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Volumn 68, Issue 5, 2004, Pages 959-967

S-oxygenation of the thioether organophosphate insecticides phorate and disulfoton by human lung flavin-containing monooxygenase 2

Author keywords

dithiothreitol; DMEM; DTT; Dulbecco's modified Eagle's medium; Flavin containing monooxygenase; FMO; Insecticides; Lung; Organophosphates; PKC; protein kinase C; Toxicity

Indexed keywords

CHOLINESTERASE INHIBITOR; CYTOCHROME P450; DIMETHYLANILINE MONOOXYGENASE; DISULFOTON; GLUTATHIONE; INSECTICIDE; OXYGEN; PHORATE; SULFIDE; SULFONE; SULFOXIDE; SULFUR;

EID: 3843070896     PISSN: 00062952     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bcp.2004.05.051     Document Type: Article
Times cited : (60)

References (47)
  • 1
    • 0028945438 scopus 로고
    • Structural and catalytic properties of the mammalian flavin-containing monooxygenase
    • Cashman J.R. Structural and catalytic properties of the mammalian flavin-containing monooxygenase. Chem. Res. Toxicol. 8:1995;165-181
    • (1995) Chem. Res. Toxicol. , vol.8 , pp. 165-181
    • Cashman, J.R.1
  • 2
    • 0036036854 scopus 로고    scopus 로고
    • An overview of the mechanism, substrate specificities, and structure of FMOs
    • Ziegler D.M. An overview of the mechanism, substrate specificities, and structure of FMOs. Drug Metab. Rev. 34:2003;503-511
    • (2003) Drug Metab. Rev. , vol.34 , pp. 503-511
    • Ziegler, D.M.1
  • 3
    • 0028302414 scopus 로고
    • A nomenclature for the mammalian flavin-containing monooxygenase gene family based on amino acid sequence identities
    • Lawton M., Cashman J., Cresteil T., Dolphin C., Elfarra A., Hines R.N., et al. A nomenclature for the mammalian flavin-containing monooxygenase gene family based on amino acid sequence identities. Arch. Biochem. Biophys. 308:1994;254-257
    • (1994) Arch. Biochem. Biophys. , vol.308 , pp. 254-257
    • Lawton, M.1    Cashman, J.2    Cresteil, T.3    Dolphin, C.4    Elfarra, A.5    Hines, R.N.6
  • 4
    • 0032515069 scopus 로고    scopus 로고
    • The flavin-containing monooxygenase 2 gene (FMO2) of humans, but not of other primates, encodes a truncated, nonfunctional protein
    • Dolphin C.T., Beckett D.J., Janmohamed A., Cullingford T.E., Smith R.L., Shepard E.A., et al. The flavin-containing monooxygenase 2 gene (FMO2) of humans, but not of other primates, encodes a truncated, nonfunctional protein. J. Biol. Chem. 273:1998;30599-30607
    • (1998) J. Biol. Chem. , vol.273 , pp. 30599-30607
    • Dolphin, C.T.1    Beckett, D.J.2    Janmohamed, A.3    Cullingford, T.E.4    Smith, R.L.5    Shepard, E.A.6
  • 6
    • 0031588975 scopus 로고    scopus 로고
    • Pulmonary flavin-containing monooxygenase (FMO) in rhesus macaque: Expression of FMO2 protein and analysis of the cDNA
    • Yueh M.F., Krueger S.K., Williams D.E. Pulmonary flavin-containing monooxygenase (FMO) in rhesus macaque: expression of FMO2 protein and analysis of the cDNA. Biochim. Biophys. Acta. 1350:1997;267-271
    • (1997) Biochim. Biophys. Acta , vol.1350 , pp. 267-271
    • Yueh, M.F.1    Krueger, S.K.2    Williams, D.E.3
  • 7
    • 0021957282 scopus 로고
    • Identification of distinct hepatic and pulmonary forms of microsomal flavin-containing monooxygenase in the mouse and rabbit
    • Tynes R.E., Sabourin P.J., Hodgson E. Identification of distinct hepatic and pulmonary forms of microsomal flavin-containing monooxygenase in the mouse and rabbit. Biochem. Biophys. Res. Commun. 126:1985;1069-1075
    • (1985) Biochem. Biophys. Res. Commun. , vol.126 , pp. 1069-1075
    • Tynes, R.E.1    Sabourin, P.J.2    Hodgson, E.3
  • 8
    • 0021747810 scopus 로고
    • Rabbit lung flavin-containing monooxygenase is immunochemically and catalytically distinct from the liver enzyme
    • Williams D.E., Ziegler D.M., Nordin D.J., Hales S.E., Masters B.S.S. Rabbit lung flavin-containing monooxygenase is immunochemically and catalytically distinct from the liver enzyme. Biochem. Biophys. Res. Commun. 125:1984;116-122
    • (1984) Biochem. Biophys. Res. Commun. , vol.125 , pp. 116-122
    • Williams, D.E.1    Ziegler, D.M.2    Nordin, D.J.3    Hales, S.E.4    Masters, B.S.S.5
  • 9
    • 0022360477 scopus 로고
    • Rabbit lung flavin-containing monooxygenase. Purification, characterization and induction during pregnancy
    • Williams D.E., Hale S.E., Muerhoff A.S., Masters B.S.S. Rabbit lung flavin-containing monooxygenase. Purification, characterization and induction during pregnancy. Mol. Pharmacol. 28:1985;381-390
    • (1985) Mol. Pharmacol. , vol.28 , pp. 381-390
    • Williams, D.E.1    Hale, S.E.2    Muerhoff, A.S.3    Masters, B.S.S.4
  • 10
    • 0022860321 scopus 로고
    • Formation of hydrogen peroxide and N-hydroxylated amines catalyzed by pulmonary flavin-containing monooxygenases in the presence of primary alkylamines
    • Tynes R.E., Sabourin P.J., Hodgson E., Philpot R.M. Formation of hydrogen peroxide and N-hydroxylated amines catalyzed by pulmonary flavin-containing monooxygenases in the presence of primary alkylamines. Arch. Biochem. Biophys. 251:1986;654-664
    • (1986) Arch. Biochem. Biophys. , vol.251 , pp. 654-664
    • Tynes, R.E.1    Sabourin, P.J.2    Hodgson, E.3    Philpot, R.M.4
  • 11
    • 0022861737 scopus 로고
    • Substrate specificity of the rabbit lung flavin-containing monooxygenase for amines: Oxidation products of primary alkylamines
    • Poulsen L.L., Taylor K., Williams D.E., Masters B.S.S., Ziegler D.M. Substrate specificity of the rabbit lung flavin-containing monooxygenase for amines: oxidation products of primary alkylamines. Mol. Pharmacol. 30:1986;680-685
    • (1986) Mol. Pharmacol. , vol.30 , pp. 680-685
    • Poulsen, L.L.1    Taylor, K.2    Williams, D.E.3    Masters, B.S.S.4    Ziegler, D.M.5
  • 12
    • 0025151081 scopus 로고
    • Substrate specificities of rabbit lung and porcine liver flavin-containing monooxygenases: Differences due to substrate size
    • Nagata T., Williams D.E., Ziegler D.M. Substrate specificities of rabbit lung and porcine liver flavin-containing monooxygenases: differences due to substrate size. Chem. Res. Toxicol. 3:1990;372-376
    • (1990) Chem. Res. Toxicol. , vol.3 , pp. 372-376
    • Nagata, T.1    Williams, D.E.2    Ziegler, D.M.3
  • 13
    • 0035195097 scopus 로고    scopus 로고
    • Sequencing, expression, and characterization of cDNA expressed flavin-containing monooxygenase 2 from mouse
    • Karoly E.D., Rose R.L. Sequencing, expression, and characterization of cDNA expressed flavin-containing monooxygenase 2 from mouse. J. Biochem. Mol. Toxicol. 15:2001;300-308
    • (2001) J. Biochem. Mol. Toxicol. , vol.15 , pp. 300-308
    • Karoly, E.D.1    Rose, R.L.2
  • 15
    • 0026937248 scopus 로고
    • Guinea pig or rabbit lung flavin-containing monooxygenases with distinct mobilites in SDS-PAGE are allelic variants that differ at only two positions
    • Nikbakht K.N., Lawton M.P., Philpot R.M. Guinea pig or rabbit lung flavin-containing monooxygenases with distinct mobilites in SDS-PAGE are allelic variants that differ at only two positions. Pharmacogenetics. 2:1992;207-216
    • (1992) Pharmacogenetics , vol.2 , pp. 207-216
    • Nikbakht, K.N.1    Lawton, M.P.2    Philpot, R.M.3
  • 16
    • 0034329485 scopus 로고    scopus 로고
    • Ethnic differences in human flavin-containing monooxygenase 2 (FMO2) polymorphisms: Detection of expressed protein in African Americans
    • Whestine J.R., Yueh M.-F., Hopp K.A., McCarver D.G., Williams D.E., Park C.-S., et al. Ethnic differences in human flavin-containing monooxygenase 2 (FMO2) polymorphisms: detection of expressed protein in African Americans. Toxicol. Appl. Pharmacol. 168:2000;216-224
    • (2000) Toxicol. Appl. Pharmacol. , vol.168 , pp. 216-224
    • Whestine, J.R.1    Yueh, M.-F.2    Hopp, K.A.3    McCarver, D.G.4    Williams, D.E.5    Park, C.-S.6
  • 17
    • 0036136926 scopus 로고    scopus 로고
    • Identification of active flavin-containing monooxygenase isoform 2 in human lung and characterization of expressed protein
    • Krueger S.K., Martin S.R., Yueh M.-F., Pereira C.B., Williams D.E. Identification of active flavin-containing monooxygenase isoform 2 in human lung and characterization of expressed protein. Drug Metab. Dispos. 30:2002;34-41
    • (2002) Drug Metab. Dispos. , vol.30 , pp. 34-41
    • Krueger, S.K.1    Martin, S.R.2    Yueh, M.-F.3    Pereira, C.B.4    Williams, D.E.5
  • 20
    • 34250240907 scopus 로고
    • Dialkyl phosphates in urine samples from pesticide formulators exposed to disulfoton and phorate
    • Brokopp C.D., Wyatt J.L., Gabica J. Dialkyl phosphates in urine samples from pesticide formulators exposed to disulfoton and phorate. Bull. Environ. Contam. Toxicol. 26:1981;524-529
    • (1981) Bull. Environ. Contam. Toxicol. , vol.26 , pp. 524-529
    • Brokopp, C.D.1    Wyatt, J.L.2    Gabica, J.3
  • 22
    • 0021287501 scopus 로고
    • The metabolism of insecticides: The role of monooxygenase enzymes
    • Kulkarni A.P., Hodgson E. The metabolism of insecticides: the role of monooxygenase enzymes. Annu. Rev. Pharmacol. Toxicol. 24:1984;19-42
    • (1984) Annu. Rev. Pharmacol. Toxicol. , vol.24 , pp. 19-42
    • Kulkarni, A.P.1    Hodgson, E.2
  • 23
    • 0019209724 scopus 로고
    • Flavin adenine dinucleotide-dependent monooxygenase: Its role in the sulfoxidation of pesticides in mammals
    • Hajjar N.P., Hodgson E. Flavin adenine dinucleotide-dependent monooxygenase: its role in the sulfoxidation of pesticides in mammals. Science. 209:1980;1134-1136
    • (1980) Science , vol.209 , pp. 1134-1136
    • Hajjar, N.P.1    Hodgson, E.2
  • 24
    • 0019941896 scopus 로고
    • Sulfoxidation of thioether-containing pesticides by the flavin-adenine dinucleotide-dependent monooxygenase of pig liver microsomes
    • Hajjar N.P., Hodgson E. Sulfoxidation of thioether-containing pesticides by the flavin-adenine dinucleotide-dependent monooxygenase of pig liver microsomes. Biochem. Pharmacol. 31:1982;745-752
    • (1982) Biochem. Pharmacol. , vol.31 , pp. 745-752
    • Hajjar, N.P.1    Hodgson, E.2
  • 25
    • 0022321365 scopus 로고
    • Oxidation of pesticides by purified microsomal FAD-containing monooxygenase from mouse and pig liver
    • Smyser B.P., Sabourin P.J., Hodgson E. Oxidation of pesticides by purified microsomal FAD-containing monooxygenase from mouse and pig liver. Pest Biochem. Physiol. 24:1985;368-374
    • (1985) Pest Biochem. Physiol. , vol.24 , pp. 368-374
    • Smyser, B.P.1    Sabourin, P.J.2    Hodgson, E.3
  • 26
    • 1342317375 scopus 로고
    • Magnitude of involvement of the mammalian flavin-containing monooxygenase in the microsomal oxidation of pesticides
    • Tynes R.E., Hodgson E. Magnitude of involvement of the mammalian flavin-containing monooxygenase in the microsomal oxidation of pesticides. J. Agric. Food Chem. 33:1985;471-479
    • (1985) J. Agric. Food Chem. , vol.33 , pp. 471-479
    • Tynes, R.E.1    Hodgson, E.2
  • 27
    • 0023902245 scopus 로고
    • Stereospecificity in the oxidation of phorate and phorate sulphoxide by purified FAD-containing monooxygenase and cytochrome P-450 isozymes
    • Levi P.E., Hodgson E. Stereospecificity in the oxidation of phorate and phorate sulphoxide by purified FAD-containing monooxygenase and cytochrome P-450 isozymes. Xenobiotica. 18:1988;29-39
    • (1988) Xenobiotica , vol.18 , pp. 29-39
    • Levi, P.E.1    Hodgson, E.2
  • 28
    • 0023924867 scopus 로고
    • Hepatic and extrahepatic microsomal oxidation of phorate by the cytochrome P-450 and FAD-containing monooxygenase systems in the mouse
    • Kinsler S., Levi P.E., Hodgson E. Hepatic and extrahepatic microsomal oxidation of phorate by the cytochrome P-450 and FAD-containing monooxygenase systems in the mouse. Pest Biochem. Physiol. 31:1988;54-60
    • (1988) Pest Biochem. Physiol. , vol.31 , pp. 54-60
    • Kinsler, S.1    Levi, P.E.2    Hodgson, E.3
  • 29
    • 0024992252 scopus 로고
    • Relative contributions of the cytochrome P450 and flavin-containing monooxygenases to the microsomal oxidation of phorate following treatment of mice with phenobarbital, hydrocortisone, acetone, and piperonyl butoxide
    • Kinsler S., Levi P.E., Hodgson E. Relative contributions of the cytochrome P450 and flavin-containing monooxygenases to the microsomal oxidation of phorate following treatment of mice with phenobarbital, hydrocortisone, acetone, and piperonyl butoxide. Pest Biochem. Physiol. 37:1990;174-181
    • (1990) Pest Biochem. Physiol. , vol.37 , pp. 174-181
    • Kinsler, S.1    Levi, P.E.2    Hodgson, E.3
  • 30
    • 0026757563 scopus 로고
    • The role of the flavin-containing monooxygenase (EC 1.14.13.8) in the metabolism and mode of action of agricultural chemicals
    • Hodgson E., Levi P.E. The role of the flavin-containing monooxygenase (EC 1.14.13.8) in the metabolism and mode of action of agricultural chemicals. Xenobiotica. 22:1992;1175-1183
    • (1992) Xenobiotica , vol.22 , pp. 1175-1183
    • Hodgson, E.1    Levi, P.E.2
  • 31
    • 0032450277 scopus 로고    scopus 로고
    • Flavin-containing monooxygenase and cytochrome P450 mediated metabolism of pesticides: From mouse to human
    • Hodgson E., Cherrington N., Coleman S.C., Liu S., Falls J.G., Cao Y., et al. Flavin-containing monooxygenase and cytochrome P450 mediated metabolism of pesticides: from mouse to human. Rev. Toxicol. 2:1998;231-243
    • (1998) Rev. Toxicol. , vol.2 , pp. 231-243
    • Hodgson, E.1    Cherrington, N.2    Coleman, S.C.3    Liu, S.4    Falls, J.G.5    Cao, Y.6
  • 32
    • 1342323499 scopus 로고    scopus 로고
    • In vitro sulfoxidation of thioether compounds by human cytochrome P450 and flavin-containing monooxygenase isoforms with particular reference to the CYP2C subfamily
    • Usmani K.A., Karoly E.D., Hodgson E., Rose R.L. In vitro sulfoxidation of thioether compounds by human cytochrome P450 and flavin-containing monooxygenase isoforms with particular reference to the CYP2C subfamily. Drug Metab. Dispos. 32:2004;333-339
    • (2004) Drug Metab. Dispos. , vol.32 , pp. 333-339
    • Usmani, K.A.1    Karoly, E.D.2    Hodgson, E.3    Rose, R.L.4
  • 33
    • 0029348381 scopus 로고
    • Stereoselective sulfoxidation of the pesticide methiocarb by flavin-containing monooxygenase and cytochrome P450-dependent monooxygenases of rat liver microsomes. Anticholinesterase activity of the two sulfoxide enantiomers
    • Buronfosse T., Moroni P., Benoit E., Riviere J.L. Stereoselective sulfoxidation of the pesticide methiocarb by flavin-containing monooxygenase and cytochrome P450-dependent monooxygenases of rat liver microsomes. Anticholinesterase activity of the two sulfoxide enantiomers. J. Biochem. Toxicol. 10:1995;179-189
    • (1995) J. Biochem. Toxicol. , vol.10 , pp. 179-189
    • Buronfosse, T.1    Moroni, P.2    Benoit, E.3    Riviere, J.L.4
  • 34
    • 0034241811 scopus 로고    scopus 로고
    • Size limits of thiocarbamides accepted as substrates by human flavin-containing monooxygenase 1
    • Kim Y.M., Ziegler D.M. Size limits of thiocarbamides accepted as substrates by human flavin-containing monooxygenase 1. Drug Metab. Dispos. 28:2000;1003-1006
    • (2000) Drug Metab. Dispos. , vol.28 , pp. 1003-1006
    • Kim, Y.M.1    Ziegler, D.M.2
  • 35
    • 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. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:1976;248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 36
    • 0015881843 scopus 로고
    • A rapid micromethod for determination of FMN and FAD in mixtures
    • Fader E.J., Siegel L.M. A rapid micromethod for determination of FMN and FAD in mixtures. Anal. Biochem. 53:1973;332-336
    • (1973) Anal. Biochem. , vol.53 , pp. 332-336
    • Fader, E.J.1    Siegel, L.M.2
  • 37
    • 0029819905 scopus 로고    scopus 로고
    • Determination of nitric oxide synthase cofactors: Heme, FAD, FMN, and tetrahydrobiopterin
    • Klatt P., Schmidt K., Werner E.R., Mayer B. Determination of nitric oxide synthase cofactors: heme, FAD, FMN, and tetrahydrobiopterin. Methods Enzymol. 268:1996;358-365
    • (1996) Methods Enzymol. , vol.268 , pp. 358-365
    • Klatt, P.1    Schmidt, K.2    Werner, E.R.3    Mayer, B.4
  • 38
    • 0009255993 scopus 로고
    • Stereochemistry of oxygenation of organic sulphides with pig liver microsomal FAD-containing monooxygenase: Comparison with cytochrome P-450PB oxidations
    • Fujimori K., Matsuura T., Mikami A., Watanabe Y., Oae S., Iyanagi T. Stereochemistry of oxygenation of organic sulphides with pig liver microsomal FAD-containing monooxygenase: comparison with cytochrome P-450PB oxidations. J. Chem. Soc., Perkin Trans. 1:1990;1435-1440
    • (1990) J. Chem. Soc., Perkin Trans. , vol.1 , pp. 1435-1440
    • Fujimori, K.1    Matsuura, T.2    Mikami, A.3    Watanabe, Y.4    Oae, S.5    Iyanagi, T.6
  • 39
    • 0025038595 scopus 로고
    • Stereoselective S-oxygenation of 2-aryl-1,4-dithiolanes by the flavin-containing and cytochrome P450 monooxygenases
    • Cashman J.R., Olsen L.D. Stereoselective S-oxygenation of 2-aryl-1,4-dithiolanes by the flavin-containing and cytochrome P450 monooxygenases. Mol. Pharmacol. 38:1990;573-585
    • (1990) Mol. Pharmacol. , vol.38 , pp. 573-585
    • Cashman, J.R.1    Olsen, L.D.2
  • 40
    • 0028812229 scopus 로고
    • Chiral sulfoxidation of albendazole by the flavin adenine dinucleotide-containing and cytochrome P450-dependent monooxygenases from rat liver microsomes
    • Moroni P., Buronfosse T., Longin-Sauvageon C., Delatour P., Benoit E. Chiral sulfoxidation of albendazole by the flavin adenine dinucleotide- containing and cytochrome P450-dependent monooxygenases from rat liver microsomes. Drug Metab. Dispos. 23:1995;160-165
    • (1995) Drug Metab. Dispos. , vol.23 , pp. 160-165
    • Moroni, P.1    Buronfosse, T.2    Longin-Sauvageon, C.3    Delatour, P.4    Benoit, E.5
  • 41
    • 0343624354 scopus 로고
    • Functional groups bearing sulfur
    • Jakoby WB, Bend JR, Caldwell J, editors. New York: Academic Press;
    • Ziegler DM. Functional groups bearing sulfur. In: Jakoby WB, Bend JR, Caldwell J, editors. Metabolism of functional groups. New York: Academic Press; 1982. p. 171-84.
    • (1982) Metabolism of Functional Groups , pp. 171-184
    • Ziegler, D.M.1
  • 43
    • 0001977860 scopus 로고
    • Metabolic oxygenation of organic nitrogen and sulfur compounds
    • Mitchell JR, Horning MG, editors. New York: Raven Press;
    • Ziegler DM. Metabolic oxygenation of organic nitrogen and sulfur compounds. In: Mitchell JR, Horning MG, editors. Drug metabolism and toxicity. New York: Raven Press; 1984. p. 33-53.
    • (1984) Drug Metabolism and Toxicity , pp. 33-53
    • Ziegler, D.M.1
  • 44
    • 0000645518 scopus 로고
    • Further studies on the metabolism of thimet by plants, insects, and mammals
    • Bowman J.S., Casida J.E. Further studies on the metabolism of thimet by plants, insects, and mammals. J. Econ. Entomol. 51:1958;838-843
    • (1958) J. Econ. Entomol. , vol.51 , pp. 838-843
    • Bowman, J.S.1    Casida, J.E.2
  • 45
    • 0037478407 scopus 로고    scopus 로고
    • Human extrahepatic cytochromes P450: Function in xenobiotic metabolism and tissue-selective chemical toxicity in the respiratory and gastrointestinal tracts
    • Ding X., Kaminsky L.S. Human extrahepatic cytochromes P450: function in xenobiotic metabolism and tissue-selective chemical toxicity in the respiratory and gastrointestinal tracts. Annu. Rev. Pharmacol. Toxicol. 43:2003;149-173
    • (2003) Annu. Rev. Pharmacol. Toxicol. , vol.43 , pp. 149-173
    • Ding, X.1    Kaminsky, L.S.2
  • 46
    • 0036401287 scopus 로고    scopus 로고
    • Expression and regulation of xenobiotic-metabolizing cytochrome P450 (CYP) enzymes in human lung
    • Hukkanen J., Pelkonen O., Hakkola J., Raunio H. Expression and regulation of xenobiotic-metabolizing cytochrome P450 (CYP) enzymes in human lung. Crit. Rev. Toxicol. 32:2002;391-411
    • (2002) Crit. Rev. Toxicol. , vol.32 , pp. 391-411
    • Hukkanen, J.1    Pelkonen, O.2    Hakkola, J.3    Raunio, H.4
  • 47
    • 2442686708 scopus 로고    scopus 로고
    • Human flavin-containing monooxygenase form 2S-oxygenation: Sulfenic acid formation from thioureas and oxidation of glutathione
    • Henderson M.C., Krueger S.K., Stevens J.F., Williams D.E. Human flavin-containing monooxygenase form 2S-oxygenation: sulfenic acid formation from thioureas and oxidation of glutathione. Chem. Res. Toxicol. 17:2004;633-640
    • (2004) Chem. Res. Toxicol. , vol.17 , pp. 633-640
    • Henderson, M.C.1    Krueger, S.K.2    Stevens, J.F.3    Williams, D.E.4


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