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Volumn 17, Issue 5, 2004, Pages 650-662

Glutathione transferase zeta-catalyzed bioactivation of dichloroacetic acid: Reaction of glyoxylate with amino acid nucleophiles

Author keywords

[No Author keywords available]

Indexed keywords

ACETOACETIC ACID; AMINO ACID; ANTIFLAMMIN 2; BOVINE SERUM ALBUMIN; DICHLOROACETIC ACID; DRINKING WATER; FLUORINE; GLUCOSE 6 PHOSPHATE DEHYDROGENASE; GLUTATHIONE; GLUTATHIONE TRANSFERASE; GLUTATHIONE TRANSFERASE ZETA; GLYOXYLIC ACID; IMIDAZOLIDINE DERIVATIVE; INTERLEUKIN 8; UNCLASSIFIED DRUG;

EID: 2442666573     PISSN: 0893228X     EISSN: None     Source Type: Journal    
DOI: 10.1021/tx034099+     Document Type: Article
Times cited : (12)

References (57)
  • 1
    • 0038308900 scopus 로고
    • Kinetics and equilibria for the reversible hydration of the aldehyde group in glyoxylic acid
    • Sørensen, P. E., Bruhn, K., and Lindeløv, F. (1974) Kinetics and equilibria for the reversible hydration of the aldehyde group in glyoxylic acid. Acta Chem. Scand. A 28, 162-168.
    • (1974) Acta Chem. Scand. A , vol.28 , pp. 162-168
    • Sørensen, P.E.1    Bruhn, K.2    Lindeløv, F.3
  • 3
    • 0014006847 scopus 로고
    • Thiol addition to the carbonyl group. Equilibria and kinetics
    • Lienhard, G. E., and Jencks, W. P. (1966) Thiol addition to the carbonyl group. Equilibria and kinetics. J. Am. Chem. Soc. 88, 3982-3995.
    • (1966) J. Am. Chem. Soc. , vol.88 , pp. 3982-3995
    • Lienhard, G.E.1    Jencks, W.P.2
  • 4
    • 0020646786 scopus 로고
    • Characterization of non-volatile aqueous chlorination products of humic substances
    • Miller, J. W., and Uden, P. C. (1983) Characterization of non-volatile aqueous chlorination products of humic substances. Environ. Sci. Technol. 17, 150-157.
    • (1983) Environ. Sci. Technol. , vol.17 , pp. 150-157
    • Miller, J.W.1    Uden, P.C.2
  • 5
    • 0020831190 scopus 로고
    • Chlorinated acids and chloral in drinking water
    • Uden, P. C., and Miller, J. W. (1983) Chlorinated acids and chloral in drinking water. J. Am. Water Works Assoc. 75, 524-527.
    • (1983) J. Am. Water Works Assoc. , vol.75 , pp. 524-527
    • Uden, P.C.1    Miller, J.W.2
  • 6
    • 0032210675 scopus 로고    scopus 로고
    • Biotransformation of perchloroethene: Dose-dependent excretion of trichloroacetic acid, dichloroacetic acid, and N-acetyl-S-(trichlorovinyl)-L-cysteine in rats and humans after inhalation
    • Völkel, W., Friedewald, M., Lederer, E., Pähler, A., Parker, J., and Dekant, W. (1998) Biotransformation of perchloroethene: dose-dependent excretion of trichloroacetic acid, dichloroacetic acid, and N-acetyl-S-(trichlorovinyl)-L-cysteine in rats and humans after inhalation. Toxicol. Appl. Pharmacol. 153, 20-27.
    • (1998) Toxicol. Appl. Pharmacol. , vol.153 , pp. 20-27
    • Völkel, W.1    Friedewald, M.2    Lederer, E.3    Pähler, A.4    Parker, J.5    Dekant, W.6
  • 7
    • 0021263456 scopus 로고
    • Novel metabolites of trichloroethylene through dechlorination reactions in rats, mice and humans
    • Dekant, W., Metzler, M., and Henschler, D. (1984) Novel metabolites of trichloroethylene through dechlorination reactions in rats, mice and humans. Biochem. Pharmacol. 33, 2021-2027.
    • (1984) Biochem. Pharmacol. , vol.33 , pp. 2021-2027
    • Dekant, W.1    Metzler, M.2    Henschler, D.3
  • 8
    • 0031587942 scopus 로고    scopus 로고
    • Kinetics and metabolism of chloral hydrate in children: Identification of dichloroacetate as a metabolite
    • Henderson, G. N., Yan, Z., James, M. O., Davydova, N., and Stacpoole, P. W. (1997) Kinetics and metabolism of chloral hydrate in children: identification of dichloroacetate as a metabolite. Biochem. Biophys. Res. Commun. 235, 695-698.
    • (1997) Biochem. Biophys. Res. Commun. , vol.235 , pp. 695-698
    • Henderson, G.N.1    Yan, Z.2    James, M.O.3    Davydova, N.4    Stacpoole, P.W.5
  • 10
    • 0024452528 scopus 로고
    • The pharmacology of dichloroacetate
    • Stacpoole, P. W. (1989) The pharmacology of dichloroacetate. Metabolism 38, 1124-1144.
    • (1989) Metabolism , vol.38 , pp. 1124-1144
    • Stacpoole, P.W.1
  • 11
    • 0016285850 scopus 로고
    • Mechanism of activation of pyruvate dehydrogenase by dichloroacetate and other halogenated carboxylic acids
    • Whitehouse, S., Cooper, R. H., and Randle, P. J. (1974) Mechanism of activation of pyruvate dehydrogenase by dichloroacetate and other halogenated carboxylic acids. Biochem. J. 141, 761-774.
    • (1974) Biochem. J. , vol.141 , pp. 761-774
    • Whitehouse, S.1    Cooper, R.H.2    Randle, P.J.3
  • 14
    • 0033965334 scopus 로고    scopus 로고
    • Comparative pathogenesis of haloacetic acid and protein kinase inhibitor embryotoxicity in mouse whole embryo culture
    • Ward, K. W., Rogers, E. H., and Hunter, E. S., III (2000) Comparative pathogenesis of haloacetic acid and protein kinase inhibitor embryotoxicity in mouse whole embryo culture. Toxicol. Sci. 53, 118-126.
    • (2000) Toxicol. Sci. , vol.53 , pp. 118-126
    • Ward, K.W.1    Rogers, E.H.2    Hunter III, E.S.3
  • 15
    • 0030592952 scopus 로고    scopus 로고
    • The carcinogenicity of dichloroacetic acid in the male Fischer 344 rat
    • DeAngelo, A. B., Daniel, F. B., Most, B. M., and Olson, G. R. (1996) The carcinogenicity of dichloroacetic acid in the male Fischer 344 rat. Toxicology 114, 207-221.
    • (1996) Toxicology , vol.114 , pp. 207-221
    • DeAngelo, A.B.1    Daniel, F.B.2    Most, B.M.3    Olson, G.R.4
  • 16
    • 0026093018 scopus 로고
    • The carcinogenicity of dichloroacetic acid in the male B6C3F1 mouse
    • DeAngelo, A. B., Daniel, F. B., Stober, J. A., and Olson, G. R. (1991) The carcinogenicity of dichloroacetic acid in the male B6C3F1 mouse. Fundam. Appl. Toxicol. 16, 337-347.
    • (1991) Fundam. Appl. Toxicol. , vol.16 , pp. 337-347
    • DeAngelo, A.B.1    Daniel, F.B.2    Stober, J.A.3    Olson, G.R.4
  • 17
    • 0031439569 scopus 로고    scopus 로고
    • Zeta, a novel class of glutathione transferases in a range of species from plants to humans
    • Board, P. G., Baker, R. T., Chelvanayagam, G., and 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.
    • (1997) Biochem. J. , vol.328 , pp. 929-935
    • Board, P.G.1    Baker, R.T.2    Chelvanayagam, G.3    Jermiin, L.S.4
  • 18
    • 0034009330 scopus 로고    scopus 로고
    • Discovery of a functional polymorphism in human glutathione transferase zeta by expressed sequence tag database analysis
    • Blackburn, A. C., Tzeng, H. F., Anders, M. W., and Board, P. G. (2000) Discovery of a functional polymorphism in human glutathione transferase zeta by expressed sequence tag database analysis. Pharmacogeneties 10, 49-57.
    • (2000) Pharmacogeneties , vol.10 , pp. 49-57
    • Blackburn, A.C.1    Tzeng, H.F.2    Anders, M.W.3    Board, P.G.4
  • 20
    • 0040942636 scopus 로고    scopus 로고
    • Characterization of a fungal maleylacetoacetate isomerase gene and identification of its human homologue
    • Fernández-Cañón, J. M., and Peñalva, M. A. (1998) Characterization of a fungal maleylacetoacetate isomerase gene and identification of its human homologue. J. Biol. Chem. 273, 329-337.
    • (1998) J. Biol. Chem. , vol.273 , pp. 329-337
    • Fernández-Cañón, J.M.1    Peñalva, M.A.2
  • 21
    • 0032522741 scopus 로고    scopus 로고
    • Glutathione transferase zeta catalyzes the oxygenation of the carcinogen dichloroacetic acid to glyoxylic acid
    • Tong, Z., Board, P. G., and Anders, M. W. (1998) Glutathione transferase zeta catalyzes the oxygenation of the carcinogen dichloroacetic acid to glyoxylic acid. Biochem. J. 331, 371-374.
    • (1998) Biochem. J. , vol.331 , pp. 371-374
    • Tong, Z.1    Board, P.G.2    Anders, M.W.3
  • 22
    • 0031741776 scopus 로고    scopus 로고
    • Glutathione transferase zeta-catalyzed biotransformation of dichloroacetic acid and other α-haloacids
    • Tong, Z., Board, P. G., and Anders, M. W. (1998) Glutathione transferase zeta-catalyzed biotransformation of dichloroacetic acid and other α-haloacids. Chem. Res. Toxicol. 11, 1332-1338.
    • (1998) Chem. Res. Toxicol. , vol.11 , pp. 1332-1338
    • Tong, Z.1    Board, P.G.2    Anders, M.W.3
  • 24
    • 0033391126 scopus 로고    scopus 로고
    • Inactivation of glutathione transferase zeta by dichloroacetic acid and other fluorine-lacking α-haloalkanoic acids
    • Anderson, W. B., Board, P. G., Gargano, B., and Anders, M. W. (1999) Inactivation of glutathione transferase zeta by dichloroacetic acid and other fluorine-lacking α-haloalkanoic acids. Chem. Res. Toxicol. 12, 1144-1149.
    • (1999) Chem. Res. Toxicol. , vol.12 , pp. 1144-1149
    • Anderson, W.B.1    Board, P.G.2    Gargano, B.3    Anders, M.W.4
  • 25
    • 0034053786 scopus 로고    scopus 로고
    • Polymorphism- and species-dependent inactivation of glutathione transferase zeta by dichloroacetate
    • Tzeng, H. F., Blackburn, A. C., Board, P. G., and Anders, M. W. (2000) Polymorphism- and species-dependent inactivation of glutathione transferase zeta by dichloroacetate. Chem. Res. Toxicol. 13, 231-236.
    • (2000) Chem. Res. Toxicol. , vol.13 , pp. 231-236
    • Tzeng, H.F.1    Blackburn, A.C.2    Board, P.G.3    Anders, M.W.4
  • 26
    • 0036852695 scopus 로고    scopus 로고
    • Mass spectral characterization of dichloroacetic acid-modified human glutathione transferase zeta
    • Anderson, W. B., Liebler, D. C., Board, P. G., and Anders, M. W. (2002) Mass spectral characterization of dichloroacetic acid-modified human glutathione transferase zeta. Chem. Res. Toxicol. 15, 1387-1397.
    • (2002) Chem. Res. Toxicol. , vol.15 , pp. 1387-1397
    • Anderson, W.B.1    Liebler, D.C.2    Board, P.G.3    Anders, M.W.4
  • 27
    • 0022977611 scopus 로고
    • Amino acid sequence of the pyruvate and the glyoxylate active-site lysine peptide of Escherichia coli 2-keto-4-hydroxyglutarate aldolase
    • Vlahos, C. J., and Dekker, E. E. (1986) Amino acid sequence of the pyruvate and the glyoxylate active-site lysine peptide of Escherichia coli 2-keto-4-hydroxyglutarate aldolase. J. Biol. Chem. 261, 11049-11055.
    • (1986) J. Biol. Chem. , vol.261 , pp. 11049-11055
    • Vlahos, C.J.1    Dekker, E.E.2
  • 28
    • 0028440741 scopus 로고
    • Glyoxylate for affinity labelling of 6-phosphogluconate dehydrogenase
    • Hanau, S., and Berteilli, M. (1994) Glyoxylate for affinity labelling of 6-phosphogluconate dehydrogenase. Boll. Soc. Ital. Biol. Sper. 70, 135-141.
    • (1994) Boll. Soc. Ital. Biol. Sper. , vol.70 , pp. 135-141
    • Hanau, S.1    Berteilli, M.2
  • 29
    • 0030927213 scopus 로고    scopus 로고
    • Protein targets of xenobiotic reactive intermediates
    • Pumford, N. R., and Halmes, N. C. (1997) Protein targets of xenobiotic reactive intermediates. Annu. Rev. Pharmacol. Toxicol. 37, 91-117.
    • (1997) Annu. Rev. Pharmacol. Toxicol. , vol.37 , pp. 91-117
    • Pumford, N.R.1    Halmes, N.C.2
  • 30
    • 0035703703 scopus 로고    scopus 로고
    • Molecular mechanisms of adverse drug reactions
    • Nelson, S. D. (2001) Molecular mechanisms of adverse drug reactions. Curr. Ther. Res. 62, 885-899.
    • (2001) Curr. Ther. Res. , vol.62 , pp. 885-899
    • Nelson, S.D.1
  • 31
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 32
    • 0020078719 scopus 로고
    • Assay of cysteine conjugate β-lyase activity with S-(2-benzothiazolyl)cysteine as the substrate
    • Dohn, D. R., and Anders, M. W. (1982) Assay of cysteine conjugate β-lyase activity with S-(2-benzothiazolyl)cysteine as the substrate. Anal. Biochem. 120, 379-386.
    • (1982) Anal. Biochem. , vol.120 , pp. 379-386
    • Dohn, D.R.1    Anders, M.W.2
  • 33
    • 0025949443 scopus 로고
    • Prodrugs of peptides. 15. 4-imidazolidinone prodrug derivatives of enkephalins to prevent aminopeptidase-catalyzed metabolism in plasma and absorptive mucosae
    • Rasmussen, G. J., and Bundgaard, H. (1991) Prodrugs of peptides. 15. 4-imidazolidinone prodrug derivatives of enkephalins to prevent aminopeptidase-catalyzed metabolism in plasma and absorptive mucosae. Int. J. Pharm. 76, 113-122.
    • (1991) Int. J. Pharm. , vol.76 , pp. 113-122
    • Rasmussen, G.J.1    Bundgaard, H.2
  • 34
    • 0015526438 scopus 로고
    • The condensation of aldehydes and ketones with dipeptides
    • Panetta, C. A., and Pesh-Imam, M. (1972) The condensation of aldehydes and ketones with dipeptides. J. Org. Chem. 37, 302-304.
    • (1972) J. Org. Chem. , vol.37 , pp. 302-304
    • Panetta, C.A.1    Pesh-Imam, M.2
  • 35
    • 0018894522 scopus 로고
    • "Acetaldehyde-enkephalins": Elucidation of the structure of the acetaldehyde adducts of methionine-enkephalin and leucine-enkephalin
    • Summers, M. C., Gidley, M. J., and Sanders, J. K. (1980) "Acetaldehyde-enkephalins": elucidation of the structure of the acetaldehyde adducts of methionine-enkephalin and leucine-enkephalin. FEBS Lett. 111, 307-310.
    • (1980) FEBS Lett. , vol.111 , pp. 307-310
    • Summers, M.C.1    Gidley, M.J.2    Sanders, J.K.3
  • 38
    • 0000352887 scopus 로고
    • On the mechanism of Schiff base formation and hydrolysis
    • Cordes, E. H., and Jencks, W. P. (1962) On the mechanism of Schiff base formation and hydrolysis. J. Am. Chem. Soc. 84, 832-837.
    • (1962) J. Am. Chem. Soc. , vol.84 , pp. 832-837
    • Cordes, E.H.1    Jencks, W.P.2
  • 39
    • 85050903073 scopus 로고
    • Mechanism and catalysis of simple carbonyl group reactions
    • (Cohen, S. G., Streitwieser, A., Jr., and Taft, R. W., Eds.), Interscience Publishers, New York
    • Jencks, W. P. (1964) Mechanism and catalysis of simple carbonyl group reactions. In Progress in Physical Organic Chemistry (Cohen, S. G., Streitwieser, A., Jr., and Taft, R. W., Eds.) Vol. 2, pp 63-128, Interscience Publishers, New York.
    • (1964) Progress in Physical Organic Chemistry , vol.2 , pp. 63-128
    • Jencks, W.P.1
  • 42
    • 0016428906 scopus 로고
    • Evidence for an essential lysine in glucose-6-phosphate dehydrogenase from Leuconostoc mesenteroides
    • Milhausen, M., and Levy, H. R. (1975) Evidence for an essential lysine in glucose-6-phosphate dehydrogenase from Leuconostoc mesenteroides. Eur. J. Biochem. 50, 453-461.
    • (1975) Eur. J. Biochem. , vol.50 , pp. 453-461
    • Milhausen, M.1    Levy, H.R.2
  • 43
    • 0022633847 scopus 로고
    • Covalent binding of acetaldehyde selectively inhibits the catalytic activity of lysine-dependent enzymes
    • Mauch, T. J., Donohue, T. M., Jr., Zetterman, R. K., Sorrell, M. F., and Tuma, D. J. (1986) Covalent binding of acetaldehyde selectively inhibits the catalytic activity of lysine-dependent enzymes. Hepatology 6, 263-269.
    • (1986) Hepatology , vol.6 , pp. 263-269
    • Mauch, T.J.1    Donohue Jr., T.M.2    Zetterman, R.K.3    Sorrell, M.F.4    Tuma, D.J.5
  • 44
    • 0028930481 scopus 로고
    • Mechanism-based enzyme inactivators
    • Silverman, R. B. (1995) Mechanism-based enzyme inactivators. Methods Enzymol. 249, 240-283.
    • (1995) Methods Enzymol. , vol.249 , pp. 240-283
    • Silverman, R.B.1
  • 46
    • 0014410251 scopus 로고
    • The reaction of phenylglyoxal with arginine residues in proteins
    • Takahashi, K. (1968) The reaction of phenylglyoxal with arginine residues in proteins. J. Biol. Chem. 243, 6171-6179.
    • (1968) J. Biol. Chem. , vol.243 , pp. 6171-6179
    • Takahashi, K.1
  • 47
    • 0025818677 scopus 로고
    • Prodrugs of peptides. 10. Protection of di- and tripeptides against aminopeptidase by formation of bioreversible 4-imidazolidinene derivatives
    • Rasmussen, G. J., and Bundgaard, H. (1991) Prodrugs of peptides. 10. Protection of di- and tripeptides against aminopeptidase by formation of bioreversible 4-imidazolidinene derivatives. Int. J. Pharm. 71, 45-53.
    • (1991) Int. J. Pharm. , vol.71 , pp. 45-53
    • Rasmussen, G.J.1    Bundgaard, H.2
  • 50
    • 0015606851 scopus 로고
    • The effect of partial hepatectomy on the toxicity of ethylene glycol, glycolic acid, glyoxylic acid and glycine
    • Richardson, K. E. (1973) The effect of partial hepatectomy on the toxicity of ethylene glycol, glycolic acid, glyoxylic acid and glycine. Toxicol. Appl. Pharmacol. 24, 530-538.
    • (1973) Toxicol. Appl. Pharmacol. , vol.24 , pp. 530-538
    • Richardson, K.E.1
  • 51
    • 0034908715 scopus 로고    scopus 로고
    • Ethylene glycol-mediated tubular injury: Identification of critical metabolites and injury pathways
    • Poldelski, V., Johnson, A., Wright, S., Rosa, V. D., and Zager, R. A. (2001) Ethylene glycol-mediated tubular injury: identification of critical metabolites and injury pathways. Am. J. Kidney Dis. 38, 339-348.
    • (2001) Am. J. Kidney Dis. , vol.38 , pp. 339-348
    • Poldelski, V.1    Johnson, A.2    Wright, S.3    Rosa, V.D.4    Zager, R.A.5
  • 52
    • 0033533466 scopus 로고    scopus 로고
    • Inhibition of glutathione S-transferase ζ and tyrosine metabolism by dichloroacetate: A potential unifying mechanism for its altered biotransformation and toxicity
    • Cornett, R., James, M. O., Henderson, G. N., Cheung, J., Shroads, A. L., and Stacpoole, P. W. (1999) Inhibition of glutathione S-transferase ζ and tyrosine metabolism by dichloroacetate: a potential unifying mechanism for its altered biotransformation and toxicity. Biochem. Biophys. Res. Commun. 262, 752-756.
    • (1999) Biochem. Biophys. Res. Commun. , vol.262 , pp. 752-756
    • Cornett, R.1    James, M.O.2    Henderson, G.N.3    Cheung, J.4    Shroads, A.L.5    Stacpoole, P.W.6
  • 53
    • 0038493934 scopus 로고    scopus 로고
    • Perturbation of maleylacetoacetic acid metabolism in rats with dichloroacetic acid-induced glutathione transferase zeta deficiency
    • Lantum, H. B. M., Cornejo, J., Pierce, R. H., and Anders, M. W. (2003) Perturbation of maleylacetoacetic acid metabolism in rats with dichloroacetic acid-induced glutathione transferase zeta deficiency. Toxicol. Sci. 74, 192-202.
    • (2003) Toxicol. Sci. , vol.74 , pp. 192-202
    • Lantum, H.B.M.1    Cornejo, J.2    Pierce, R.H.3    Anders, M.W.4
  • 54
    • 0001752925 scopus 로고
    • The synthesis of model compounds for maleylacetoacetic acid maleylacetone
    • Fowler, J., and Seltzer, S. (1970) The synthesis of model compounds for maleylacetoacetic acid maleylacetone. J. Org. Chem. 35, 3529-3532.
    • (1970) J. Org. Chem. , vol.35 , pp. 3529-3532
    • Fowler, J.1    Seltzer, S.2
  • 55
    • 0036093186 scopus 로고    scopus 로고
    • Alkylation and inactivation of human glutathione transferase zeta (hGSTZ1-1) by maleylacetone and fumarylacetone
    • Lantum, H. B., Liebler, D. C., Board, P. G., and Anders, M. W. (2002) Alkylation and inactivation of human glutathione transferase zeta (hGSTZ1-1) by maleylacetone and fumarylacetone. Chem. Res. Toxicol. 15, 707-716.
    • (2002) Chem. Res. Toxicol. , vol.15 , pp. 707-716
    • Lantum, H.B.1    Liebler, D.C.2    Board, P.G.3    Anders, M.W.4
  • 56
    • 0023804303 scopus 로고
    • Contributions of mass spectrometry to peptide and protein structure
    • Biemann, K. (1988) Contributions of mass spectrometry to peptide and protein structure. Biomed. Environ. Mass Spectrom. 16, 99-111.
    • (1988) Biomed. Environ. Mass Spectrom. , vol.16 , pp. 99-111
    • Biemann, K.1
  • 57
    • 0025617140 scopus 로고
    • Appendix 5. Nomenclature for peptide fragment ions (positive ions)
    • Biemann, K. (1990) Appendix 5. Nomenclature for peptide fragment ions (positive ions). Methods Enzymol. 193, 886-887.
    • (1990) Methods Enzymol. , vol.193 , pp. 886-887
    • Biemann, K.1


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