메뉴 건너뛰기




Volumn 11, Issue 9, 1998, Pages 995-1004

Generation of antibodies to di- and trichloroacetylated proteins and immunochemical detection of protein adducts in rats treated with perchloroethene

Author keywords

[No Author keywords available]

Indexed keywords

HEMOCYANIN; HEXACHLOROETHANE; SERUM ALBUMIN;

EID: 0031670441     PISSN: 0893228X     EISSN: None     Source Type: Journal    
DOI: 10.1021/tx9800102     Document Type: Article
Times cited : (16)

References (32)
  • 2
    • 0013395630 scopus 로고
    • U.S. Department of Health, Education, and Welfare, Bethesda, Maryland
    • National Cancer Institute, NCI (1976) Bioassay of trichloroethylene for possible carcinogenicity, U.S. Department of Health, Education, and Welfare, Bethesda, Maryland.
    • (1976) Bioassay of Trichloroethylene for Possible Carcinogenicity
  • 3
    • 0023500127 scopus 로고
    • Bioactivation of tetrachloroethylene-role of glutathione S-transferase-catalyzed conjugation versus cytochrome P-450-dependent phospholipid alkylation
    • Dekant, W., Martens, G., Vamvakas, S., Metzler, M., and Henschler, D. (1987) Bioactivation of tetrachloroethylene-role of glutathione S-transferase-catalyzed conjugation versus cytochrome P-450-dependent phospholipid alkylation. Drug Metab. Dispos. 15, 702-709.
    • (1987) Drug Metab. Dispos. , vol.15 , pp. 702-709
    • Dekant, W.1    Martens, G.2    Vamvakas, S.3    Metzler, M.4    Henschler, D.5
  • 4
    • 0028143816 scopus 로고
    • Metabolism of tetrachloroethene in rats: Identification of Nε-(dichloroacetyl)-L-lysine and Nε-(trichloroacetyl)-L-lysine as protein adducts
    • Birner, G., Richling, C., Henschler, D., Anders, M. W., and Dekant, W. (1994) Metabolism of tetrachloroethene in rats: identification of Nε-(dichloroacetyl)-L-lysine and Nε-(trichloroacetyl)-L-lysine as protein adducts. Chem. Res. Toxicol. 7, 724- 732.
    • (1994) Chem. Res. Toxicol. , vol.7 , pp. 724-732
    • Birner, G.1    Richling, C.2    Henschler, D.3    Anders, M.W.4    Dekant, W.5
  • 5
    • 0022724047 scopus 로고
    • Identification of S-l,2,2-trichlorovinyl-N-acetylcysteine as a urinary metabolite of tetrachloroethylene: Bioactivation through glutathione conjugation as a possible explanation of its nephrocarcinogenicity
    • Dekant, W., Metzler, M., and Henschler, D. (1986) Identification of S-l,2,2-trichlorovinyl-N-acetylcysteine as a urinary metabolite of tetrachloroethylene: bioactivation through glutathione conjugation as a possible explanation of its nephrocarcinogenicity. J. Biochem. Toxicol. 1, 57-72.
    • (1986) J. Biochem. Toxicol. , vol.1 , pp. 57-72
    • Dekant, W.1    Metzler, M.2    Henschler, D.3
  • 6
    • 0021867892 scopus 로고
    • Structure/activity studies of the nephrotoxic and mutagenic action of cysteine conjugates of chloro-and fluoroalkenes
    • Green, T., and Odum, J. (1985) Structure/activity studies of the nephrotoxic and mutagenic action of cysteine conjugates of chloro-and fluoroalkenes. Chem.-Biol. Interact, 54, 15-31.
    • (1985) Chem.-Biol. Interact , vol.54 , pp. 15-31
    • Green, T.1    Odum, J.2
  • 7
    • 0025210067 scopus 로고
    • Perchloroethylene-induced rat kidney tumors: An investigation of the mechanisms involved and their relevance to humans
    • Green, T., Odum, J., Nash, J. A., and Foster, J. R. (1990) Perchloroethylene-induced rat kidney tumors: an investigation of the mechanisms involved and their relevance to humans. Toxicol. Appl. Pharmacol. 103, 77-89.
    • (1990) Toxicol. Appl. Pharmacol. , vol.103 , pp. 77-89
    • Green, T.1    Odum, J.2    Nash, J.A.3    Foster, J.R.4
  • 8
    • 0023023223 scopus 로고
    • Bacterial β-lyase mediated cleavage and mutagenicity of cysteine conjugates derived from the nephrocarcinogenic alkenes trichloroethylene, tetrachloroethylene and hexachlorobutadiene
    • Dekant, W., Vamvakas, S., Berthold, K., Schmidt, S., Wild, D., and Henschler, D. (1986) Bacterial β-lyase mediated cleavage and mutagenicity of cysteine conjugates derived from the nephrocarcinogenic alkenes trichloroethylene, tetrachloroethylene and hexachlorobutadiene. Chem.-Biol. Interact. 60, 31-45.
    • (1986) Chem.-Biol. Interact. , vol.60 , pp. 31-45
    • Dekant, W.1    Vamvakas, S.2    Berthold, K.3    Schmidt, S.4    Wild, D.5    Henschler, D.6
  • 9
    • 0023937244 scopus 로고
    • Thioacylating intermediates as metabolites of S-(l,2-dichlorovinyl)-L-cysteine and S-(l,2,2-trichlorovinyl)-L-cysteine formed by cysteine conjugate β-lyase
    • Dekant, W., Berthold, K., Vamvakas, S., Henschler, D., and Anders, M. W. (1988) Thioacylating intermediates as metabolites of S-(l,2-dichlorovinyl)-L-cysteine and S-(l,2,2-trichlorovinyl)-L-cysteine formed by cysteine conjugate β-lyase. Chem. Res. Toxicol. 1, 175-178.
    • (1988) Chem. Res. Toxicol. , vol.1 , pp. 175-178
    • Dekant, W.1    Berthold, K.2    Vamvakas, S.3    Henschler, D.4    Anders, M.W.5
  • 10
    • 0000666578 scopus 로고
    • Thioketene formation from α-haloalkenyl 2-nitrophenyl disulfides: Models for biological reactive intermediates of cytotoxic S-conjugates
    • Dekant, W., Urban, G., Görsman, C., and Anders, M. W. (1991) Thioketene formation from α-haloalkenyl 2-nitrophenyl disulfides: models for biological reactive intermediates of cytotoxic S-conjugates. J. Am. Chem. Soc. 113, 5120-5122.
    • (1991) J. Am. Chem. Soc. , vol.113 , pp. 5120-5122
    • Dekant, W.1    Urban, G.2    Görsman, C.3    Anders, M.W.4
  • 11
    • 0001776185 scopus 로고
    • Untersuchungen zum Aufbau von Fermentmodellen mit sterischer Spezifität
    • Lautsch, W., and Heinicke, D. (1957) Untersuchungen zum Aufbau von Fermentmodellen mit sterischer Spezifität. Kolloid Z. 154, 1-4.
    • (1957) Kolloid Z , vol.154 , pp. 1-4
    • Lautsch, W.1    Heinicke, D.2
  • 12
    • 0017184389 scopus 로고
    • A rapid and sensitive method for quantitation of microgram quantities of protein utilizing the principal of protein-dye binding
    • Bradford, M. M. (1976) A rapid and sensitive method for quantitation of microgram quantities of protein utilizing the principal of protein-dye binding. Anal. Biochem. 72, 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 13
    • 0019881707 scopus 로고
    • A simple modified carbodiimide method for conjugation of small-molecular-weight compounds to immunoglobulin G with minimal protein cross-linking
    • Davis, M. T., and Preston, J. F. (1981) A simple modified carbodiimide method for conjugation of small-molecular-weight compounds to immunoglobulin G with minimal protein cross-linking. Anal. Biochem. 116, 402-407.
    • (1981) Anal. Biochem. , vol.116 , pp. 402-407
    • Davis, M.T.1    Preston, J.F.2
  • 14
    • 0026614994 scopus 로고
    • The determination of ε-amino groups in soluble and poorly soluble proteinaceous materials by a spectrophotometric method using trinitrobenzenesulfonic acid
    • Bubnis, W. A., and Ofner III, C. M. (1992) The determination of ε-amino groups in soluble and poorly soluble proteinaceous materials by a spectrophotometric method using trinitrobenzenesulfonic acid. Anal. Biochem. 207, 129-133.
    • (1992) Anal. Biochem. , vol.207 , pp. 129-133
    • Bubnis, W.A.1    Ofner III, C.M.2
  • 15
    • 0002507772 scopus 로고
    • ELISA and related enzyme immunoassays
    • Catty, D., Eds., IRL Press at Oxford University Press: Oxford
    • Catty, D., and Raykundalia, C. (1989) ELISA and related enzyme immunoassays, In Antibodies, Vol. II, A practical approach (Catty, D., Eds.) pp 97-154, IRL Press at Oxford University Press: Oxford.
    • (1989) Antibodies, II, A Practical Approach , vol.2 , pp. 97-154
    • Catty, D.1    Raykundalia, C.2
  • 16
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 17
    • 0026047099 scopus 로고
    • Halothane metabolism: Immunochemical evidence for molecular mimicry of trifluoroacetylated protein adducts by constitutive polypeptides
    • Christen, U., Burgin, M., and Gut, J. (1991) Halothane metabolism: Immunochemical evidence for molecular mimicry of trifluoroacetylated protein adducts by constitutive polypeptides. Mol. Pharmacol. 40, 390-400.
    • (1991) Mol. Pharmacol. , vol.40 , pp. 390-400
    • Christen, U.1    Burgin, M.2    Gut, J.3
  • 18
    • 0026467002 scopus 로고
    • Molecular mimicry of trifluoroacetylated human liver protein adducts by constitutive proteins and immunochemical evidence for its impairment in halothane hepatitis
    • Gut, J., Christen, U., Huwyler, J., Bürgin, M., and Kenna, J. G. (1992) Molecular mimicry of trifluoroacetylated human liver protein adducts by constitutive proteins and immunochemical evidence for its impairment in halothane hepatitis. Eur. J. Biochem. 210, 569-576.
    • (1992) Eur. J. Biochem. , vol.210 , pp. 569-576
    • Gut, J.1    Christen, U.2    Huwyler, J.3    Bürgin, M.4    Kenna, J.G.5
  • 19
    • 0027468138 scopus 로고
    • Halothane metabolism: The dihydrolipoamide acetyltransferase subunit of the pyruvate dehydrogenase complex molecularly mimics trifluoroacetyl-protein adducts
    • Christen, U., Jenö, P., and Gut, J. (1993) Halothane metabolism: the dihydrolipoamide acetyltransferase subunit of the pyruvate dehydrogenase complex molecularly mimics trifluoroacetyl-protein adducts. Biochemistry 32, 1492-1499.
    • (1993) Biochemistry , vol.32 , pp. 1492-1499
    • Christen, U.1    Jenö, P.2    Gut, J.3
  • 20
    • 0023003510 scopus 로고
    • Renal cysteine conjugate β-lyase: Bioactivation of nephrotoxic cysteine S-conjugates in mitochondrial outer membrane
    • Lash, L. H., Elfarra, A. A., and Anders, M. W, (1986) Renal cysteine conjugate β-lyase: Bioactivation of nephrotoxic cysteine S-conjugates in mitochondrial outer membrane. J. Biol. Chem. 261, 5930-5935.
    • (1986) J. Biol. Chem. , vol.261 , pp. 5930-5935
    • Lash, L.H.1    Elfarra, A.A.2    Anders, M.W.3
  • 21
    • 0025327939 scopus 로고
    • Glutamine transaminase k/cysteine conjugate β-lyase
    • Cooper, A. J. L., and Anders, M. W. (1990) Glutamine transaminase k/cysteine conjugate β-lyase. Ann. N.Y. Acad. Sci. 585, 118- 127.
    • (1990) Ann. N.Y. Acad. Sci. , vol.585 , pp. 118-127
    • Cooper, A.J.L.1    Anders, M.W.2
  • 22
    • 3543103413 scopus 로고
    • Enzymology of cysteine 5-conjugate β-lyases
    • Cooper, A. J. L. (1994) Enzymology of cysteine 5-conjugate β-lyases. Adv. Pharmacol. 27, 73-115.
    • (1994) Adv. Pharmacol. , vol.27 , pp. 73-115
    • Cooper, A.J.L.1
  • 23
    • 0031057097 scopus 로고    scopus 로고
    • Identification of three distinct tumor suppressor loci on the short arm of chromosome 9 in small cell lung cancer
    • Kirn, S. K., Ro, J. Y., Kemp, B. L., Lee, J. S., Kwon, T. J., Fong, K. M., Sekido, Y., Minna, J. D., Hong, W. K, and Mao, L. (1997) Identification of three distinct tumor suppressor loci on the short arm of chromosome 9 in small cell lung cancer. Cancer Res. 57, 400-403.
    • (1997) Cancer Res , vol.57 , pp. 400-403
    • Kirn, S.K.1    Ro, J.Y.2    Kemp, B.L.3    Lee, J.S.4    Kwon, T.J.5    Fong, K.M.6    Sekido, Y.7    Minna, J.D.8    Hong, W.K.9    Mao, L.10
  • 24
    • 0023923003 scopus 로고
    • Biosynthesis and biotransformation of glutathione S-conjugates to toxic metabolites
    • Anders, M. W., Lash, L. H., Dekant, W., Elfarra, A. A., and Dohn, D. R. (1988) Biosynthesis and biotransformation of glutathione S-conjugates to toxic metabolites. Crit. Rev. Toxicol. 18, 311- 342.
    • (1988) Crit. Rev. Toxicol. , vol.18 , pp. 311-342
    • Anders, M.W.1    Lash, L.H.2    Dekant, W.3    Elfarra, A.A.4    Dohn, D.R.5
  • 25
    • 0018252554 scopus 로고
    • Cysteine conjugate β-lyase in rat liver. A novel enzyme catalyzing formation of thiol-containing metabolites of drugs
    • Tateishi, M., Suzuki, S., and Shimizu, H. (1978) Cysteine conjugate β-lyase in rat liver. A novel enzyme catalyzing formation of thiol-containing metabolites of drugs. J. Biol. Chem. 253, 8854-8859.
    • (1978) J. Biol. Chem. , vol.253 , pp. 8854-8859
    • Tateishi, M.1    Suzuki, S.2    Shimizu, H.3
  • 26
    • 0025816970 scopus 로고
    • Formation of difluorothionoacetyl- Protein adducts by S-(1,1,2,2-tetrafluoroethyl)-L-cysteine metabolites: Nucleophilic catalysis of stable adduct formation by histidine and tyrosine
    • Hayden, P. J., Yang, Y., Ward, A. J. I., Dulik, D. M., McCann, D. J., and Stevens, J. L. (1991) Formation of difluorothionoacetyl- protein adducts by S-(1,1,2,2-tetrafluoroethyl)-L-cysteine metabolites: nucleophilic catalysis of stable adduct formation by histidine and tyrosine. Biochemistry 30, 5935-5943.
    • (1991) Biochemistry , vol.30 , pp. 5935-5943
    • Hayden, P.J.1    Yang, Y.2    Ward, A.J.I.3    Dulik, D.M.4    McCann, D.J.5    Stevens, J.L.6
  • 27
    • 0026035519 scopus 로고
    • Role of human cytochrome P-450 IIE1 in the oxidation of many low molecular weight cancer suspects
    • Guengerich, F. P., Kim, D.-H., and Iwasai, M. (1991) Role of human cytochrome P-450 IIE1 in the oxidation of many low molecular weight cancer suspects. Chem. Res. Toxicol. 4, 168- 179.
    • (1991) Chem. Res. Toxicol. , vol.4 , pp. 168-179
    • Guengerich, F.P.1    Kim, D.-H.2    Iwasai, M.3
  • 28
    • 0029996390 scopus 로고    scopus 로고
    • Immunochemical detection of protein adducts in mice treated with trichloroethylene
    • Halmes, N. C., Mcmillan, D. C., Oatis, J. E., and Pumford, N. R. (1996) Immunochemical detection of protein adducts in mice treated with trichloroethylene. Chem. Res. Toxicol. 9, 451-456.
    • (1996) Chem. Res. Toxicol. , vol.9 , pp. 451-456
    • Halmes, N.C.1    Mcmillan, D.C.2    Oatis, J.E.3    Pumford, N.R.4
  • 29
    • 0028324336 scopus 로고
    • Glutathione-S-transferase is a target for covalent modification by a halothane reactive intermediate in the guinea pig liver
    • Brown, A. P., and Gandolfi, A. J. (1994) Glutathione-S-transferase is a target for covalent modification by a halothane reactive intermediate in the guinea pig liver. Toxicology 89, 35-47.
    • (1994) Toxicology , vol.89 , pp. 35-47
    • Brown, A.P.1    Gandolfi, A.J.2
  • 30
    • 0015120455 scopus 로고
    • 2-Oxoacid dehydrogenases of rat liver mitochondria as the site of action of S-(1,2- Dichlorovinyl)-L-cysteine and S-(l,2-dichlorovinyl)-3-mercaptopropionic acid
    • Stonard, M. D., and Parker, V. H. (1971) 2-Oxoacid dehydrogenases of rat liver mitochondria as the site of action of S-(1,2- dichlorovinyl)-L-cysteine and S-(l,2-dichlorovinyl)-3-mercaptopropionic acid. Biochem. Pharmacol. 20, 2417-2427.
    • (1971) Biochem. Pharmacol. , vol.20 , pp. 2417-2427
    • Stonard, M.D.1    Parker, V.H.2
  • 31
    • 0023492515 scopus 로고
    • Mechanism of S-(l,2-dichlorovinyl)-L-cysteine- And S-(l,2-dichlorovinyl)-L-homocys- teine-induced renal mitochondrial toxicity
    • Lash, L. H., and Anders, M. W. (1987) Mechanism of S-(l,2-dichlorovinyl)-L-cysteine- and S-(l,2-dichlorovinyl)-L-homocys- teine-induced renal mitochondrial toxicity. Mol. Pharmacol. 32, 549-556.
    • (1987) Mol. Pharmacol. , vol.32 , pp. 549-556
    • Lash, L.H.1    Anders, M.W.2
  • 32
    • 0025327018 scopus 로고
    • The effect of haloalk- Ene cysteine conjugates on rat renal glutathione reductase and lipoyl dehydrogenase activities
    • Lock, E. A., and Schnellmann, R. G. (1990) The effect of haloalk- ene cysteine conjugates on rat renal glutathione reductase and lipoyl dehydrogenase activities. Toxicol. Appl. Pharmacol. 104, 180-190.
    • (1990) Toxicol. Appl. Pharmacol. , vol.104 , pp. 180-190
    • Lock, E.A.1    Schnellmann, R.G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.