.L. (1968) Studies on the mechanism of phenobarbital-enhanced sulfobromophthalein disappearance. J Pharmacol Exp Ther 161:361–366.
   PubMed Web of Science ®Google Scholar
• Ladner, J.E., Parsons, J.F., Rife, C.L., Gilliland, G.L., Armstrong, R.N. (2004) Parallel evolutionary pathways for glutathione transferases: structure and mechanism of the mitochondrial class kappa enzyme rGSTK1-1. Biochemistry 43:352–361.
   PubMed Web of Science ®Google Scholar
• Kluth, D., Banning, A., Paur, I., Blomhoff, R., Brigelius-Flohé, R. (2007) Modulation of pregnane X receptor- and electrophile responsive element-mediated gene expression by dietary polyphenolic compounds. Free Radic Biol Med 42:315–325.
   PubMed Web of Science ®Google Scholar
• Ki, S.H., Cho, I.J., Choi, D.W., Kim, S.G. (2005) Glucocorticoid receptor (GR)-associated SMRT binding to C/EBPβ TAD and Nrf2 Neh4/5: role of SMRT recruited to GR in GSTA2 gene repression. Mol Cell Biol 25:4150–4165.
   PubMed Web of Science ®Google Scholar
• Kobayashi, K., Sueyoshi, T., Inoue, K., Moore, R., Negishi, M. (2003) Cytoplasmic accumulation of the nuclear receptor CAR by a tetratricopeptide repeat protein in HepG2 cells. Mol Pharmacol 64:1069–1075.
   PubMed Web of Science ®Google Scholar
• Kobayashi, M., Itoh, K., Suzuki, T., Osanai, H., Nishikawa, K., Katoh, Y., Takagi, Y., Yamamoto, M. (2002) Identification of the interactive interface and phylogenic conservation of the Nrf2-Keap1 system. Genes Cells 7:807–820.
   PubMed Web of Science ®Google Scholar
• Kwak, M.K., Wakabayashi, N., Itoh, K., Motohashi, H., Yamamoto, M., Kensler, T.W. (2003) Modulation of gene expression by cancer chemopreventive dithiolethiones through the Keap1-Nrf2 pathway. Identification of novel gene clusters for cell survival. J Biol Chem 278:8135–8145.
   PubMed Web of Science ®Google Scholar
• Lai, H.C., Li, N., Weiss, M.J., Reddy, C.C., Tu, C.P. (1984) The nucleotide sequence of a rat liver glutathione S-transferase subunit cDNA clone. J Biol Chem 259:5536–5542.
   PubMed Web of Science ®Google Scholar
• Lai, H.C., Qian, B., Grove, G., Tu, C.P. (1988) Gene expression of rat glutathione S-transferases. Evidence for gene conversion in the evolution of the Yb multigene family. J Biol Chem 263:11389–11395.
   PubMed Web of Science ®Google Scholar
• Lam, B.K., Penrose, J.F., Freeman, G.J., Austen, K.F. (1994) Expression cloning of a cDNA for human leukotriene C4 synthase, an integral membrane protein conjugating reduced glutathione to leukotriene A4. Proc Natl Acad Sci USA 91:7663–7667.
   PubMed Web of Science ®Google Scholar
• Lawrence, R.A., and Burk, R.F. (1976) Glutathione peroxidase activity in selenium-deficient rat liver. Biochem Biophys Res Commun 71:952–958.
   PubMed Web of Science ®Google Scholar
• Lempiäinen, H., Müller, A., Brasa, S., Teo, S.S., Roloff, T.C., Morawiec, L., Zamurovic, N., Vicart, A., Funhoff, E., Couttet, P., Schübeler, D., Grenet, O., Marlowe, J., Moggs, J., Terranova, R. (2011) Phenobarbital mediates an epigenetic switch at the constitutive androstane receptor (CAR) target gene Cyp2b10 in the liver of B6C3F1 mice. PloS ONE 6(3):e18216. doi:10.1371/journal.pone.0018216.
   PubMedGoogle Scholar
• Levi, A.J., Gatmaitan, Z., Arias, I.M. (1969) Two hepatic cytoplasmic protein fractions, Y and Z, and their possible role in the hepatic uptake of bilirubin, sulfobromophthalein, and other anions. J Clin Invest 48:2156–2167.
   PubMed Web of Science ®Google Scholar
• Litwack, G., Ketterer, B., Arias, I.M. (1971) Ligandin: a hepatic protein which binds steroids, bilirubin, carcinogens and a number of exogenous organic anions. Nature 234:466–467.
   PubMed Web of Science ®Google Scholar
• Liu, M., Zhou, L., Xu, A., Lam, K.S., Wetzel, M.D., Xiang, R., Zhang, J., Xin, X., Dong, L.Q., Liu, F. (2008) A disulfide-bond A oxidoreductase-like protein (DsbA-L) regulates adiponectin multimerization. Proc Natl Acad Sci USA 105:18302–18307.
   PubMed Web of Science ®Google Scholar
• Liu, S., Zhang, P., Ji, X., Johnson, W.W., Gilliland, G.L., Armstrong, R.N. (1992) Contribution of tyrosine 6 to the catalytic mechanism of isoenzyme 3-3 of glutathione S-transferase. J Biol Chem 267:4296–4299.
   PubMed Web of Science ®Google Scholar
• Ma, K.F., Yang, H.Y., Chen, Z., Qi, L.Y., Zhu, D.Y., Lou, Y.J. (2008) Enhanced expressions and activations of leukotriene C4 synthesis enzymes in D-galactosamine/lipopolysaccharide-induced rat fulminant hepatic failure model. World J Gastroenterol 14:2748–2756.
   PubMed Web of Science ®Google Scholar
• Ma, Q., Kinneer, K., Bi, Y., Chan, J.Y., Kan, Y.W. (2004) Induction of murine NAD(P)H:quinone oxidoreductase by 2,3,7,8-tetrachlorodibenzo-p-dioxin requires the CNC (cap ‘n’ collar) basic leucine zipper transcription factor Nrf2 (nuclear factor erythroid 2-related factor 2): cross-interaction between AhR (aryl hydrocarbon receptor) and Nrf2 signal transduction. Biochem J 377:205–213.
   PubMed Web of Science ®Google Scholar
• Maglich, J.M., Stoltz, C.M., Goodwin, B., Hawkins-Brown, D., Moore, J.T., Kliewer, S.A. (2002) Nuclear pregnane x receptor and constitutive androstane receptor regulate overlapping but distinct sets of genes involved in xenobiotic detoxification. Mol Pharmacol 62:638–646.
   PubMed Web of Science ®Google Scholar
• Mahéo, K., Morel, F., Langouët, S., Kramer, H., Le Ferrec, E., Ketterer, B., Guillouzo, A. (1997) Inhibition of cytochromes P-450 and induction of glutathione S-transferases by sulforaphane in primary human and rat hepatocytes. Cancer Res 57:3649–3652.
   PubMed Web of Science ®Google Scholar
• Mancini, J.A., Blood, K., Guay, J., Gordon, R., Claveau, D., Chan, C.C., Riendeau, D. (2001) Cloning, expression, and up-regulation of inducible rat prostaglandin E synthase during lipopolysaccharide-induced pyresis and adjuvant-induced arthritis. J Biol Chem 276:4469–4475.
   PubMed Web of Science ®Google Scholar
• Mannervik, B., and Danielson, U.H. (1988) Glutathione transferases–structure and catalytic activity. CRC Crit Rev Biochem 23:283–337.
   PubMed Web of Science ®Google Scholar
• Mannervik, B., and Jensson, H. (1982) Binary combinations of four protein subunits with different catalytic specificities explain the relationship between six basic glutathione S-transferases in rat liver cytosol. J Biol Chem 257:9909–9912.
   PubMed Web of Science ®Google Scholar
• Mannervik, B., Board, P.G., Hayes, J.D., Listowsky, I., Pearson, W.R. (2005) Nomenclature for mammalian soluble glutathione transferases. Methods Enzymol 401:1–8.
   PubMed Web of Science ®Google Scholar
• Martinez Molina, D., Eshaghi, S., Nordlund, P. (2008) Catalysis within the lipid bilayer-structure and mechanism of the MAPEG family of integral membrane proteins. Curr Opin Struct Biol 18:442–449.
   PubMed Web of Science ®Google Scholar
• Martinez Molina, D., Wetterholm, A., Kohl, A., McCarthy, A.A., Niegowski, D., Ohlson, E., Hammarberg, T., Eshaghi, S., Haeggström, J.Z., Nordlund, P. (2007) Structural basis for synthesis of inflammatory mediators by human leukotriene C4 synthase. Nature 448:613–616.
   PubMed Web of Science ®Google Scholar
• McLellan, L.I., and Hayes, J.D. (1989) Differential induction of class Alpha glutathione S-transferases in mouse liver by the anticarcinogenic antioxidant butylated hydroxyanisole. Purification and characterization of glutathione S-transferase Ya1Ya1. Biochem J 263:393–402.
   PubMed Web of Science ®Google Scholar
• McLellan, L.I., Wolf, C.R., Hayes, J.D. (1989) Human microsomal glutathione S-transferase. Its involvement in the conjugation of hexachlorobuta-1,3-diene with glutathione. Biochem J 258:87–93.
   PubMed Web of Science ®Google Scholar
• McLellan, L.I., Kerr, L.A., Cronshaw, A.D., Hayes, J.D. (1991) Regulation of mouse glutathione S-transferases by chemoprotectors. Molecular evidence for the existence of three distinct Alpha-class glutathione S-transferase subunits, Ya1, Ya2, and Ya3, in mouse liver. Biochem J 276:461–469
   PubMed Web of Science ®Google Scholar
• McMahon, M., Itoh, K., Yamamoto, M., Chanas, S.A., Henderson, C.J., McLellan, L.I., Wolf, C.R., Cavin, C., Hayes, J.D. (2001) The Cap’n’Collar basic leucine zipper transcription factor Nrf2 (NF-E2 p45-related factor 2) controls both constitutive and inducible expression of intestinal detoxification and glutathione biosynthetic enzymes. Cancer Res 61:3299–3307.
   PubMed Web of Science ®Google Scholar
• McMahon, M., Itoh, K., Yamamoto, M., Hayes, J.D. (2003) Keap1-dependent proteasomal degradation of transcription factor Nrf2 contributes to the negative regulation of antioxidant response element-driven gene expression. J Biol Chem 278:21592–21600.
   PubMed Web of Science ®Google Scholar
• McMahon, M., Thomas, N., Itoh, K., Yamamoto, M., Hayes, J.D. (2004) Redox-regulated turnover of Nrf2 is determined by at least two separate protein domains, the redox-sensitive Neh2 degron and the redox-insensitive Neh6 degron. J Biol Chem 279:31556–31567.
   PubMed Web of Science ®Google Scholar
• McMahon, M., Thomas, N., Itoh, K., Yamamoto, M., Hayes, J.D. (2006) Dimerization of substrate adaptors can facilitate cullin-mediated ubiquitylation of proteins by a “tethering” mechanism: a two-site interaction model for the Nrf2-Keap1 complex. J Biol Chem 281:24756–24768.
   PubMed Web of Science ®Google Scholar
• McMahon, M., Lamont, D.J., Beattie, K.A., Hayes, J.D. (2010) Keap1 perceives stress via three sensors for the endogenous signaling molecules nitric oxide, zinc, and alkenals. Proc Natl Acad Sci USA 107:18838–18843.
   PubMed Web of Science ®Google Scholar
• McWalter, G.K., Higgins, L.G., McLellan, L.I., Henderson, C.J., Song, L., Thornalley, P.J., Itoh, K., Yamamoto, M., Hayes, J.D. (2004) Transcription factor Nrf2 is essential for induction of NAD(P)H:quinone oxidoreductase 1, glutathione S-transferases, and glutamate cysteine ligase by broccoli seeds and isothiocyanates. J Nutr 134:3499S–3506S.
   PubMed Web of Science ®Google Scholar
• Miao, W., Hu, L., Scrivens, P.J., Batist, G. (2005) Transcriptional regulation of NF-E2 p45-related factor (NRF2) expression by the aryl hydrocarbon receptor-xenobiotic response element signaling pathway: direct cross-talk between phase I and II drug-metabolizing enzymes. J Biol Chem 280:20340–20348.
   PubMed Web of Science ®Google Scholar
• Miller, D.K., Gillard, J.W., Vickers, P.J., Sadowski, S., Léveillé, C., Mancini, J.A., Charleson, P., Dixon, R.A., Ford-Hutchinson, A.W., Fortin, R., et al. (1990) Identification and isolation of a membrane protein necessary for leukotriene production. Nature 343:278–281.
   PubMed Web of Science ®Google Scholar
• Moch, R.W. (1986) Pathology of BHA- and BHT-induced lesions. Food Chem Toxicol 24:1167–1169.
   PubMed Web of Science ®Google Scholar
• Moore, L.B., Parks, D.J., Jones, S.A., Bledsoe, R.K., Consler, T.G., Stimmel, J.B., Goodwin, B., Liddle, C., Blanchard, S.G., Willson, T.M., Collins, J.L., Kliewer, S.A. (2000) Orphan nuclear receptors constitutive androstane receptor and pregnane X receptor share xenobiotic and steroid ligands. J Biol Chem 275:15122–15127.
   PubMed Web of Science ®Google Scholar
• Morel, F., Fardel, O., Meyer, D.J., Langouet, S., Gilmore, K.S., Meunier, B., Tu, C.P., Kensler, T.W., Ketterer, B., Guillouzo, A. (1993) Preferential increase of glutathione S-transferase class Alpha transcripts in cultured human hepatocytes by phenobarbital, 3-methylcholanthrene, and dithiolethiones. Cancer Res 53:231–234.
   PubMed Web of Science ®Google Scholar
• Morel, F., Rauch, C., Petit, E., Piton, A., Theret, N., Coles, B., Guillouzo, A. (2004) Gene and protein characterization of the human glutathione S-transferase Kappa and evidence for a peroxisomal localization. J Biol Chem 279:16246–16253.
   PubMed Web of Science ®Google Scholar
• Morey, K.S., and Litwack, G. (1969) Isolation and properties of cortisol metabolite binding proteins of rat liver cytosol. Biochemistry 8:4813–4821.
   PubMed Web of Science ®Google Scholar
• Morgenstern, R., DePierre, J.W., Ernster, L. (1979) Activation of microsomal glutathione S-transferase activity by sulfhydryl reagents. Biochem Biophys Res Commun 87:657–663.
   PubMed Web of Science ®Google Scholar
• Morgenstern, R., Guthenberg, C., Depierre, J.W. (1982) Microsomal glutathione S-transferase. Purification, initial characterization and demonstration that it is not identical to the cytosolic glutathione S-transferases A, B and C. Eur J Biochem 128:243–248.
   PubMedGoogle Scholar
• Morgenstern, R., and DePierre, J.W. (1983) Microsomal glutathione transferase. Purification in unactivated form and further characterization of the activation process, substrate specificity and amino acid composition. Eur J Biochem 134:591–597.
   PubMedGoogle Scholar
• Motohashi, H., O’Connor, T., Katsuoka, F., Engel, J.D., Yamamoto, M. (2002) Integration and diversity of the regulatory network composed of Maf and CNC families of transcription factors. Gene 294:1–12.
   PubMed Web of Science ®Google Scholar
• Mukhtar, H., and Bresnick, E. (1976a) Effects of phenobarbital and 3-methylcholanthrene administration on glutathione S-epoxide transferase activity in rat liver. Biochem Pharmacol 25:1081–1084.
   PubMed Web of Science ®Google Scholar
• Mukhtar, H., and Bresnick, E. (1976b) Mouse liver and lung glutathione S-epoxide transferase: effects of phenobarbital and 3-methylcholanthrene administration. Chem Biol Interact 15:59–67.
   PubMed Web of Science ®Google Scholar
• Mutoh, S., Osabe, M., Inoue, K., Moore, R., Pedersen, L., Perera, L., Rebolloso, Y., Sueyoshi, T., Negishi, M. (2009) Dephosphorylation of threonine 38 is required for nuclear translocation and activation of human xenobiotic receptor CAR (NR1I3). J Biol Chem 284:34785–34792.
   PubMed Web of Science ®Google Scholar
• Nicholson, D.W., Ali, A., Vaillancourt, J.P., Calaycay, J.R., Mumford, R.A., Zamboni, R.J., Ford-Hutchinson, A.W. (1993) Purification to homogeneity and the N-terminal sequence of human leukotriene C4 synthase: a homodimeric glutathione S-transferase composed of 18-kDa subunits. Proc Natl Acad Sci USA 90:2015–2019.
   PubMed Web of Science ®Google Scholar
• Nims, R.W., Sinclair, P.R., Sinclair, J.F., Dragnev, K.H., Jones, C.R., Mellini, D.W., Thomas, P.E., Lubet, R.A. (1993) Dose-response relationships for the induction of P450 2B by 1,4-bis[2-(3,5-dichloropyridyloxy)]benzne (TCPOBOP) in rat and cultured rat hepatocytes. Xenobiotica 23:1411–1426.
   PubMed Web of Science ®Google Scholar
• Nioi, P., McMahon, M., Itoh, K., Yamamoto, M., Hayes, J.D. (2003) Identification of a novel Nrf2-regulated antioxidant response element (ARE) in the mouse NAD(P)H:quinone oxidoreductase 1 gene: reassessment of the ARE consensus sequence. Biochem J 374:337–348.
   PubMed Web of Science ®Google Scholar
• Ogura, K., Nishiyama, T., Okada, T., Kajital, J., Narihata, H., Watabe, T., Hiratsuka, A., Watabe, T. (1991) Molecular cloning and amino acid sequencing of rat liver class theta glutathione S-transferase Yrs-Yrs inactivating reactive sulfate esters of carcinogenic arylmethanols. Biochem Biophys Res Commun 181:1294–1300.
   PubMed Web of Science ®Google Scholar
• Ohta, K., Ohigashi, M., Naganawa, A., Ikeda, H., Sakai, M., Nishikawa, J., Imagawa, M., Osada, S., Nishihara, T. (2007) Histone acetyltransferase MOZ acts as a co-activator of Nrf2-MafK and induces tumour marker gene expression during hepatocarcinogenesis. Biochem J 402:559–566.
   PubMed Web of Science ®Google Scholar
• Ohtake, F., Baba, A., Takada, I., Okada, M., Iwasaki, K., Miki, H., Takahashi, S., Kouzmenko, A., Nohara, K., Chiba, T., Fujii-Kuriyama, Y., Kato, S. (2007) Dioxin receptor is a ligand-dependent E3 ubiquitin ligase. Nature 446:562–566.
   PubMed Web of Science ®Google Scholar
• Okawa, H., Motohashi, H., Kobayashi, A., Aburatani, H., Kensler, T.W., Yamamoto, M. (2006) Hepatocyte-specific deletion of the Keap1 gene activates Nrf2 and confers potent resistance against acute drug toxicity. Biochem Biophys Res Commun 339:79–88.
   PubMed Web of Science ®Google Scholar
• Okey, A.B., Riddick, D.S., Harper, P.A. (1994) Molecular biology of the aromatic hydrocarbon (dioxin) receptor. Trends Pharmacol Sci 15:226–232.
   PubMed Web of Science ®Google Scholar
• Okuda, A., Sakai, M., Muramatsu, M. (1987) The structure of the rat glutathione S-transferase P gene and related pseudogenes. J Biol Chem 262:3858–3863.
   PubMed Web of Science ®Google Scholar
• Okuda, A., Imagawa, M., Sakai, M., Muramatsu, M. (1990) Functional cooperativity between two TPA responsive elements in undifferentiated F9 embryonic stem cells. EMBO J 9:1131–1135.
   PubMed Web of Science ®Google Scholar
• Park, E.Y., Cho, I.J., Kim, S.G. (2004) Transactivation of the PPAR-responsive enhancer module in chemopreventive glutathione S-transferase gene by the peroxisome proliferator-activated receptor-gamma and retinoid X receptor heterodimer. Cancer Res 64:3701–3713.
   PubMed Web of Science ®Google Scholar
• Park, Y., Li, H., Kemper, B. (1996) Phenobarbital induction mediated by a distal CYP2B2 sequence in rat liver transiently transfected in situ. J Biol Chem 271:23725–23728.
   PubMed Web of Science ®Google Scholar
• Pawelzik, S.C., Uda, N.R., Spahiu, L., Jegerschöld, C., Stenberg, P., Hebert, H., Morgenstern, R., Jakobsson, P.J. (2010) Identification of key residues determining species differences in inhibitor binding of microsomal prostaglandin E synthase-1. J Biol Chem 285:29254–29261.
   PubMed Web of Science ®Google Scholar
• Pearson, W.R., Windle, J.J., Morrow, J.F., Benson, A.M., Talalay, P. (1983) Increased synthesis of glutathione S-transferases in response to anticarcinogenic antioxidants. Cloning and measurement of messenger RNA. J Biol Chem 258:2052–2062.
   PubMed Web of Science ®Google Scholar
• Pearson, W.R., Reinhart, J., Sisk, S.C., Anderson, K.S., Adler, P.N. (1988) Tissue-specific induction of murine glutathione transferase mRNAs by butylated hydroxyanisole. J Biol Chem 263:13324–13332.
   PubMed Web of Science ®Google Scholar
• Pemble, S., Schroeder, K.R., Spencer, S.R., Meyer, D.J., Hallier, E., Bolt, H.M., Ketterer, B., Taylor, J.B. (1994) Human glutathione S-transferase theta (GSTT1): cDNA cloning and the characterization of a genetic polymorphism. Biochem J 300:271–276.
   PubMed Web of Science ®Google Scholar
• Pemble, S.E., Wardle, A.F., Taylor, J.B. (1996) Glutathione S-transferase class Kappa: characterization by the cloning of rat mitochondrial GST and identification of a human homologue. Biochem J 319:749–754.
   PubMed Web of Science ®Google Scholar
• Pickett, C.B., Donohue, A.M., Lu, A.Y., Hales, B.F. (1982) Rat liver glutathione S-transferase B: the functional mRNAs specific for the Ya Yc subunits are induced differentially by phenobarbital. Arch Biochem Biophys 215:539–543.
   PubMed Web of Science ®Google Scholar
• Pickett, C.B., Telakowski-Hopkins, C.A., Ding, G.J., Argenbright, L., Lu, A.Y. (1984) Rat liver glutathione S-transferases. Complete nucleotide sequence of a glutathione S-transferase mRNA and the regulation of the Ya, Yb, and Yc mRNAs by 3-methylcholanthrene and phenobarbital. J Biol Chem 259:5182–5188.
   PubMed Web of Science ®Google Scholar
• Pimental, R.A., Liang, B., Yee, G.K., Wilhelmsson, A., Poellinger, L., Paulson, K.E. (1993) Dioxin receptor and C/EBP regulate the function of the glutathione S-transferase Ya gene xenobiotic response element. Mol Cell Biol 13:4365–4373.
   PubMed Web of Science ®Google Scholar
• Poland, A., Mak, I., Glover, E., Boatman, R.J., Ebetino, F.H., Kende, A.S. (1980) 1,4-Bis[2-(3,5-dichloropyridyloxy)]benzene, a potent phenobarbital-like inducer of microsomal monooxygenase activity. Mol Pharmacol 18:571–580.
   PubMed Web of Science ®Google Scholar
• Prochaska, H.J., and Talalay, P. (1988) Regulatory mechanisms of monofunctional and bifunctional anticarcinogenic enzyme inducers in murine liver. Cancer Res 48:4776–4782.
   PubMed Web of Science ®Google Scholar
• Pugazhenthi, S., Akhov, L., Selvaraj, G., Wang, M., Alam, J. (2007) Regulation of heme oxygenase-1 expression by demethoxy curcuminoids through Nrf2 by a PI3-kinase/Akt-mediated pathway in mouse beta-cells. Am J Physiol Endocrinol Metab 293:E645–655.
   PubMed Web of Science ®Google Scholar
• Pulford, D.J., and Hayes, J.D. (1996) Characterization of the rat glutathione S-transferase Yc2 subunit gene, GSTA5: identification of a putative antioxidant-responsive element in the 5′-flanking region of rat GSTA5 that may mediate chemoprotection against aflatoxin B1. Biochem J 318:75–84.
   PubMed Web of Science ®Google Scholar
• Rada, P., Rojo, A.I., Chowdhry, S., McMahon, M., Hayes, J.D., Cuadrado, A. (2011) SCF/beta-TrCP promotes glycogen synthase kinase 3-dependent degradation of the Nrf2 transcription factor in a Keap1-independent manner. Mol Cell Biol. 31:1121–1133.
   PubMedGoogle Scholar
• Ramos-Gomez, M., Kwak, M.K., Dolan, P.M., Itoh, K., Yamamoto, M., Talalay, P., Kensler, T.W. (2001) Sensitivity to carcinogenesis is increased and chemoprotective efficacy of enzyme inducers is lost in nrf2 transcription factor-deficient mice. Proc Natl Acad Sci USA 98:3410–3415.
   PubMed Web of Science ®Google Scholar
• Reddy, K.V., Serio, K.J., Hodulik, C.R., Bigby, T.D. (2003) 5-lipoxygenase-activating protein gene expression. Key role of CCAAT/enhancer-binding proteins (C/EBP) in constitutive and tumor necrosis factor (TNF) α-induced expression in THP-1 cells. J Biol Chem 278:13810–13818.
   PubMed Web of Science ®Google Scholar
• Reinemer, P., Dirr, H.W., Ladenstein, R., Schäffer, J., Gallay, O., Huber, R. (1991) The three-dimensional structure of class pi glutathione S-transferase in complex with glutathione sulfonate at 2.3 Å resolution. EMBO J 10:1997–2005.
   PubMed Web of Science ®Google Scholar
• Reyes, H., Levi, A.J., Gatmaitan, Z., Arias, I.M. (1969) Organic anion-binding protein in rat liver: drug induction and its physiologic consequence. Proc Natl Acad Sci USA 64:168–170.
   PubMed Web of Science ®Google Scholar
• Reyes, H., Levi, A.J., Gatmaitan, Z., Arias, I.M. (1971) Studies of Y and Z, two hepatic cytoplasmic organic anion-binding proteins: effect of drugs, chemicals, hormones, and cholestasis. J Clin Invest 50:2242–2252.
   PubMed Web of Science ®Google Scholar
• Riddick, C.A., Serio, K.J., Hodulik, C.R., Ring, W.L., Regan, M.S., Bigby, T.D. (1999) TGF-β increases leukotriene C4 synthase expression in the monocyte-like cell line, THP-1. J Immunol 162:1101–1107.
   PubMed Web of Science ®Google Scholar
• Robinson, A., Huttley, G.A., Booth, H.S., Board, P.G. (2004) Modelling and bioinformatics studies of the human Kappa-class glutathione transferase predict a novel third glutathione transferase family with similarity to prokaryotic 2-hydroxychromene-2-carboxylate isomerases. Biochem J 379:541–552.
   PubMed Web of Science ®Google Scholar
• Rushmore, T.H., and Pickett, C.B. (1990) 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 265:14648–14653.
   PubMed Web of Science ®Google Scholar
• Rushmore, T.H., King, R.G., Paulson, K.E., Pickett, C.B. (1990) 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 USA 87:3826–3830.
   PubMed Web of Science ®Google Scholar
• Rushmore, T.H., Morton, M.R., Pickett, C.B. (1991) The antioxidant responsive element. Activation by oxidative stress and identification of the DNA consensus sequence required for functional activity. J Biol Chem 266:11632–11639.
   PubMed Web of Science ®Google Scholar
• Ryan, A.J., James, M.O., Ben-Zvi, Z., Law, F.C., Bend, J.R. (1976) Hepatic and extrahepatic metabolism of 14C-styrene oxide. Environ Health Perspect 17:135–144.
   PubMed Web of Science ®Google Scholar
• Sakai, M., Okuda, A., Muramatsu, M. (1988) Multiple regulatory elements and phorbol 12-O-tetradecanoate 13-acetate responsiveness of the rat placental glutathione transferase gene. Proc Natl Acad Sci USA 85:9456–9460.
   PubMed Web of Science ®Google Scholar
• Samuelsson, B., Morgenstern, R., Jakobsson, P.J. (2007) Membrane prostaglandin E synthase-1: a novel therapeutic target. Pharmacol Rev 59:207–224.
   PubMed Web of Science ®Google Scholar
• Schröder, O., Sjöström, M., Qiu, H., Jakobsson, P.J., Haeggström, J.Z. (2005) Microsomal glutathione S-transferases: selective up-regulation of leukotriene C4 synthase during lipopolysaccharide-induced pyresis. Cell Mol Life Sci 62:87–94.
   PubMed Web of Science ®Google Scholar
• Serio, K.J., Hodulik, C.R., Bigby, T.D. (2000) Sp1 and Sp3 function as key regulators of leukotriene C4 synthase gene expression in the monocyte-like cell line, THP-1. Am J Respir Cell Mol Biol 23:234–240.
   PubMed Web of Science ®Google Scholar
• Serio, K.J., Johns, S.C., Luo, L., Hodulik, C.R., Bigby, T.D. (2003) Lipopolysaccharide down-regulates the leukotriene C4 synthase gene in the monocyte-like cell line, THP-1. J Immunol 170:2121–2128.
   PubMed Web of Science ®Google Scholar
• Serio, K.J., Reddy, K.V., Bigby, T.D. (2005) Lipopolysaccharide induces 5-lipoxygenase-activating protein gene expression in THP-1 cells via a NF-κB and C/EBP-mediated mechanism. Am J Physiol Cell Physiol 288:C1125–1133.
   PubMed Web of Science ®Google Scholar
• Serio, K.J., Luo, C., Luo, L., Mao, J.T. (2007) TNF-α downregulates the leukotriene C4 synthase gene in mononuclear phagocytes. Am J Physiol Lung Cell Mol Physiol 292:L215–222.
   PubMed Web of Science ®Google Scholar
• Sherratt, P.J., Manson, M.M., Thomson, A.M., Hissink, E.A., Neal, G.E., van Bladeren, P.J., Green, T., Hayes, J.D. (1998) Increased bioactivation of dihaloalkanes in rat liver due to induction of class Theta glutathione S-transferase T1-1. Biochem J 335:619–630.
   PubMed Web of Science ®Google Scholar
• Singh, S.P., Zimniak, L., Zimniak, P. (2010) The human hGSTA5 gene encodes an enzymatically active protein. Biochim Biophys Acta 1800:16–22.
   PubMed Web of Science ®Google Scholar
• 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., et al. (1993) Structure determination and refinement of human alpha class glutathione transferase A1-1, and a comparison with the Mu and Pi class enzymes. J Mol Biol 232:192–212.
   PubMed Web of Science ®Google Scholar
• Song, J., Clagett-Dame, M., Peterson, R.E., Hahn, M.E., Westler, W.M., Sicinski, R.R., DeLuca, H.F. (2002) A ligand for the aryl hydrocarbon receptor isolated from lung. Proc Natl Acad Sci USA 99:14694–14699.
   PubMed Web of Science ®Google Scholar
• Sparnins, V.L., Venegas, P.L, Wattenberg, L.W. (1982) Glutathione S-transferase activity: enhancement by compounds inhibiting chemical carcinogenesis and by dietary constituents. J Natl Cancer Inst 68:493–496.
   PubMed Web of Science ®Google Scholar
• Spencer, S.R., Wilczak, C.A., Talalay, P. (1990) Induction of glutathione transferases and NAD(P)H:quinone reductase by fumaric acid derivatives in rodent cells and tissues. Cancer Res 50:7871–7875.
   PubMed Web of Science ®Google Scholar
• Spencer, S.R., Xue, L.A., Klenz, E.M., Talalay, P. (1991) The potency of inducers of NAD(P)H:(quinone-acceptor) oxidoreductase parallels their efficiency as substrates for glutathione transferases. Structural and electronic correlations. Biochem J 273:711–717.
   PubMed Web of Science ®Google Scholar
• Stenberg, G., Ridderström, M., Engström, A., Pemble, S.E., Mannervik, B. (1992) Cloning and heterologous expression of cDNA encoding class alpha rat glutathione transferase 8-8, an enzyme with high catalytic activity towards genotoxic α,β-unsaturated carbonyl compounds. Biochem J 284:313–319.
   PubMed Web of Science ®Google Scholar
• Stockstill, M.E., and Dauterman, W.C. (1982) Studies on the induction of glutathione S-transferases in mouse liver. Drug Chem Toxicol 5:427–437.
   PubMed Web of Science ®Google Scholar
• Strid, T., Söderström, M., Hammarström, S. (2008) Leukotriene C4 synthase promoter driven expression of GFP reveals cell specificity. Biochem Biophys Res Commun 366:80–85.
   PubMed Web of Science ®Google Scholar
• Subbaramaiah, K., Yoshimatsu, K., Scherl, E., Das, K.M., Glazier, K.D., Golijanin, D., Soslow, R.A., Tanabe, T., Naraba, H., Dannenberg, A.J. (2004) Microsomal prostaglandin E synthase-1 is overexpressed in inflammatory bowel disease. Evidence for involvement of the transcription factor Egr-1. J Biol Chem 279:12647–12658.
   PubMed Web of Science ®Google Scholar
• Sueyoshi, T., and Negishi, M. (2001) Phenobarbital response elements of cytochrome P450 genes and nuclear receptors. Annu Rev Pharmacol Toxicol 41:123–143.
   PubMed Web of Science ®Google Scholar
• Suga, T., and Akagi, M. (1970) Studies on mercapturic acids. Effect of some chemical compounds on the activities of glutathione-conjugating enzymes. Chem Pharm Bull (Tokyo) 18:115–119.
   PubMedGoogle Scholar
• Suzuki, T., Takagi, Y., Osanai, H., Li, L., Takeuchi, M., Katoh, Y., Kobayashi, M., Yamamoto, M. (2005) Pi class glutathione S-transferase genes are regulated by Nrf2 through an evolutionarily conserved regulatory element in zebrafish. Biochem J 388:65–73.
   PubMed Web of Science ®Google Scholar
• Sykiotis, G.P., and Bohmann, D. (2008) Keap1/Nrf2 signaling regulates oxidative stress tolerance and lifespan in Drosophila. Dev Cell 14:76–85.
   PubMed Web of Science ®Google Scholar
• Tan, K.L., Chelvanayagam, G., Parker, M.W., Board, P.G. (1996) Mutagenesis of the active site of the human Theta-class glutathione transferase GSTT2-2: catalysis with different substrates involves different residues. Biochem J 319:315–321.
   PubMed Web of Science ®Google Scholar
• Telakowski-Hopkins, C.A., Rodkey, J.A., Bennett, C.D., Lu, A.Y., Pickett, C.B. (1985) Rat liver glutathione S-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 260:5820–5825.
   PubMed Web of Science ®Google Scholar
• Telakowski-Hopkins, C.A., Rothkopf, G.S., Pickett, C.B. (1986) Structural analysis of a rat liver glutathione S-transferase Ya gene. Proc Natl Acad Sci USA 83:9393–9397.
   PubMed Web of Science ®Google Scholar
• Telakowski-Hopkins, C.A., King, R.G., Pickett, C.B. (1988) Glutathione S-transferase Ya subunit gene: identification of regulatory elements required for basal level and inducible expression. Proc Natl Acad Sci USA 85:1000–1004.
   PubMed Web of Science ®Google Scholar
• Thimmulappa R.K., Mai, K.H., Srisuma, S., Kensler, T.W., Yamamoto, M., Biswal, S. (2002) Identification of Nrf2-regulated genes induced by the chemopreventive agent sulforaphane by oligonucleotide microarray. Cancer Res 62:5196–5203.
   PubMed Web of Science ®Google Scholar
• Thomson, A.M., Meyer, D.J., Hayes, J.D. (1998) Sequence, catalytic properties and expression of chicken glutathione-dependent prostaglandin D2 synthase, a novel class Sigma glutathione S-transferase. Biochem J 333:317–325.
   PubMed Web of Science ®Google Scholar
• Trottier, E., Belzil, A., Stoltz, C., Anderson, A. (1995) Localization of a phenobarbital-responsive element (PBRE) in the 5′-flanking region of the rat CYP2B2 gene. Gene 158:263–268.
   PubMed Web of Science ®Google Scholar
• Tullet, J.M., Hertweck, M., An, J.H., Baker, J., Hwang, J.Y., Liu, S., Oliveira, R.P., Baumeister, R., Blackwell, T.K. (2008) Direct inhibition of the longevity-promoting factor SKN-1 by insulin-like signaling in C. elegans. Cell 132:1025–1038.
   PubMed Web of Science ®Google Scholar
• Ulland, B.M., Weisburger, J.H., Yamamoto, R.S., Weisburger, E.K. (1973) Antioxidants and carcinogenesis: butylated hydroxytoluene, but not diphenyl-p-phenylenediamine, inhibits cancer induction by N-2-fluorenylacetamide and by N-hydroxy-N-2-fluorenylacetamide in rats. Food Cosmet Toxicol 11:199–207.
   PubMedGoogle Scholar
• Vasiliou, V., Puga, A., Chang, C.Y., Tabor, M.W., Nebert, D.W. (1995) Interaction between the Ah receptor and proteins binding to the AP-1-like electrophile response element (EpRE) during murine phase II [Ah] battery gene expression. Biochem Pharmacol 50:2057–2068.
   PubMed Web of Science ®Google Scholar
• Wasserman, W.W., and Fahl, W.E. (1997) Functional antioxidant responsive elements. Proc Natl Acad Sci USA 94:5361–5366.
   PubMed Web of Science ®Google Scholar
• Wattenberg, L.W. (1972) Inhibition of carcinogenic and toxic effects of polycyclic hydrocarbons by phenolic antioxidants and ethoxyquin. J Natl Cancer Inst 48:1425–1430.
   PubMed Web of Science ®Google Scholar
• Wattenberg, L.W. (1973) Inhibition of chemical carcinogen-induced pulmonary neoplasia by butylated hydroxyanisole. J Natl Cancer Inst 50:1541–1544.
   PubMed Web of Science ®Google Scholar
• Wattenberg, L.W. (1974) Inhibition of carcinogenic and toxic effects of polycyclic hydrocarbons by several sulfur-containing compounds. J Natl Cancer Inst 52:1583–1587.
   PubMed Web of Science ®Google Scholar
• Wattenberg, L.W. (1975) Inhibition of dimethylhydrazine-induced neoplasia of the large intestine by disulfiram. J Natl Cancer Inst 54:1005–1006.
   PubMed Web of Science ®Google Scholar
• Wei, P., Zhang, J., Egan-Hafley, M., Liang, S., Moore, D.D. (2000a) The nuclear receptor CAR mediates specific xenobiotic induction of drug metabolism. Nature 407:920–923.
   PubMed Web of Science ®Google Scholar
• Wei, Y.D., Bergander, L., Rannug, U., Rannug, A. (2000b) Regulation of CYP1A1 transcription via the metabolism of the tryptophan-derived 6-formylindolo[3,2-b]carbazole. Arch Biochem Biophys 383:99–107.
   PubMed Web of Science ®Google Scholar
• Weisburger, E.K., and Evarts, R.P. (1977) Inhibitory effect of butylated hydroxytoluene (BHT) on intestinal carcinogenesis in rats by azoxymethane. Food Cosmet Toxicol 15:139–141.
   PubMedGoogle Scholar
• Welsch, D.J., Creely, D.P., Hauser, S.D., Mathis, K.J., Krivi, G.G., Isakson, P.C. (1994) Molecular cloning and expression of human leukotriene-C4 synthase. Proc Natl Acad Sci USA 91:9745–9749.
   PubMed Web of Science ®Google Scholar
• Whitlock, J.P., Jr. (1987) The regulation of gene expression by 2,3,7,8-tetrachlorodibenzo-p-dioxin. Pharmacol Rev 39:147–161.
   PubMed Web of Science ®Google Scholar
• Yates, M.S., Kwak, M.K., Egner, P.A., Groopman, J.D., Bodreddigari, S., Sutter, T.R., Baumgartner, K.J, Roebuck, B.D., Liby, K.T., Yore, M.M., Honda, T., Gribble, G.W., Sporn, M.B., Kensler, T.W. (2006) Potent protection against aflatoxin-induced tumorigenesis through induction of Nrf2-regulated pathways by the triterpenoid 1-[2-cyano-3,12-dioxooleana-1,9(11)-dien-28-oyl]imidazole. Cancer Res 66:2488–2494.
   PubMed Web of Science ®Google Scholar
• Yeager, R.L., Reisman, S.A., Aleksunes, L.M., Klaassen, C.D. (2009) Introducing the “TCDD-inducible AhR-Nrf2 gene battery”. Toxicol Sci 111:238–246.
   PubMed Web of Science ®Google Scholar
• Younes, M., Schlichting, R., Siegers, C.P. (1980) Glutathione S-transferase activities in rat liver: effect of some factors influencing the metabolism of xenobiotics. Pharmacol Res Commun 12:115–129.
   PubMedGoogle Scholar
• Zhang, D.D., and Hannink, M. (2003) Distinct cysteine residues in Keap1 are required for Keap1-dependent ubiquitination of Nrf2 and for stabilization of Nrf2 by chemopreventive agents and oxidative stress. Mol Cell Biol 23:8137–8151.
   PubMed Web of Science ®Google Scholar
• Zhang, D.D., Lo, S.C., Cross, J.V., Templeton, D.J., Hannink, M. (2004) Keap1 is a redox-regulated substrate adaptor protein for a Cul3-dependent ubiquitin ligase complex. Mol Cell Biol 24:10941–10953.
   PubMed Web of Science ®Google Scholar
• Zhang, Y., Talalay, P., Cho, C.G., Posner, G.H. (1992) A major inducer of anticarcinogenic protective enzymes from broccoli: isolation and elucidation of structure. Proc Natl Acad Sci USA 89:2399–2403.
   PubMed Web of Science ®Google Scholar