메뉴 건너뛰기




Volumn 26, Issue 2, 2002, Pages 149-156

Effects of dimethoate and beta-naphthoflavone on selected biomarkers of Poecilia reticulata

Author keywords

Beta naphthoflavone; Biomarkers; Organophosphate pesticides; Poecilia reticulata

Indexed keywords

ACETYLCHOLINESTERASE; ADENOSINE TRIPHOSPHATASE (POTASSIUM SODIUM); ADENOSINE TRIPHOSPHATASE (POTASSIUM); BETA NAPHTHOFLAVONE; BIOLOGICAL MARKER; CYTOCHROME P450 1A; DIMETHOATE; ENZYME; ETHOXYRESORUFIN DEETHYLASE; GLUTATHIONE TRANSFERASE; LACTATE DEHYDROGENASE; ORGANOPHOSPHATE PESTICIDE; UNSPECIFIC MONOOXYGENASE;

EID: 0141831158     PISSN: 09201742     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1025457831923     Document Type: Article
Times cited : (236)

References (40)
  • 1
    • 0031733938 scopus 로고    scopus 로고
    • Liver glutathione content and glutathione-dependent enzymes of two species of freshwater fish as bioindicators of chemical pollution
    • Almar, M., Otero, L., Santos, C. and González Gallego, J. 1998. Liver glutathione content and glutathione-dependent enzymes of two species of freshwater fish as bioindicators of chemical pollution. J. Environ. Sci. Health B33: 769-783.
    • (1998) J. Environ. Sci. Health , vol.B33 , pp. 769-783
    • Almar, M.1    Otero, L.2    Santos, C.3    González Gallego, J.4
  • 3
    • 0030952629 scopus 로고    scopus 로고
    • In vivo and in vitro effects of deltamethrin on cytochrome P450 monooxygenase activity in carp (Cyprinus carpio L.) liver
    • Banka, L., Deér, K.A., Nemcsók, J. and Ábrahám, M. 1997. In vivo and in vitro effects of deltamethrin on cytochrome P450 monooxygenase activity in carp (Cyprinus carpio L.) liver. J. Environ. Sci. Health B32: 789-802.
    • (1997) J. Environ. Sci. Health , vol.B32 , pp. 789-802
    • Banka, L.1    Deér, K.A.2    Nemcsók, J.3    Ábrahám, M.4
  • 4
    • 0032926189 scopus 로고    scopus 로고
    • Effect of acute exposure of the organophosphate insecticide Rogor on some biochemical aspects of Clarias batrachus (Linnaeus)
    • Begum, G. and Vijayaraghavan, S. 1999. Effect of acute exposure of the organophosphate insecticide Rogor on some biochemical aspects of Clarias batrachus (Linnaeus). Environ. Res. A80: 80-83.
    • (1999) Environ. Res. , vol.A80 , pp. 80-83
    • Begum, G.1    Vijayaraghavan, S.2
  • 5
    • 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. 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.1
  • 6
    • 0029098924 scopus 로고
    • Induction of cytochrome P450 as a biomarker for environmental contamination in aquatic ecosystems
    • Bucheli, T.D. and Fent, K. 1995. Induction of cytochrome P450 as a biomarker for environmental contamination in aquatic ecosystems. Crit. Rev. Environ. Sci. Technol. 25: 201-268.
    • (1995) Crit. Rev. Environ. Sci. Technol. , vol.25 , pp. 201-268
    • Bucheli, T.D.1    Fent, K.2
  • 7
    • 0027300220 scopus 로고
    • Inhibition and inactivation of constitutive cytochromes P450 in rat liver by parathion
    • Butler, A.M. and Murray, M. 1993. Inhibition and inactivation of constitutive cytochromes P450 in rat liver by parathion. Mol. Pharmacol. 43: 902-908.
    • (1993) Mol. Pharmacol. , vol.43 , pp. 902-908
    • Butler, A.M.1    Murray, M.2
  • 8
    • 0023223310 scopus 로고
    • The occurrence of chemically induced hormesis
    • Calabrese, E.J., McCarthy, M.E. and Kenyon, E. 1987. The occurrence of chemically induced hormesis. Health Phys. 52: 531-541.
    • (1987) Health Phys. , vol.52 , pp. 531-541
    • Calabrese, E.J.1    McCarthy, M.E.2    Kenyon, E.3
  • 9
    • 0033547382 scopus 로고    scopus 로고
    • Negative regulation of rat GST-Ya gene via antioxidant/electrophile response element is directed by a C/EBP-like site
    • Chen, Y.-H. and Ramos, K.S. 1999. Negative regulation of rat GST-Ya gene via antioxidant/electrophile response element is directed by a C/EBP-like site. Biochem. Biophys. Res. Commun. 265: 18-23.
    • (1999) Biochem. Biophys. Res. Commun. , vol.265 , pp. 18-23
    • Chen, Y.-H.1    Ramos, K.S.2
  • 10
    • 0029941410 scopus 로고    scopus 로고
    • Branchial Na-K-ATPase and osmoregulation in the purple shore crab, Hemigrapsus nudus (Dana)
    • Corotto, F.S. and Holliday, C.W. 1996. Branchial Na-K-ATPase and osmoregulation in the purple shore crab, Hemigrapsus nudus (Dana). Comp. Biochem. Physiol. 113A: 361-368.
    • (1996) Comp. Biochem. Physiol. , vol.113 A , pp. 361-368
    • Corotto, F.S.1    Holliday, C.W.2
  • 11
    • 0027499909 scopus 로고
    • Inhibition of acetylcholinesterase and acute toxicity of organophosphorus compounds to fish: A preliminary structure-activity analysis
    • De Bruijn, J. and Hermens, J. 1993. Inhibition of acetylcholinesterase and acute toxicity of organophosphorus compounds to fish: A preliminary structure-activity analysis. Aquat. Toxicol. 24: 257-274.
    • (1993) Aquat. Toxicol. , vol.24 , pp. 257-274
    • De Bruijn, J.1    Hermens, J.2
  • 12
    • 0034804762 scopus 로고    scopus 로고
    • Lactate dehydrogenase activity - An effective parameter in aquatic toxicity tests
    • Diamantino, T.C., Almeida, E., Soares, A.M.V.M. and Guilhermino, L. 2001. Lactate dehydrogenase activity - An effective parameter in aquatic toxicity tests. Chemosphere 45: 553-560.
    • (2001) Chemosphere , vol.45 , pp. 553-560
    • Diamantino, T.C.1    Almeida, E.2    Soares, A.M.V.M.3    Guilhermino, L.4
  • 13
    • 33644811612 scopus 로고
    • A new and rapid colorimetric determination of acetylcholinesterase activity
    • Ellman, G.L., Courtney, K.D., Andres, V. and Featherstone, R.M. 1961. A new and rapid colorimetric determination of acetylcholinesterase activity. Biochem. Pharmacol. 7: 88-95.
    • (1961) Biochem. Pharmacol. , vol.7 , pp. 88-95
    • Ellman, G.L.1    Courtney, K.D.2    Andres, V.3    Featherstone, R.M.4
  • 15
    • 0032076184 scopus 로고    scopus 로고
    • Laboratory and field-caging studies on hepatic enzymatic activities in european eel and rainbow trout
    • Fenet, H., Casellas, C. and Bontoux, J. 1998. Laboratory and field-caging studies on hepatic enzymatic activities in european eel and rainbow trout. Ecotoxicol. Environ. Saf. 40: 137-143.
    • (1998) Ecotoxicol. Environ. Saf. , vol.40 , pp. 137-143
    • Fenet, H.1    Casellas, C.2    Bontoux, J.3
  • 16
    • 0032101527 scopus 로고    scopus 로고
    • Effect of methidathion on the cytochrome P-450 1A in the cyprinid fish gudgeon (Gobio gobio)
    • Flammarion, P., Migeon, B., Urios, S., Morfin, P. and Garric, J. 1998. Effect of methidathion on the cytochrome P-450 1A in the cyprinid fish gudgeon (Gobio gobio). Aquat. Toxicol. 42: 93-102.
    • (1998) Aquat. Toxicol. , vol.42 , pp. 93-102
    • Flammarion, P.1    Migeon, B.2    Urios, S.3    Morfin, P.4    Garric, J.5
  • 17
    • 0035166230 scopus 로고    scopus 로고
    • Acetylcholinesterase inhibition in estuarine fish and invertebrates as an indicator of organophosphorus insecticide exposure and effects
    • Fulton, M.H. and Key, P.B. 2001. Acetylcholinesterase inhibition in estuarine fish and invertebrates as an indicator of organophosphorus insecticide exposure and effects. Environ. Toxicol. Chem. 20: 37-45.
    • (2001) Environ. Toxicol. Chem. , vol.20 , pp. 37-45
    • Fulton, M.H.1    Key, P.B.2
  • 18
    • 0031902370 scopus 로고    scopus 로고
    • Should the use of inhibition of cholinesterases as a specific biomarker for organophosphate and carbamate pesticides be questioned?
    • Guilhermino, L., Barros, P., Silva, M.C. and Soares, A.M.V.M. 1998. Should the use of inhibition of cholinesterases as a specific biomarker for organophosphate and carbamate pesticides be questioned? Biomarkers 3: 157-163.
    • (1998) Biomarkers , vol.3 , pp. 157-163
    • Guilhermino, L.1    Barros, P.2    Silva, M.C.3    Soares, A.M.V.M.4
  • 19
    • 0034689161 scopus 로고    scopus 로고
    • In vitro and in vivo inhibition of Daphnia magna acetylcholinesterase by surfactant agents: Possible implications for contamination biomonitoring
    • Guilhermino, L., Lacerda, M.N., Nogueira, A.J.A. and Soares, A.M.V.M. 2000. In vitro and in vivo inhibition of Daphnia magna acetylcholinesterase by surfactant agents: Possible implications for contamination biomonitoring. Sci. Total Environ. 247: 137-141.
    • (2000) Sci. Total Environ. , vol.247 , pp. 137-141
    • Guilhermino, L.1    Lacerda, M.N.2    Nogueira, A.J.A.3    Soares, A.M.V.M.4
  • 20
    • 0030032490 scopus 로고    scopus 로고
    • Inhibition of acetylcholinesterase activity as effect criterion in acute tests with juvenile Daphnia magna
    • Guilhermino, L., Lopes, M.C., Carvalho, A.P. and Soares, A.M.V.M. 1996. Inhibition of acetylcholinesterase activity as effect criterion in acute tests with juvenile Daphnia magna. Chemosphere 32: 727-738.
    • (1996) Chemosphere , vol.32 , pp. 727-738
    • Guilhermino, L.1    Lopes, M.C.2    Carvalho, A.P.3    Soares, A.M.V.M.4
  • 21
    • 0016275313 scopus 로고
    • Glutathione S-transferases - The first enzymatic step in mercapturic acid formation
    • Habig, W.H., Pabst, M.J. and Jakoby, W.B. 1974. Glutathione S-transferases - The first enzymatic step in mercapturic acid formation. J. Biol. Chem. 249: 7130-7139.
    • (1974) J. Biol. Chem. , vol.249 , pp. 7130-7139
    • Habig, W.H.1    Pabst, M.J.2    Jakoby, W.B.3
  • 24
    • 0002675904 scopus 로고    scopus 로고
    • In vitro and in vivo studies of potential biomarkers of lead and uranium contamination: Lipid peroxidation, acetylcholinesterase, catalase and glutathione peroxidase activities in three non-mammalian species
    • Labrot, F., Ribera, D., Saint Denis, M. and Narbonne, J.F. 1996. In vitro and in vivo studies of potential biomarkers of lead and uranium contamination: Lipid peroxidation, acetylcholinesterase, catalase and glutathione peroxidase activities in three non-mammalian species. Biomarkers 1: 21-28.
    • (1996) Biomarkers , vol.1 , pp. 21-28
    • Labrot, F.1    Ribera, D.2    Saint Denis, M.3    Narbonne, J.F.4
  • 26
    • 0026693922 scopus 로고
    • Molecular studies of the phase II xenobiotic conjugative enzymes of marine Pleuronectid flatfish
    • Leaver, M.J., Clarke, D.J. and George, S.G. 1992. Molecular studies of the phase II xenobiotic conjugative enzymes of marine Pleuronectid flatfish. Aquat. Toxicol. 22: 265-278.
    • (1992) Aquat. Toxicol. , vol.22 , pp. 265-278
    • Leaver, M.J.1    Clarke, D.J.2    George, S.G.3
  • 27
    • 0028001171 scopus 로고
    • Kinetic parameters of desulfuration and dearylation of parathion and chlorpyrifos by rat liver microsomes
    • Ma, T. and Chambers, J.E. 1994. Kinetic parameters of desulfuration and dearylation of parathion and chlorpyrifos by rat liver microsomes. Fd Chem. Toxic. 32: 763-767.
    • (1994) Fd Chem. Toxic. , vol.32 , pp. 763-767
    • Ma, T.1    Chambers, J.E.2
  • 29
    • 0034526229 scopus 로고    scopus 로고
    • Changes in carbohydrate metabolism in hemolymph and fat body of the silkworm, Bombyx mori L., exposed to organophosphorus insecticides
    • Nath, B.S. 2000. Changes in carbohydrate metabolism in hemolymph and fat body of the silkworm, Bombyx mori L., exposed to organophosphorus insecticides. Pestic. Biochem. Physiol. 68: 127-137.
    • (2000) Pestic. Biochem. Physiol. , vol.68 , pp. 127-137
    • Nath, B.S.1
  • 32
    • 0033135583 scopus 로고    scopus 로고
    • Effects of 2,4-diamin on some parameters of protein and carbohydrate metabolisms in the serum, muscle and liver of Cyprinus carpio
    • Oruç, E.Ö. and Üner, N. 1999. Effects of 2,4-diamin on some parameters of protein and carbohydrate metabolisms in the serum, muscle and liver of Cyprinus carpio. Environ. Poll. 105: 267-272.
    • (1999) Environ. Poll. , vol.105 , pp. 267-272
    • Oruç, E.Ö.1    Üner, N.2
  • 34
    • 0024377341 scopus 로고
    • Glutathione S-transferases: Gene structure, regulation, and biological function
    • Pickett, C.B. and Lu, A.Y.H. 1989. Glutathione S-transferases: Gene structure, regulation, and biological function. Annu. Rev. Biochem. 58: 743-64.
    • (1989) Annu. Rev. Biochem. , vol.58 , pp. 743-764
    • Pickett, C.B.1    Lu, A.Y.H.2
  • 36
    • 0032193147 scopus 로고    scopus 로고
    • In vivo inhibition of AChE activity in the european eel Anguilla anguilla exposed to technical grade fenitrothion
    • Sancho, E., Ferrando, M.D. and Andreu, E. 1998. In vivo inhibition of AChE activity in the european eel Anguilla anguilla exposed to technical grade fenitrothion. Comp. Biochem. Physiol. C 120: 389-395.
    • (1998) Comp. Biochem. Physiol. C , vol.120 , pp. 389-395
    • Sancho, E.1    Ferrando, M.D.2    Andreu, E.3
  • 37
    • 0030456796 scopus 로고    scopus 로고
    • Biomonitoring of aquatic pollution with feral eel (Anguilla anguilla), II. Biomarkers: Pollution-induced biochemical responses
    • Van Der Oost, R., Goksøyr, A., Celander, M., Heida, H. and Vermeulen, N.P.E. 1996. Biomonitoring of aquatic pollution with feral eel (Anguilla anguilla), II. Biomarkers: Pollution-induced biochemical responses. Aquat. Toxicol. 36: 189-222.
    • (1996) Aquat. Toxicol. , vol.36 , pp. 189-222
    • Van Der Oost, R.1    Goksøyr, A.2    Celander, M.3    Heida, H.4    Vermeulen, N.P.E.5
  • 38
    • 0000191753 scopus 로고
    • Lactate dehydrogenase
    • Third Edition, Academic Press, New York
    • Vassault, A. 1983. Lactate dehydrogenase. In: Methods of Enzymatic Analysis, Vol. III, pp. 118-126. Third Edition, Academic Press, New York.
    • (1983) Methods of Enzymatic Analysis , vol.3 , pp. 118-126
    • Vassault, A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.