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Conjugation—Deconjugation Reactions in Drug Metabolism and Toxicity pp 79–107Cite as

Regulation of Expression of Rat Liver Glutathione S-Transferases: Xenobiotic and Antioxidant Induction of the Ya Subunit Gene

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Part of the book series: Handbook of Experimental Pharmacology ((HEP,volume 112))

Abstract

The glutathione S-transferases (GSTs) are a family of proteins that conjugate glutathione, via the sulfur atom of cysteine, to various electrophiles (Boyland and Chasseaud 1969; Chasseaud 1979; Jacoby 1978; Mannervik 1985; Mannervik and Danielson 1988; Pickett and Lu 1989; Coles and Ketterer 1990; Armstrong 1991; Tsuchida and Sato 1992). In addition to the conjugation of electrophiles, the GSTs bind with high affinity a variety of hydrophobic compounds such as heme, bilirubin, polycyclic hydrocarbons, and dexamethazone (Litwack et al. 1971; Arias et al. 1976; Bhargava et al. 1980; Homma a n d Listowsky 1985).

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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  CAS  Google Scholar 

  • Angel P, Imagawa M, Chiu R, Stein B, Imbra RJ, Rahmsdorf HJ, Jonat C, Herrlich P, Karin M (1987) Phorbol ester-inducible genes contain a common cis element recognized by a TPA-modulated transacting factor. Cell 49: 729–739

    PubMed  CAS  Google Scholar 

  • Arias IM, Fleischner G, Kirsch R, Mishkin S, Gatmaitan Z (1976) On the structure, regulation, and function of ligandin. In: Arias IM, Jacoby WB (eds) Glutathione: metabolism and function. Raven, New York, pp 175–188

    Google Scholar 

  • Armstrong RN (1991) Chem Res Toxicol 4: 131–140

    PubMed  CAS  Google Scholar 

  • Awasthi YC, Bhatnagar A, Singh SV (1987) Evidence for the involvement of histidine at the active site of glutathione S-transferase pi from human liver. Biochem Biophys Res Commun 143: 965–970

    PubMed  CAS  Google Scholar 

  • Bass NM, Kirsch RE, Tuffs SA, Marks I, Saunders SJ (1977) Ligandin heterogeneity: evidence that the two non-identical subunits are monomers of two distinct proteins. Biochim Biophys Acta 492: 163–175

    PubMed  CAS  Google Scholar 

  • Beale D, Meyer DJ, Taylor JB, Ketterer B (1983) Evidence that the Yb subunits of hepatic glutathione transferases represent two different but related families of polypeptides. Eur J Biochem 137: 125–129

    PubMed  CAS  Google Scholar 

  • Bhargava MM, Ohmi N, Listowski I, Arias IM (1980) Subunit composition, organic anion binding, catalytic and immunological properties of ligandin from rat testis. J Biol Chem 255: 724–727

    PubMed  CAS  Google Scholar 

  • Boyland E, Chasseaud LF (1969) The role of glutathione and glutathione Stransferases in mercapturic acid biosynthesis. Adv Enzymol Relat Areas Mol Biol 32: 173–219

    PubMed  CAS  Google Scholar 

  • Chang L, Wang L, Tam M (1991) The single cysteine residue on an alpha family chick liver glutathione S-transferase CL 3–3 is not functionally important. Biochem Biophys Res Comm 180: 323–328

    PubMed  CAS  Google Scholar 

  • Chasseaud LF (1979) Role of glutathione and glutathione S-transferase in the metabolism of chemical carcinogens and other electrophilic agents. Adv Cancer Res 29: 175–274

    PubMed  CAS  Google Scholar 

  • Coles B, Ketterer B (1990) The role of glutathione and glutathione transferases in chemical carcinogenesis. CRC Crit Rev Biochem Mol Biol 25: 47–50

    CAS  Google Scholar 

  • Daniel V, Sarid S, Bar-Nun S, Litwack G (1983) Rat ligandin mRNA molecular cloning and sequencing. Arch Biochem Biophys 227: 266–271

    PubMed  CAS  Google Scholar 

  • DeJong JL, Morgenstern R, Jornvall H, DePierrre JW, Tu C-PD (1988) Gene expression of rat and human microsomal glutathione S-transferases. J Biol Chem 263: 8430–8436

    Google Scholar 

  • DeLong MJ, Santamaria AB, Talalay P (1987) Role of Pl-450 in the induction of NAD(P)H: quinone reductase in a murine hepatoma cell line and its mutant. Carcinogenesis 8: 1549–1553

    CAS  Google Scholar 

  • Denison MS, Fisher JM, Whitlock JP Jr (1988) The DNA recognition site for the dioxin-Ah receptor complex. J Biol Chem 263: 17221–17224

    PubMed  CAS  Google Scholar 

  • Denison MS, Fisher JM, Whitlock JP Jr (1989) Protein-DNA interactions at recognition sites for the dioxin–Ah receptor complex. J Biol Chem 264: 16478–16482

    PubMed  CAS  Google Scholar 

  • Diccianni MB, Imagawa M, Muramatsu M (1992) The dyad palindromic glutathione S-transferase P enhancer binds multiple factors including API. Nucleic Acids Res 20: 5153–5158

    PubMed  CAS  Google Scholar 

  • Ding GJ-F, Lu AYH, Pickett CB (1985) Rat liver glutathione S-transferases. Nucleotide sequence analysis of a Ybl cDNA clone and prediction of the complete amino acid sequence of the Ybl subunit. J Biol Chem 260: 13268–13271

    Google Scholar 

  • Ding GJ-F, Ding VD-H, Rodkey JA, Bennett CD, Lu AYH, Pickett CB (1986) Rat liver glutathione S-transferases. DNA sequence analysis of a Yb2 cDNA clone and regulation of the Ybl and Yb2 mRNAs by phenobarbital. J Biol Chem 261: 7952–7957

    PubMed  CAS  Google Scholar 

  • Ding VD-H, Pickett CB (1985) Transcriptional regulation of rat liver glutathione Stransferase genes by phenobarbital and 3-methylcholanthrene. Arch Biochem Biophys 240: 553–559

    PubMed  CAS  Google Scholar 

  • Eriksson LC, Sharma RN, Roomi MW, Ho RK, Farber E, Murray RK (1983) A characteristic electrophoretic pattern of cytosolic polypeptides from hepatocyte nodules generated during liver carcinogenesis in several models. Biochem Biophys Res Commun 177: 740–745

    Google Scholar 

  • Favreau LV, Pickett CB (1991) 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 266: 4556–4561

    Google Scholar 

  • Ford-Hutchinson AW (1990) Leukotriene B4 in inflammation. Grit Rev Immunol 10: 1–12

    CAS  Google Scholar 

  • Friling RS, 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  CAS  Google Scholar 

  • Friling RS, Bergelson S, Daniel V (1992) Two adjacent AP-l-like binding sites from the electrophilic responsive element of the murine glutathione S-transferase Ya subunit gene. Proc Natl Acad Sci USA 89: 668–672

    PubMed  CAS  Google Scholar 

  • Fujisawa-Sehara A, Yamane M, Fujii-Kuriyama Y (1988) A DNA-binding factor specific for xenobiotic responsive elements of P450c gene exists as a cryptic form in cytoplasm: its possible translocation to nucleus. Proc Natl Acad Sci USA 85: 5859–5863

    PubMed  CAS  Google Scholar 

  • Hayes JD, Mantle TJ (1986) Anomalous electrophoretic behaviour of the glutathione S-transferase Ya and Yk subunits isolated from man and rodents. Biochem J 237: 731–740

    PubMed  CAS  Google Scholar 

  • Hiratsuka A, Sebata N, Kawashima K, Okuda H, Ogura K, Watabe T, Satoh K, Hatayama I, Tsuchida S, Ishikawa T, Sato K (1990) A new class of rat glutathione S-transferase Yrs-Yrs inactivating reactive sulfate esters as metabolites of carcinogenic arylmethanols. J Biol Chem 265: 11973–11981

    PubMed  CAS  Google Scholar 

  • Homma H, Listowsky I (1985) Identification of Yb-glutathione-S-transferase as a major rat liver protein labeled with dexamethasone 21-methanesulfonate. Proc Natl Acad Sci USA 82: 7165–7169

    PubMed  CAS  Google Scholar 

  • Hsieh JC, Huang SC, Chen WL, Lai YC, Tam MF (1991) Cysteine-86 is not needed for the enzymic activity of glutathione S-transferase 3-3. Biochemical J 278: 293–297

    CAS  Google Scholar 

  • Imagawa M, Osada S, Koyama Y, Suzuki T, Hirom PC, Morimura S, Muramatsu M (1991a) SF-B that binds to a negative element in glutathione transferase P gene is similar or identical to trans-activator LAP/IL6-DBP. Biochem Biophys Res Comm 179: 293–300

    PubMed  CAS  Google Scholar 

  • Imagawa M, Osada S, Okuda A, Muramatsu M (1991b) Silencer binding proteins function on multiple cis-elements in the glutathione transferase P gene. Nucleic Acids Res 19: 5–10

    PubMed  CAS  Google Scholar 

  • Izumi T, Honda Z, Oshihi N, Kitamusa S, Seyama Y, Shimizu T (1989) Partial purification and characterization of leukotriene C4 synthase from guinea pig lung. Adv Prostaglandin Thromboxane Leukotriene Res 19: 90–93

    CAS  Google Scholar 

  • Jakoby WB (1978) The glutathione S-transferases: a group of multifunctional detoxification proteins. Adv Enzymol Relat Areas MoT Biol 46: 383–414

    CAS  Google Scholar 

  • Jacoby WB, Habig WH (1980) Detoxication enzymes. In: Jacoby WB (ed) Enzymatic basis of detoxication. Academic, New York, pp 63–94

    Google Scholar 

  • Jacoby WB, Ketterer B, Mannervik B (1984) Glutathione transferases: nomenclature. Biochem Pharmacol 33: 2539–2540

    Google Scholar 

  • Jaiswal AK (1991) Human NAD(P)H: quinone oxioreductase (NQ01) gene structure and induction by dioxin. Biochemistry 30: 10647–10653

    PubMed  CAS  Google Scholar 

  • Ji X, Zhang P, Armstrong RN, Gilliland GL (1992) The 3-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-Angstrom resolution. Biochemistry 31: 10169–10184

    PubMed  CAS  Google Scholar 

  • Kalinyak JE, Taylor JM (1982) Rat glutathione S-transferase. Cloning of doublestranded cDNA and induction of its mRNA. J Biol Chem 257: 523–530

    Google Scholar 

  • Kitahara A, Satoh K, Nishimura K, Ishikawa T, Ruike K, Sato K, Tsuda H, Ito N (1984) Changes in molecular forms of rat hepatic glutathione S-transf erase during chemical hepatocarcinogenesis. Cancer Res 44: 2698–2703

    PubMed  CAS  Google Scholar 

  • Kolm R, Sroga GE, Mannervik B (1992) Participation of the phenolic hydroxyl group of tyr-8 in the catalytic mechanism of human glutathione S-transferase Pl-1. Biochem J 285: 537–540

    PubMed  CAS  Google Scholar 

  • Kong KH, Inoue H, Takahashi K (1991) Non-essentiality of cystein and histidine residues for the catalytic activity of human class Pi glutathione S-transferase. Biochem Biophys Res Commun 181: 748–755

    PubMed  CAS  Google Scholar 

  • Kong KH, Nishida M, Inuoe H, Takahashi K (1992) Tyrosine-7 is an essential residue for the catalytic activity of human class Pi glutathione S-transferase: chemical modification and site-directed mutagenisis. Biochem Biophys Res Commun 182: 1122–1129

    PubMed  CAS  Google Scholar 

  • Lai H-C, Li N-Q, Weiss MJ, Reddy CC, Tu C-PD (1984) The nucleotide sequence of a rat liver glutathione S-transferase subunit cDNA clone. J Biol Chem 259: 5536–5542

    PubMed  CAS  Google Scholar 

  • Lai H-CJ, Grove G, Tu C-PD (1986) Cloning and sequence analysis of a cDNA for a rat liver glutathione S-transferase Yb subunit. Nucleic Acids Res 14: 6101–6114

    PubMed  CAS  Google Scholar 

  • Lai H-CJ, Tu C-PD (1986) Rat glutathione S-transferases supergene family. Characterization of an anionic Yb subunit cDNA clone. J Biol Chem 261: 13793–13799

    Google Scholar 

  • Lai H-CJ, Qian B, Grove G, Tu C-PD (1988) Gene expression of rat glutathione Stransferases. Evidence for gene conversion in the evolution of the Yb multigene family. J Biol Chem 263: 11389–11395

    Google Scholar 

  • Li Y, Jaiswal AK (1992) Regulation of human NAD(P)H: quinone oxidoreductase gene. Role of API binding site combined within human antioxidant responsive element. J Biol Chem 267: 15097–15104

    Google Scholar 

  • Litwack G, Ketterer B, Arias IM (1971) Nature 234: 466–467

    PubMed  CAS  Google Scholar 

  • Liu S, Zhang P, Ji X, Johnson WW, Gilliland GL, Armstrong RN (1992) Contribution of tyrosine 6 to the catalytic mechanism of isozyme 3-3 of glutathione Stransferase. J Biol Chem 267: 4296–4299

    PubMed  CAS  Google Scholar 

  • Lundqvist G, Yucel-Lindberg T, Morgenstern R (1992) The oligometric structure of rat liver microsomal glutathione S-transferase studies by chemical cross-linking. Biochim Biophys Acta 1159: 103–108

    PubMed  CAS  Google Scholar 

  • Mannervik B (1985) The isoenzymes of glutathione transferase. Adv Enzymol Relat Areas Mol Biol 57: 357–417

    PubMed  CAS  Google Scholar 

  • Mannervik B, Danielson UH (1988) Glutathione transferases - structure and catalytic activity. CRC Crit Rev Biochem Mol Biol 23: 283–337

    CAS  Google Scholar 

  • Mannervik B, Jenson 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  CAS  Google Scholar 

  • Mannervik B, Alin P, Guthenberg C, Jenson H, Tahir MK, Warholm M, Jornvall H (1985) Identification of three classes of cytosolic glutathione transferase common to several mammalian species: correlation between structural data and enzymatic properties. Prod Natl Acad Sci USA 82: 7202–7206

    CAS  Google Scholar 

  • Manoharan TH, Gulick AM, Puchalski RB, Servais AL, Fahl WE (1992) Structural studies on human glutathione S-transferase pi - substitution mutations to determine amino acids necessary for binding glutathione. J Biol Chem 267: 18940–18945

    PubMed  CAS  Google Scholar 

  • Meyer DJ, Coles B, Pemble SE, Gilmore KS, Fraser GM, Ketterer B (1991) Theta, a new class of glutathione transferases purified from rat and man. Biochem J 274: 409–414

    PubMed  CAS  Google Scholar 

  • Morgenstern R, Lundqvist G, Mosialou E, Andersson C (1988) Membrane-bound glutathione transferase: function and properties. In: Hayes JD, Pickett CB, Mantle TJ (eds) Glutathione S-transferases and drug resistance. Taylor and Francis, New York, pp 57–64

    Google Scholar 

  • Morton MR, Bayney RM, Pickett CB (1990) Isolation and characterization of the rat glutathione S-transferase Ybl subunit gene. Arch Biochem Biophys 277: 56–60

    PubMed  CAS  Google Scholar 

  • Neubold LA, Shirayoshi Y, Ozato K, Jones JE, Nebert DW (1989) Regulation of mouse CYP1A1 gene expression by dioxin: requirement of two cis-acting elements during induction. Mol Cell Biol 9: 2378–2386

    Google Scholar 

  • Nguyen T, Pickett CB (1992) Regulation of rat glutathione S-transferase-Ya subunit gene expression - DNA-protein interaction at the antioxidant responsive element. J Biol Chem 267: 13535–13539

    PubMed  CAS  Google Scholar 

  • Nicholson DW, Ali A, Klemba MW, Munday NA, Zamboni RJ, Ford-Hutchinson AW (1992a) Human leukotriene C4 synthase expression in DMSO-differentiated U937 cells. J Biol Chem 267: 17849–17857

    PubMed  CAS  Google Scholar 

  • Nicholson DW, Klemba NW, Rasper DM, Metiers KM, Zamboni RJ, Ford-Hutchinson AW (1992b) Purification of human leukotriene C4 synthase from DMSO-differentiated U937 cells. Eur J Biochem 209: 725–734

    PubMed  CAS  Google Scholar 

  • Ogura K, Nishiyama T, Okuda 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 esthers of carcinogenic arylmethanols. Biochem Biophys Res Commun 181: 1294–1300

    CAS  Google Scholar 

  • Okuda A, Sakai M, Muramatsu M (1987) The structure of the rat glutathione Stransferase P gene and related pseudogenes. J Biol Chem 262: 3858–3863

    PubMed  CAS  Google Scholar 

  • Okuda A, Imagawa M, Maeda Y, Sakai M, Muramatsu M (1989) Structural and functional analysis of an enhancer GPEI having a phorbol 12-O-tetradecanoate 13-acetate responsive element-like sequence found in the rat glutathione transferase P gene. J Biol Chem 264: 16919–16926

    PubMed  CAS  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  CAS  Google Scholar 

  • Paulson KE, Darnell JE Jr, Rushmore TH, Pickett CB (1990) Analysis of the upstream elements of the xenobiotic compound-inducible and positionally regulated glutathione S-transferase Ya gene. Mol Cell Biol 10: 1841–1852

    PubMed  CAS  Google Scholar 

  • Pickett CB, Lu AYH (1989) Glutathione S-transferases: gene structure, regulation, and biological function. Annu Rev Biochem 58: 743–764

    PubMed  CAS  Google Scholar 

  • Pickett CB, Jeter RL, Wang RN, Lu AYH (1983) Coordinate induction of multiple mRNAs specific for rat liver phénobarbital inducible cytochrome P450. Arch Biochem Biophys 225: 854–860

    PubMed  CAS  Google Scholar 

  • Pickett CB, Telakowski-Hopkins CA, Ding GJ-F, Argenbright L, Lu AYH (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 phénobarbital. J Biol Chem 259: 5182–5188

    PubMed  CAS  Google Scholar 

  • Piper PJ (1984) Physiol Rev 64: 744–761

    PubMed  CAS  Google Scholar 

  • Prochaska HJ, Talalay P (1988) Regulatory mechanisms of monofunctional and Afunctional anticarcinogenic enzyme induction in murine liver. Cancer Res 48: 4776–34782

    PubMed  CAS  Google Scholar 

  • Prochaska HJ, De Long MJ, Talalay P (1985) On the mechanism of induction of cancer-protective enzymes: a unifying proposal. Proc Natl Acad Sci USA 82: 8232–8236

    PubMed  CAS  Google Scholar 

  • Reinemer P, Dirr HW, Ladenstein R, Schaffer J, Gallay O, Huber R (1991) The three-dimensional structure of class pi glutathione S-transferase in complex with glutathione sulfonate at 2.3 A resolution. EMBO J 10: 1997–2005

    PubMed  CAS  Google Scholar 

  • Reinemer P, Dirr HW, Ladenstein R, Huber R, Lo Bello M, Federici G, Parker W (1992) Three-dimensional structure of class Pi glutathione S-transferase from human placenta in complex with S-hexylglutathione at 2.8 A resolution. J Mol Biol 227: 214–226

    PubMed  CAS  Google Scholar 

  • Ricci G, Del Boccio G, Pennelli A, Lo Bello M, Petruzzelli R, Caccuri AM, Barra D, Federici G (1991) Redox forms of human placenta glutathione transferase. J Biol Chem 266: 21409–21415

    PubMed  CAS  Google Scholar 

  • Riley RJ, Workman P (1992) DT-diaphorase and cancer chemotherapy. Biochem Pharmacol 43: 1657–1669

    PubMed  CAS  Google Scholar 

  • Rothkopf GS, Telakowski-Hopkins CA, Stotish RL, Pickett CB (1986) Multiplicity of glutathione S-transferase genes in the rat and association with a type 2 Alu repetitive element. Biochemistry 25: 993–1002

    PubMed  CAS  Google Scholar 

  • Rushmore TH, Pickett CB (1990) Transcriptional regulation of the rat glutathione Stransferase Ya subunit gene. Characterization of a xenobiotic-responsive element controlling inducible expression by phenolic antioxidants. J Biol Chem 265: 14648–14653

    Google Scholar 

  • Rushmore TH, Pickett CB (1991) Xenobiotic responsive elements controlling inducible expression by planar aromatic compounds and phenolic antioxidants. Methods Enzymol 206: 409–420

    PubMed  CAS  Google Scholar 

  • Rushmore TH, Pickett CB (1992) Induction of the rat glutathione S-transferase Ya subunit gene through the antioxidant responsive element ( ARE) by flavonoids. Proc Am Assoc Cancer Res 33: 14

    Google Scholar 

  • Rushmore TH, Morton MR, Pickett CB (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

    Google Scholar 

  • Rushmore TH, King RG, Paulson KE, Pickett CB (1990) Regulation of glutathione S-transferase Ya subunit gene expression: identification of a unique xenobioticresponsive element controlling inducible expression by planar aromatic compounds. Proc Natl Acad Sci USA 87: 3826–3830

    PubMed  CAS  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  CAS  Google Scholar 

  • Sato K, Kitahara A, Satoh K, Ishikawa T, Tatematsu M, Ito N (1984) The placental form of glutathione S-transferase as a new marker protein for preneoplasia in rat chemical hepatocarcinogenesis. Gann 75: 199–202

    PubMed  CAS  Google Scholar 

  • Satoh K, Kitahara A, Soma Y, Knaba Y, Hatayama I, Sato K (1985) Purification, induction, and distribution of placental glutathione transferase: a new marker enzyme for preneoplastic cells in the rat chemical hepatocarcinogenesis. Proc Natl Acad Sci USA 82: 3964–3968

    PubMed  CAS  Google Scholar 

  • Soderstrom M, Mannervik B, Hammarstrom S (1990) Leukotriene C4 synthase: characterization in mouse mastocytoma cells. Methods Enzymol 187: 306–312

    PubMed  CAS  Google Scholar 

  • Stenberg G, Board PG, Mannervik B (1991) Mutation of an evolutionarily conserved tyrosine residue in the active site of a human class alpha glutathione S-transferase. FEBS Lett 293: 153–155

    Google Scholar 

  • Stenberg G, Ridderstrom M, Engstrom A, Pemble SE, Mannervik B (1992) Cloning and heterologous expression of a cDNA encoding class alpha rat glutathione Stransferase 8–8, an enzyme with high catalytic activity towards genotoxic alpha, beta unsaturated carbonyl compounds. Biochemical J 284: 313–319

    CAS  Google Scholar 

  • Suguoka Y, Kano T, Okuda A, Sakai M, Kitagawa T, Muramatsu M (1985) Cloning and the nucleotide sequence of rat glutathione S-transferase P cDNA. Nucleic Acids Res 13: 6049–6057

    PubMed  CAS  Google Scholar 

  • Talalay P, DeLong MJ, Prochaska HJ (1988) Identification of a common chemical signal regulating the induction of enzymes that protect against chemical carcinogenesis. Proc Natl Acad Sci USA 85: 8261–8265

    PubMed  CAS  Google Scholar 

  • Tamai K, Satoh K, Tsuchida S, Hatayama I, Maki T, Sato K (1990) Specific inactivation of glutathione S-transferases in class pi by SH-modifiers. Biochem Biophys Res Commun 167: 331–338

    PubMed  CAS  Google Scholar 

  • Tamai K, Shen H, Tsuchida S, Hatayama I, Satoh K, Yasui A, Oikawa A, Sato K (1991) Role of cysteine residues in the activity of rat glutathione transferase P (7–7): elucidation by oligonucleotide site-directed mutagenesis. Biochem Biophys Res Commun 179: 790–797

    PubMed  CAS  Google Scholar 

  • Telakowski-Hopkins CA, Rodkey JA, Bennett CD, Lu AYH, Pickett CB (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

    Google Scholar 

  • Telakowski-Hopkins CA, Rothkopf GS, Pickett CB (1986) Structural analysis of a rat liver glutathione S-transf erase Ya gene. Proc Natl Acad Sci USA 83: 9393–9397

    PubMed  CAS  Google Scholar 

  • Telakowski-Hopkins CA, King RG, Pickett CB (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  CAS  Google Scholar 

  • Tsuchida S, Sato K (1992) Glutathione transferases and cancer. CRC Crit Rev Biochem Mol Biol 27: 337–384

    CAS  Google Scholar 

  • Tu C-PD, Lai H-CJ, Li N, Weiss MJ, Reddy CC (1984) The Yc and Ya subunits of rat liver glutathione S-transf erases are the products of separate genes. J Biol Chem 259: 9434–9439

    PubMed  CAS  Google Scholar 

  • Van Ommen B, den Besten C, Rutten ALM, Ploemen JHTM, Vos RME, Muller F, Van Bladeren PJ (1988) Active site-directed irreversible inhibition of glutathione S-transferases by the glutathione conjugate of tetrachloro-1, 4-benzoquinone. J Biol Chem 263: 12939–12942

    PubMed  Google Scholar 

  • Van Ommen B, Ploemen JHTM, Ruven HJ, Vos RME, Bogaards JJP, Van Berkel WJH, Van Bladeren PJ (1989) Studies on the active site of rat glutathione S-transferase isoenzyme 4-4. Chemical modification by tetrachloro-1, 4-benzoquinone and its glutathione conjugate. Eur J Biochem 181: 423–429

    PubMed  Google Scholar 

  • Van Ommen B, Ploeman JHTM, Bogaards JJP, Monks TJ, Gau SS, Van Bladeren PJ (1991) Irreversible inhibition of rat glutathione S-transferase 1-1 by quinones and their glutathione conjugates. Structure-activity relationship and mechanism. Biochem J 276: 661–666

    Google Scholar 

  • Wang RW, Newton DJ, Pickett CB, Lu AYH (1991) Site-directed mutagenesis of glutathione S-transferase YaYa: nonessential role of histidine in catalysis. Arch Biochem Biophys 286: 574–578

    PubMed  CAS  Google Scholar 

  • Wang RW, Newton DJ, Huskey S-E, McKeever BM, Pickett CB, Lu AYH (1992a) Site-directed mutagenesis of glutathione S-transferase YaYa - important roles of tyrosine-9 and aspartic acid-101 in catalysis. J Biol Chem 267: 19866–19871

    PubMed  CAS  Google Scholar 

  • Wang RW, Newton DJ, Pickett CB, Lu AYH (1992b) Site-directed mutagenesis of glutathione S-transferase YaYa - functional studies of histidine, cysteine, and tryptophan mutants. Arch Biochem Biophys 297: 86–91

    PubMed  CAS  Google Scholar 

  • Widersten M, Holstrom E, Mannervik B (1991) Cystein residues are not required for the catalytic activity of human class mu glutathione S-transferase Mla-la. FEBS Lett 293: 156–159

    PubMed  CAS  Google Scholar 

  • Zhang P, Graminski GF, Armstrong RN (1991) Are the histidine residues of glutathione S-transferase important in catalysis? An assessment by 13C NMR spectroscopy and site-specific mutagenesis. J Biol Chem 266: 19475–19479

    PubMed  CAS  Google Scholar 

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  1. T. H. Rushmore
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  2. C. B. Pickett
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  3. A. Y. H. Lu
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  1. Laboratory for Cellular and Biochemical Toxicology College of Pharmacy, Rutgers University, Kilmer Campus 41 Gordon Road, Piscataway, NJ, 08854, USA

    Frederick C. Kauffman Ph.D. (Director) (Director)

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Rushmore, T.H., Pickett, C.B., Lu, A.Y.H. (1994). Regulation of Expression of Rat Liver Glutathione S-Transferases: Xenobiotic and Antioxidant Induction of the Ya Subunit Gene. In: Kauffman, F.C. (eds) Conjugation—Deconjugation Reactions in Drug Metabolism and Toxicity. Handbook of Experimental Pharmacology, vol 112. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-78429-3_3

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