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Volumn 107, Issue 1-3, 1999, Pages 177-187

The role of metabolism in determining susceptibility to parathion toxicity in man

Author keywords

Acetylcholinesterase; Acute toxicity; CYP3A; Interindividual variations; Parathion; Phosphorothioate pesticides

Indexed keywords

4 NITROPHENOL; ALPHA NAPHTHOFLAVONE; ARYLDIALKYLPHOSPHATASE; CYTOCHROME P450 INHIBITOR; CYTOCHROME P450 ISOENZYME; DIETHYLDITHIOCARBAMIC ACID; EDETIC ACID; ESTERASE; ETHOXYRESORUFIN DEETHYLASE; KETOCONAZOLE; METYRAPONE; NARINGENIN; NIFEDIPINE; OXYGENASE; PARAOXON; PARATHION; PENTOXYRESORUFIN DEALKYLASE; PESTICIDE; QUERCETIN; QUINIDINE; SULFAPHENAZOLE; TOLBUTAMIDE; TROLEANDOMYCIN;

EID: 0033067399     PISSN: 03784274     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0378-4274(99)00044-2     Document Type: Conference Paper
Times cited : (75)

References (37)
  • 1
    • 0003080565 scopus 로고
    • A-esterases and B-esterases in perspective
    • E. Reiner, W.N. Aldrich, & F.C.G. Hoskin. Chichester: Ellis Horwood Publications
    • Aldridge W.N. A-esterases and B-esterases in perspective. Reiner E., Aldrich W.N., Hoskin F.C.G. Enzymes Hydrolysing Organophosphorus Compounds. 1989;1-14 Ellis Horwood Publications, Chichester.
    • (1989) Enzymes Hydrolysing Organophosphorus Compounds , pp. 1-14
    • Aldridge, W.N.1
  • 2
    • 0024412071 scopus 로고
    • Cytochrome P450 hPCN3, a novel cytochrome P450 gene product that is differently expressed in adult human liver
    • Aoyama T., Yamano S., Waxman D.J. Cytochrome P450 hPCN3, a novel cytochrome P450 gene product that is differently expressed in adult human liver. J. Biol. Chem. 264:1989;10388-10395.
    • (1989) J. Biol. Chem. , vol.264 , pp. 10388-10395
    • Aoyama, T.1    Yamano, S.2    Waxman, D.J.3
  • 3
    • 0016333916 scopus 로고
    • Ethoxyresorufin in direct fluorimetric assay of a microsomal O-deethylation which is preferentially inducible by 3-methylcholanthrene
    • Burke M.D., Mayer R.T. Ethoxyresorufin in direct fluorimetric assay of a microsomal O-deethylation which is preferentially inducible by 3-methylcholanthrene. Drug. Metab. Dispos. 2:1974;583-588.
    • (1974) Drug. Metab. Dispos. , vol.2 , pp. 583-588
    • Burke, M.D.1    Mayer, R.T.2
  • 4
    • 0030893296 scopus 로고    scopus 로고
    • Biotransformation of parathion in human liver: Participation of CYP3A4 and its inactivation during microsomal parathion oxidation
    • Butler A.M., Murray M. Biotransformation of parathion in human liver: participation of CYP3A4 and its inactivation during microsomal parathion oxidation. J. Pharmacol. Exp. Ther. 280:1997;966-973.
    • (1997) J. Pharmacol. Exp. Ther. , vol.280 , pp. 966-973
    • Butler, A.M.1    Murray, M.2
  • 5
    • 0028273152 scopus 로고
    • Role of detoxication pathways in acute toxicity levels of phosphorothionate insecticide in the rat
    • Chambers J.E., Ma T., Boone J.S., Chambers H.W. Role of detoxication pathways in acute toxicity levels of phosphorothionate insecticide in the rat. Life. Sci. 54:1994;1357-1364.
    • (1994) Life. Sci. , vol.54 , pp. 1357-1364
    • Chambers, J.E.1    Ma, T.2    Boone, J.S.3    Chambers, H.W.4
  • 6
    • 0028174881 scopus 로고
    • Evaluation of triacetyloleandomycin, α-naphthoflavone and diethyldithiocarbamate as selective chemical probes for inhibition of human cytochromes P450
    • Chang T.K.H., Gonzalez F.J., Waxman D.J. Evaluation of triacetyloleandomycin, α-naphthoflavone and diethyldithiocarbamate as selective chemical probes for inhibition of human cytochromes P450. Arch. Biochem. Biophys. 311:1994;437-442.
    • (1994) Arch. Biochem. Biophys. , vol.311 , pp. 437-442
    • Chang, T.K.H.1    Gonzalez, F.J.2    Waxman, D.J.3
  • 7
    • 0021070710 scopus 로고
    • The human serum paraoxonase/arylesterase polymorphism
    • Eckerson H.W., Wyte C., La Du B.N. The human serum paraoxonase/arylesterase polymorphism. Am. J. Hum. Genet. 35:1983;1126-1138.
    • (1983) Am. J. Hum. Genet. , vol.35 , pp. 1126-1138
    • Eckerson, H.W.1    Wyte, C.2    La Du, B.N.3
  • 9
    • 0000981390 scopus 로고
    • Organic phosphorus pesticides
    • W.J. Hayes, Laws E.R. San Diego: Academic Press
    • Gallo M.A., Lawryk N.J. Organic phosphorus pesticides. Hayes W.J., Laws E.R. Handbook of Pesticide Toxicology. 2:1991;917-1123 Academic Press, San Diego.
    • (1991) Handbook of Pesticide Toxicology , vol.2 , pp. 917-1123
    • Gallo, M.A.1    Lawryk, N.J.2
  • 11
    • 0026651273 scopus 로고
    • Human cytochromes P450: Problems and prospects
    • Gonzales F.J. Human cytochromes P450: problems and prospects. Trends Pharmacol. Sci. 13:1992;346-352.
    • (1992) Trends Pharmacol. Sci. , vol.13 , pp. 346-352
    • Gonzales, F.J.1
  • 12
    • 0025685663 scopus 로고
    • In vitro inhibition of dihydropyridine oxidation and aflatoxin B-1 activation in human liver microsomes by naringenin and other flavanoids
    • Guengerich F.P., Kim D.H. In vitro inhibition of dihydropyridine oxidation and aflatoxin B-1 activation in human liver microsomes by naringenin and other flavanoids. Carcinogenesis. 11:1990;2275-2279.
    • (1990) Carcinogenesis , vol.11 , pp. 2275-2279
    • Guengerich, F.P.1    Kim, D.H.2
  • 13
    • 0025757011 scopus 로고
    • Comparison of levels of several human microsomal cytochrome P450 enzymes and epoxide hydrolase in normal and disease states using immunochemical analysis of surgical liver samples
    • Guengerich F.P., Turvy C.G. Comparison of levels of several human microsomal cytochrome P450 enzymes and epoxide hydrolase in normal and disease states using immunochemical analysis of surgical liver samples. J. Pharmacol. Exp. Ther. 256:1990;1189-1194.
    • (1990) J. Pharmacol. Exp. Ther. , vol.256 , pp. 1189-1194
    • Guengerich, F.P.1    Turvy, C.G.2
  • 15
    • 0025184340 scopus 로고
    • Mechanism-based inactivation of human liver microsomal cytochrome P450 111A4 by gestodene
    • Guengerich F.P. Mechanism-based inactivation of human liver microsomal cytochrome P450 111A4 by gestodene. Chem. Res. Toxicol. 3:1990;363-371.
    • (1990) Chem. Res. Toxicol. , vol.3 , pp. 363-371
    • Guengerich, F.P.1
  • 17
    • 0029871481 scopus 로고    scopus 로고
    • Interaction of organophosphorus compounds with carboxylesterases in the rat
    • Joanovïc M., Kosanovïc M., Maksimovïc M. Interaction of organophosphorus compounds with carboxylesterases in the rat. Arch. Toxicol. 70:1996;444-450.
    • (1996) Arch. Toxicol. , vol.70 , pp. 444-450
    • Joanovïc, M.1    Kosanovïc, M.2    Maksimovïc, M.3
  • 18
    • 0017283437 scopus 로고
    • Studies of the metabolism of parathion with an apparently homogenous preparation of rabbit liver microsomal cytochrome P450
    • Kamataki T., Leelin M.C.M., Belcher D.H., Neal R.A. Studies of the metabolism of parathion with an apparently homogenous preparation of rabbit liver microsomal cytochrome P450. Drug. Metab. Dispos. 4:1976;180-189.
    • (1976) Drug. Metab. Dispos. , vol.4 , pp. 180-189
    • Kamataki, T.1    Leelin, M.C.M.2    Belcher, D.H.3    Neal, R.A.4
  • 20
    • 0028201724 scopus 로고
    • Cytochrome P450 3A-mediated human liver microsomal taxol 6α-hydroxylation
    • Kumar G.N., Walle U.K., Walle T. Cytochrome P450 3A-mediated human liver microsomal taxol 6α-hydroxylation. J. Pharm. Exp. Ther. 268:1993;1160-1165.
    • (1993) J. Pharm. Exp. Ther. , vol.268 , pp. 1160-1165
    • Kumar, G.N.1    Walle, U.K.2    Walle, T.3
  • 21
    • 0029285924 scopus 로고
    • A kinetic analysis of hepatic microsomal activation of parathion and chlorpyrifos in control and phenobarbital-treated rats
    • Ma T., Chambers J.E. A kinetic analysis of hepatic microsomal activation of parathion and chlorpyrifos in control and phenobarbital-treated rats. J. Biochem. Toxicol. 10:1995;63-68.
    • (1995) J. Biochem. Toxicol. , vol.10 , pp. 63-68
    • Ma, T.1    Chambers, J.E.2
  • 22
    • 0024561567 scopus 로고
    • A-esterases. Enzymes looking for a role?
    • Mackness M.I. A-esterases. Enzymes looking for a role? Biochem. Pharmacol. 38:1989;385-390.
    • (1989) Biochem. Pharmacol. , vol.38 , pp. 385-390
    • Mackness, M.I.1
  • 23
    • 0026595179 scopus 로고
    • Effects of imidazole derivatives on cytochromes P450 from human hepatocytes in primary culture
    • Maurice M., Pichard L., Daujat M., Fabre I., Joyeux H., Domergue J., Maurel P. Effects of imidazole derivatives on cytochromes P450 from human hepatocytes in primary culture. FASEB. J. 6:1992;752-758.
    • (1992) FASEB. J. , vol.6 , pp. 752-758
    • Maurice, M.1    Pichard, L.2    Daujat, M.3    Fabre, I.4    Joyeux, H.5    Domergue, J.6    Maurel, P.7
  • 24
    • 0029595319 scopus 로고
    • Comparative studies of two organophosphorus compounds in the mouse
    • Mutch E., Blain P.G., Kelly S.S., Williams F.M. Comparative studies of two organophosphorus compounds in the mouse. Tox. Letts. 81:1995;45-53.
    • (1995) Tox. Letts. , vol.81 , pp. 45-53
    • Mutch, E.1    Blain, P.G.2    Kelly, S.S.3    Williams, F.M.4
  • 25
    • 0344933196 scopus 로고    scopus 로고
    • Cytochrome P450 isozymes involved in parathion metabolism in the rat
    • Mutch E., Blain P.G., Williams F.M. Cytochrome P450 isozymes involved in parathion metabolism in the rat. Hum. Exp. Toxicol. 15:1996;689.
    • (1996) Hum. Exp. Toxicol. , vol.15 , pp. 689
    • Mutch, E.1    Blain, P.G.2    Williams, F.M.3
  • 27
    • 0014320353 scopus 로고
    • Degradation and activation of parathion analogs by microsomal enzymes
    • Nakatsugawa T., Tolman N.M., Dahm P.A. Degradation and activation of parathion analogs by microsomal enzymes. Biochem. Pharmacol. 17:1968;1517-1528.
    • (1968) Biochem. Pharmacol. , vol.17 , pp. 1517-1528
    • Nakatsugawa, T.1    Tolman, N.M.2    Dahm, P.A.3
  • 28
    • 0016186355 scopus 로고
    • Studies of the binding of sulfur released in the mixed-function oxidase-catalysed metabolism of diethyl p-nitrophenyl phosphorothionate (parathion) to diethyl p-nitrophenyl phosphate (paraoxon)
    • Norman B.J., Poore R.E., Neal R.A. Studies of the binding of sulfur released in the mixed-function oxidase-catalysed metabolism of diethyl p-nitrophenyl phosphorothionate (parathion) to diethyl p-nitrophenyl phosphate (paraoxon). Biochem. Pharmacol. 23:1974;1733-1744.
    • (1974) Biochem. Pharmacol. , vol.23 , pp. 1733-1744
    • Norman, B.J.1    Poore, R.E.2    Neal, R.A.3
  • 29
    • 0017613512 scopus 로고
    • A simplification of the protein assay method of Lowry et al. which is more generally applicable
    • Peterson G.L. A simplification of the protein assay method of Lowry et al. which is more generally applicable. Anal. Biochem. 83:1977;346-356.
    • (1977) Anal. Biochem. , vol.83 , pp. 346-356
    • Peterson, G.L.1
  • 30
    • 0023853892 scopus 로고
    • Determination of nifedipine and its three principal metabolites in plasma and urine by automated electron-capture capillary gas chromatography
    • Schmid B.J., Perry H.E., Idle J.R. Determination of nifedipine and its three principal metabolites in plasma and urine by automated electron-capture capillary gas chromatography. J. Chromatog. 425:1988;107-119.
    • (1988) J. Chromatog. , vol.425 , pp. 107-119
    • Schmid, B.J.1    Perry, H.E.2    Idle, J.R.3
  • 31
    • 0026049418 scopus 로고
    • Activation of amino-α-carboline, 2-amino-1-methyl-6-phenylimidazole [4,5-b] pyridine, and a copper phthalocyanine cellulose extract of cigarette smoke condensate by cytochrome P450 enzymes in rat and human liver microsomes
    • Shimada T., Guengerich F.P. Activation of amino-α-carboline, 2-amino-1-methyl-6-phenylimidazole [4,5-b] pyridine, and a copper phthalocyanine cellulose extract of cigarette smoke condensate by cytochrome P450 enzymes in rat and human liver microsomes. Cancer Res. 51:1991;5284-5291.
    • (1991) Cancer Res. , vol.51 , pp. 5284-5291
    • Shimada, T.1    Guengerich, F.P.2
  • 32
    • 0028237729 scopus 로고
    • Interindividual variations in human liver P450 enzymes involved in the oxidation of drugs, carcinogens and toxic chemicals: Studies with liver microsomes of 30 Japanese and 30 Caucasians
    • Shimada T., Yamazaki H., Mimura M., Inui Y., Guengerich P.F. Interindividual variations in human liver P450 enzymes involved in the oxidation of drugs, carcinogens and toxic chemicals: Studies with liver microsomes of 30 Japanese and 30 Caucasians. J. Pharmacol. Exp. Ther. 270:1994;414-423.
    • (1994) J. Pharmacol. Exp. Ther. , vol.270 , pp. 414-423
    • Shimada, T.1    Yamazaki, H.2    Mimura, M.3    Inui, Y.4    Guengerich, P.F.5
  • 33
  • 34
    • 0027382051 scopus 로고
    • Inhibition and induction of cytochrome P450 isoenzymes in rat lung
    • Verschoyle R.D., Dinsdale D., Wolf C.R. Inhibition and induction of cytochrome P450 isoenzymes in rat lung. J. Pharmacol. Exp. Ther. 265:1993;386-391.
    • (1993) J. Pharmacol. Exp. Ther. , vol.265 , pp. 386-391
    • Verschoyle, R.D.1    Dinsdale, D.2    Wolf, C.R.3
  • 35
    • 0025344378 scopus 로고
    • Cytochrome P450 isozymes, epoxide hydrolase and glutathione transferases in rat and human hepatic and extrahepatic tissue
    • Waziers I., Cugnenc P.H., Yang C.S., Leroux J.P., Beaune P.H. Cytochrome P450 isozymes, epoxide hydrolase and glutathione transferases in rat and human hepatic and extrahepatic tissue. J. Pharmacol. Exp. Ther. 253:1990;387-394.
    • (1990) J. Pharmacol. Exp. Ther. , vol.253 , pp. 387-394
    • Waziers, I.1    Cugnenc, P.H.2    Yang, C.S.3    Leroux, J.P.4    Beaune, P.H.5
  • 36
    • 0026744568 scopus 로고
    • Cytochrome P450 2E1 and 2A6 enzymes as major catalysts for metabolic activation of N-nitrosodialkylamines and tobacco-related nitrosamines in human liver microsomes
    • Yamazaki H., Inui Y., Yun C.-H., Guengerich F.P., Shimada T. Cytochrome P450 2E1 and 2A6 enzymes as major catalysts for metabolic activation of N-nitrosodialkylamines and tobacco-related nitrosamines in human liver microsomes. Carcinogenesis. 13:1992;1789-1794.
    • (1992) Carcinogenesis , vol.13 , pp. 1789-1794
    • Yamazaki, H.1    Inui, Y.2    Yun, C.-H.3    Guengerich, F.P.4    Shimada, T.5
  • 37
    • 0030830029 scopus 로고    scopus 로고
    • Both cytochromes P450 2E1 and 3A are involved in the O-hydroxylation of p-nitrophenol, a catalytic activity known to be specific for P450 2E1
    • Zerilli A., Ratanasavanh D., Lucas D., Goadstuff T. Both cytochromes P450 2E1 and 3A are involved in the O-hydroxylation of p-nitrophenol, a catalytic activity known to be specific for P450 2E1. Chem. Res. Toxicol. 10:1997;1205-1212.
    • (1997) Chem. Res. Toxicol. , vol.10 , pp. 1205-1212
    • Zerilli, A.1    Ratanasavanh, D.2    Lucas, D.3    Goadstuff, T.4


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