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Volumn 1679, Issue 1, 2004, Pages 29-36

Molecular identification and expression of two non-P450 enzymes, monoamine oxidase a and flavin-containing monooxygenase 2, involved in phase I of xenobiotic biotransformation in the Pacific oyster, Crassostrea gigas

Author keywords

Crassostrea gigas; FAD; flavin adenine dinucleotide; flavin containing monooxygenase 2; Flavin containing monooxygenase 2; FMO 2; glutathione S transferase; GST; MAO A; messenger RNA; Monoamine oxidase A; monoamine oxidase A; mRNA; NADP

Indexed keywords

AMINE OXIDASE (FLAVIN CONTAINING); AMINE OXIDASE (FLAVIN CONTAINING) ISOENZYME A; ATRAZINE; COMPLEMENTARY DNA; CYTOCHROME P450; DIURON; GLYPHOSATE; HYDROCARBON; ISOPROTURON; MESSENGER RNA; QUERCETIN; UNSPECIFIC MONOOXYGENASE;

EID: 3042774163     PISSN: 01674781     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbaexp.2004.04.001     Document Type: Article
Times cited : (34)

References (40)
  • 1
    • 20244385761 scopus 로고    scopus 로고
    • Molecular identification and expression of Heat Shock Cognate (hsc70) and Heat Shock Protein (hsp70) genes in the Pacific oyster Crassostrea gigas
    • Boutet I., Tanguy A., Rousseau S., Auffret M., Moraga D. Molecular identification and expression of Heat Shock Cognate (hsc70) and Heat Shock Protein (hsp70) genes in the Pacific oyster Crassostrea gigas. Cell Stress Chaperones. 8:2003;76-85
    • (2003) Cell Stress Chaperones , vol.8 , pp. 76-85
    • Boutet, I.1    Tanguy, A.2    Rousseau, S.3    Auffret, M.4    Moraga, D.5
  • 2
    • 0035501764 scopus 로고    scopus 로고
    • Cloning of a metallothionein gene and characterization of two other cDNA sequences of the Pacific oyster Crassostrea gigas
    • Tanguy A., Mura C., Moraga D. Cloning of a metallothionein gene and characterization of two other cDNA sequences of the Pacific oyster Crassostrea gigas. Aquat. Toxicol. 55:2001;35-47
    • (2001) Aquat. Toxicol. , vol.55 , pp. 35-47
    • Tanguy, A.1    Mura, C.2    Moraga, D.3
  • 3
    • 0035948613 scopus 로고    scopus 로고
    • Cloning and characterization of a gene coding for a novel metallothionein in the Pacific oyster Crassostrea gigas (CgMT2): A case of adaptive response to metal-induced stress?
    • Tanguy A., Moraga D. Cloning and characterization of a gene coding for a novel metallothionein in the Pacific oyster Crassostrea gigas (CgMT2): a case of adaptive response to metal-induced stress? Gene. 273:2001;123-130
    • (2001) Gene , vol.273 , pp. 123-130
    • Tanguy, A.1    Moraga, D.2
  • 4
    • 0036873726 scopus 로고    scopus 로고
    • Polymorphism of metallothionein genes in the Pacific oyster Crassostrea gigas as a biomarker of response to metal exposure
    • Tanguy A., Boutet I., Bonhomme F., Boudry P., Moraga D. Polymorphism of metallothionein genes in the Pacific oyster Crassostrea gigas as a biomarker of response to metal exposure. Biomarkers. 7:2002;439-450
    • (2002) Biomarkers , vol.7 , pp. 439-450
    • Tanguy, A.1    Boutet, I.2    Bonhomme, F.3    Boudry, P.4    Moraga, D.5
  • 5
    • 0036590259 scopus 로고    scopus 로고
    • Immunochemical quantification of metallothioneins in marine mollusks: Characterization of a metal exposure bioindicator
    • Boutet I., Tanguy A., Auffret M., Riso R., Moraga D. Immunochemical quantification of metallothioneins in marine mollusks: characterization of a metal exposure bioindicator. Environ. Toxicol. Chem. 21:2002;1009-1014
    • (2002) Environ. Toxicol. Chem. , vol.21 , pp. 1009-1014
    • Boutet, I.1    Tanguy, A.2    Auffret, M.3    Riso, R.4    Moraga, D.5
  • 6
    • 1642359206 scopus 로고    scopus 로고
    • Response of the Pacific oyster Crassostrea gigas to hydrocarbon contamination under experimental conditions
    • Boutet I., Tanguy A., Moraga D. Response of the Pacific oyster Crassostrea gigas to hydrocarbon contamination under experimental conditions. Gene. 329:2004;147-157
    • (2004) Gene , vol.329 , pp. 147-157
    • Boutet, I.1    Tanguy, A.2    Moraga, D.3
  • 7
    • 0031738746 scopus 로고    scopus 로고
    • Occurrence of flavin-containing monooxygenases in non-mammalian eukaryotic organisms
    • Schlenk D. Occurrence of flavin-containing monooxygenases in non-mammalian eukaryotic organisms. Comp. Biochem. Physiol. 121C:1998;185-195
    • (1998) Comp. Biochem. Physiol. , vol.121 , pp. 185-195
    • Schlenk, D.1
  • 9
    • 0030772328 scopus 로고    scopus 로고
    • The role of non-P450 enzymes in drug oxidation
    • Beedham C. The role of non-P450 enzymes in drug oxidation. Pharm. World Sci. 19:1997;255-263
    • (1997) Pharm. World Sci. , vol.19 , pp. 255-263
    • Beedham, C.1
  • 10
    • 0026808495 scopus 로고
    • Metabolism and mutagenic activation of benzo[a]pyrene by subcellular fractions from mussel (Mytilus galloprovincialis) digestive gland and sea bass (Dicenthrarcus labrax) liver
    • Michel X.R., Cassand P.M., Ribera D.G., Narbonne J.F. Metabolism and mutagenic activation of benzo[a]pyrene by subcellular fractions from mussel (Mytilus galloprovincialis) digestive gland and sea bass (Dicenthrarcus labrax) liver. Comp. Biochem. Physiol. 103C:1992;43-51
    • (1992) Comp. Biochem. Physiol. , vol.103 , pp. 43-51
    • Michel, X.R.1    Cassand, P.M.2    Ribera, D.G.3    Narbonne, J.F.4
  • 11
    • 0037290663 scopus 로고    scopus 로고
    • Fish bioaccumulation and biomarkers in environmental risk assessment: A review
    • Van der Oost R., Beyer J., Vermeulen N.P.E. Fish bioaccumulation and biomarkers in environmental risk assessment: a review. Environ. Toxicol. Pharmacol. 13:2003;57-149
    • (2003) Environ. Toxicol. Pharmacol. , vol.13 , pp. 57-149
    • Van Der Oost, R.1    Beyer, J.2    Vermeulen, N.P.E.3
  • 13
    • 0037047747 scopus 로고    scopus 로고
    • Identification of six mRNA sequences of genes related to multixenobiotic resistance (MXR) and biotransformation in Mytilus edulis
    • Lüdeking A., Köhler A. Identification of six mRNA sequences of genes related to multixenobiotic resistance (MXR) and biotransformation in Mytilus edulis. Mar. Ecol., Prog. Ser. 238:2002;115-124
    • (2002) Mar. Ecol., Prog. Ser. , vol.238 , pp. 115-124
    • Lüdeking, A.1    Köhler, A.2
  • 14
    • 0018801101 scopus 로고
    • The liver microsomal FAD-containing monooxygenase. Spectral characterization and kinetic studies
    • Poulsen L.L., Ziegler D.M. The liver microsomal FAD-containing monooxygenase. Spectral characterization and kinetic studies. J. Biol. Chem. 254:1979;6449-6455
    • (1979) J. Biol. Chem. , vol.254 , pp. 6449-6455
    • Poulsen, L.L.1    Ziegler, D.M.2
  • 15
    • 0021792408 scopus 로고
    • Exclusive activation of aromatic amines in the marine mussel Mytilus edulis by FAD-containing monooxygenase
    • Kurelec B. Exclusive activation of aromatic amines in the marine mussel Mytilus edulis by FAD-containing monooxygenase. Biochem. Biophys. Res. Commun. 127:1985;773-778
    • (1985) Biochem. Biophys. Res. Commun. , vol.127 , pp. 773-778
    • Kurelec, B.1
  • 16
    • 0023610918 scopus 로고
    • Metabolic activation of 2-aminofluorene, 2-acetylaminofluorene and N-hydroxy-acetylaminofluorene to bacterial mutagens with mussel (Mytilus galloprovincialis) and carp (Cyprinus carpio) subcellular preparations
    • Kurelec B., Krca S. Metabolic activation of 2-aminofluorene, 2-acetylaminofluorene and N-hydroxy-acetylaminofluorene to bacterial mutagens with mussel (Mytilus galloprovincialis) and carp (Cyprinus carpio) subcellular preparations. Comp. Biochem. Physiol. 88C:1987;171-177
    • (1987) Comp. Biochem. Physiol. , vol.88 , pp. 171-177
    • Kurelec, B.1    Krca, S.2
  • 17
    • 0024938730 scopus 로고
    • Xenobiotic biotransformation in the Pacific oyster Crassostrea gigas
    • Schlenk D., Buhler D.R. Xenobiotic biotransformation in the Pacific oyster Crassostrea gigas. Comp. Biochem. Physiol. 94C:1989;476-480
    • (1989) Comp. Biochem. Physiol. , vol.94 , pp. 476-480
    • Schlenk, D.1    Buhler, D.R.2
  • 18
    • 0025283613 scopus 로고
    • The in vitro biotransformation of 2-aminofluorene in the visceral mass of the Pacific oyster, Crassostrea gigas
    • Schlenk D., Buhler D.R. The in vitro biotransformation of 2-aminofluorene in the visceral mass of the Pacific oyster, Crassostrea gigas. Xenobiotica. 20:1990;563-572
    • (1990) Xenobiotica , vol.20 , pp. 563-572
    • Schlenk, D.1    Buhler, D.R.2
  • 19
    • 0035740329 scopus 로고    scopus 로고
    • Biotransformation of xenobiotics by amine oxidases
    • Strolin Benedetti M. Biotransformation of xenobiotics by amine oxidases. Fundam. Clin. Pharmacol. 15:2001;75-84
    • (2001) Fundam. Clin. Pharmacol. , vol.15 , pp. 75-84
    • Strolin Benedetti, M.1
  • 20
    • 0031898408 scopus 로고    scopus 로고
    • Structural aspects of monoamine oxidase and its reversible inhibition
    • Wouters J. Structural aspects of monoamine oxidase and its reversible inhibition. Curr. Med. Chem. 5:1998;137-162
    • (1998) Curr. Med. Chem. , vol.5 , pp. 137-162
    • Wouters, J.1
  • 21
    • 0022486442 scopus 로고
    • Serotonin metabolism and the nature of monoamine oxidase in squid central nervous system
    • Youdim M.B., Feldman S.C., Pappas G.D., Pollard H.B. Serotonin metabolism and the nature of monoamine oxidase in squid central nervous system. Brain Res. 381:1986;300-304
    • (1986) Brain Res. , vol.381 , pp. 300-304
    • Youdim, M.B.1    Feldman, S.C.2    Pappas, G.D.3    Pollard, H.B.4
  • 22
    • 0030133260 scopus 로고    scopus 로고
    • A comparative analysis of monoamine oxidase activity in the tissues of the deep-sea squid (Berryteuthis magister) and the mouse under normal and elevated atmospheric pressure
    • Antipov A.D., Kostkin V.B., Rozengart E.V., Epshtein L.M. A comparative analysis of monoamine oxidase activity in the tissues of the deep-sea squid (Berryteuthis magister) and the mouse under normal and elevated atmospheric pressure. Zh. Evol. Biokhim. Fiziol. 32:1996;233-240
    • (1996) Zh. Evol. Biokhim. Fiziol. , vol.32 , pp. 233-240
    • Antipov, A.D.1    Kostkin, V.B.2    Rozengart, E.V.3    Epshtein, L.M.4
  • 23
    • 0034954904 scopus 로고    scopus 로고
    • Induction of marine mollusc stress proteins by chemical or physical stress
    • Snyder M.J., Girvetz E., Mulder E.P. Induction of marine mollusc stress proteins by chemical or physical stress. Arch. Environ. Contam. Toxicol. 41:2001;22-29
    • (2001) Arch. Environ. Contam. Toxicol. , vol.41 , pp. 22-29
    • Snyder, M.J.1    Girvetz, E.2    Mulder, E.P.3
  • 24
    • 0027399530 scopus 로고
    • Identification of protein coding regions by database similarity search
    • Gish W., States D.J. Identification of protein coding regions by database similarity search. Nat. Genet. 3:1993;266-272
    • (1993) Nat. Genet. , vol.3 , pp. 266-272
    • Gish, W.1    States, D.J.2
  • 26
    • 0027245885 scopus 로고
    • Site-directed mutagenesis of monoamine oxidase a and B: Role of cysteines
    • Wu H.F., Chen K., Shih J.C. Site-directed mutagenesis of monoamine oxidase A and B: role of cysteines. Mol. Pharmacol. 43:1993;888-893
    • (1993) Mol. Pharmacol. , vol.43 , pp. 888-893
    • Wu, H.F.1    Chen, K.2    Shih, J.C.3
  • 27
    • 0031588975 scopus 로고    scopus 로고
    • Pulmonary flavin-containing monooxygenase (FMO) in rhesus macaque: Expression of FMO2 protein, mRNA 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, mRNA 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
  • 28
    • 0025219896 scopus 로고
    • The flavin-containing monooxygenase enzymes expressed in rabbit liver and lung are products of related but distinctly different genes
    • Lawton M.P., Gasser R., Tynes R.E., Hodgson E., Philpot R.M. The flavin-containing monooxygenase enzymes expressed in rabbit liver and lung are products of related but distinctly different genes. J. Biol. Chem. 265:1990;5855-5861
    • (1990) J. Biol. Chem. , vol.265 , pp. 5855-5861
    • Lawton, M.P.1    Gasser, R.2    Tynes, R.E.3    Hodgson, E.4    Philpot, R.M.5
  • 29
    • 0026937248 scopus 로고
    • Guinea pig or rabbit lung flavin-containing monooxygenases with distinct mobilities 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 mobilities 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
  • 31
    • 0023656025 scopus 로고
    • Cloning and sequence of rat myoadenylate deaminase cDNA. Evidence for tissue-specific and developmental regulation
    • Sabina R.L., Marquetant R., Desai N.M., Kaletha K., Holmes E.W. Cloning and sequence of rat myoadenylate deaminase cDNA. Evidence for tissue-specific and developmental regulation. J. Biol. Chem. 262:1987;12397-12400
    • (1987) J. Biol. Chem. , vol.262 , pp. 12397-12400
    • Sabina, R.L.1    Marquetant, R.2    Desai, N.M.3    Kaletha, K.4    Holmes, E.W.5
  • 32
    • 0023058975 scopus 로고
    • Conserved AU sequence from the 3′ untranslated region of GM-CSF mRNA mediates selective mRNA degradation
    • Shaw G., Kamen R.A. Conserved AU sequence from the 3′ untranslated region of GM-CSF mRNA mediates selective mRNA degradation. Cell. 46:1986;659-667
    • (1986) Cell , vol.46 , pp. 659-667
    • Shaw, G.1    Kamen, R.A.2
  • 33
    • 0028910282 scopus 로고
    • Cloning and characterization of a developmentally regulated sea urchin cDNA encoding glutamine synthetase
    • Fucci L., Piscopo A., Aniello F., Branno M., Di Gregorio A., Calogero R., Geraci G. Cloning and characterization of a developmentally regulated sea urchin cDNA encoding glutamine synthetase. Gene. 152:1995;205-208
    • (1995) Gene , vol.152 , pp. 205-208
    • Fucci, L.1    Piscopo, A.2    Aniello, F.3    Branno, M.4    Di Gregorio, A.5    Calogero, R.6    Geraci, G.7
  • 34
    • 0024297331 scopus 로고
    • Nucleotide sequence and glucocorticoid regulation of the mRNAs for the isoenzymes of rat aspartate aminotransferase
    • Pavé-Preux M., Ferry N., Bouguet J., Hanoune J., Barouki R. Nucleotide sequence and glucocorticoid regulation of the mRNAs for the isoenzymes of rat aspartate aminotransferase. J. Biol. Chem. 263:1988;17459-17466
    • (1988) J. Biol. Chem. , vol.263 , pp. 17459-17466
    • Pavé-Preux, M.1    Ferry, N.2    Bouguet, J.3    Hanoune, J.4    Barouki, R.5
  • 35
    • 0024995831 scopus 로고
    • Tissue distribution of human monoamine oxidase a and B mRNA
    • Grimsby J., Lan N.C., Neve R., Chen K., Shih J.C. Tissue distribution of human monoamine oxidase A and B mRNA. J. Neurochem. 55:1990;1166-1169
    • (1990) J. Neurochem. , vol.55 , pp. 1166-1169
    • Grimsby, J.1    Lan, N.C.2    Neve, R.3    Chen, K.4    Shih, J.C.5
  • 36
    • 0023894686 scopus 로고
    • Flavin-containing monooxygenases: Catalytic mechanism and substrate specificities
    • Ziegler D.M. Flavin-containing monooxygenases: catalytic mechanism and substrate specificities. Drug Metab. Rev. 19:1988;1-32
    • (1988) Drug Metab. Rev. , vol.19 , pp. 1-32
    • Ziegler, D.M.1
  • 37
    • 0027462628 scopus 로고
    • Recent studies on structure and function of multisubstrate flavin-containing monooxygenases
    • Ziegler D.M. Recent studies on structure and function of multisubstrate flavin-containing monooxygenases. Annu. Rev. Pharmacol. Toxicol. 33:1993;179-199
    • (1993) Annu. Rev. Pharmacol. Toxicol. , vol.33 , pp. 179-199
    • Ziegler, D.M.1
  • 38
    • 0010444218 scopus 로고
    • The mixed function oxygenase system in molluscs: Metabolism, responses to xenobiotics and toxicity
    • Livingstone D.R., Arnold R., Chipman K., Kirchin M.A., Marsh J. The mixed function oxygenase system in molluscs: metabolism, responses to xenobiotics and toxicity. Oceanis. 16:1990;331-347
    • (1990) Oceanis , vol.16 , pp. 331-347
    • Livingstone, D.R.1    Arnold, R.2    Chipman, K.3    Kirchin, M.A.4    Marsh, J.5
  • 39
    • 0031596694 scopus 로고    scopus 로고
    • Substrate regulation of monoamine oxidases
    • Ramsay R.R. Substrate regulation of monoamine oxidases. J. Neural Transm. 52:1998;139-147
    • (1998) J. Neural Transm. , vol.52 , pp. 139-147
    • Ramsay, R.R.1
  • 40
    • 0029925564 scopus 로고    scopus 로고
    • Monoamine oxidase B expression is selectively regulated by dexamethasone in cultured rat astrocytes
    • Carlo P., Violani E., Del Rio M., Olasmaa M., Santagati S., Maggi A., Picotti G.B. Monoamine oxidase B expression is selectively regulated by dexamethasone in cultured rat astrocytes. Brain Res. 711:1996;175-183
    • (1996) Brain Res. , vol.711 , pp. 175-183
    • Carlo, P.1    Violani, E.2    Del Rio, M.3    Olasmaa, M.4    Santagati, S.5    Maggi, A.6    Picotti, G.B.7


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