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Volumn 221, Issue 2, 2007, Pages 243-250

Concentration-dependent interactions of the organophosphates chlorpyrifos oxon and methyl paraoxon with human recombinant acetylcholinesterase

Author keywords

Acetylcholinesterase; Chlorpyrifos oxon; Methyl paraoxon; Organophosphorus insecticides

Indexed keywords

ACETLYTHIOCHOLINE; CHLORPYRIFOS OXON; METHYLPARAOXON; ORGANOPHOSPHATE; RECOMBINANT ACETYLCHOLINESTERASE; RECOMBINANT ENZYME; THIOCHOLINE; UNCLASSIFIED DRUG;

EID: 34248510057     PISSN: 0041008X     EISSN: 10960333     Source Type: Journal    
DOI: 10.1016/j.taap.2007.03.013     Document Type: Article
Times cited : (19)

References (27)
  • 1
    • 0028845803 scopus 로고
    • Allosteric modulation of acetylcholinesterase activity by peripheral ligands involves a conformational transition of the anionic subsite
    • Barak D., Ordentlich A., Bromberg A., Kronman C., Marcus D., Lazar A., Ariel N., Velam B., and Shafferman A. Allosteric modulation of acetylcholinesterase activity by peripheral ligands involves a conformational transition of the anionic subsite. Biochemistry 34 (1995) 15444-15452
    • (1995) Biochemistry , vol.34 , pp. 15444-15452
    • Barak, D.1    Ordentlich, A.2    Bromberg, A.3    Kronman, C.4    Marcus, D.5    Lazar, A.6    Ariel, N.7    Velam, B.8    Shafferman, A.9
  • 2
    • 0037413712 scopus 로고    scopus 로고
    • Structural insights into ligand interactions at the acetylcholinesterase peripheral anionic site
    • Bourne Y., Taylor P., Radić Z.A., and Marchot P. Structural insights into ligand interactions at the acetylcholinesterase peripheral anionic site. EMBO 22 (2003) 1-12
    • (2003) EMBO , vol.22 , pp. 1-12
    • Bourne, Y.1    Taylor, P.2    Radić, Z.A.3    Marchot, P.4
  • 4
    • 0037138487 scopus 로고    scopus 로고
    • Acceleration of Drosophila melanogaster acetylcholinesterase methanesulfonylation: peripheral ligand d-tubocurarine enhances the affinity for small methanesulfonylfluoride
    • Golicnik M.D., Fournier D., and Stojan J. Acceleration of Drosophila melanogaster acetylcholinesterase methanesulfonylation: peripheral ligand d-tubocurarine enhances the affinity for small methanesulfonylfluoride. Chem.-Biol. Interact. 139 (2002) 145-157
    • (2002) Chem.-Biol. Interact. , vol.139 , pp. 145-157
    • Golicnik, M.D.1    Fournier, D.2    Stojan, J.3
  • 5
    • 0024587408 scopus 로고
    • Analysis of kinetic data for irreversible enzyme inhibition
    • Gray P.J., and Duggleby R.G. Analysis of kinetic data for irreversible enzyme inhibition. Biochem. J. 257 2 (1989) 419-424
    • (1989) Biochem. J. , vol.257 , Issue.2 , pp. 419-424
    • Gray, P.J.1    Duggleby, R.G.2
  • 6
    • 0015789712 scopus 로고
    • Recording spectrophotometric method for determination of dissociation and phosphorylation constants for the inhibition of acetylcholinesterase by organophosphates in the presence of substrate
    • Hart G.J., and O'Brien R.D. Recording spectrophotometric method for determination of dissociation and phosphorylation constants for the inhibition of acetylcholinesterase by organophosphates in the presence of substrate. Biochemistry 12 15 (1973) 2940-2945
    • (1973) Biochemistry , vol.12 , Issue.15 , pp. 2940-2945
    • Hart, G.J.1    O'Brien, R.D.2
  • 7
    • 0038219567 scopus 로고    scopus 로고
    • Unmasking tandem site interaction in human acetylcholinesterase. Substrate activation with cationic acetanilide substrate
    • Johnson J.L., Cusack B., Davies M.P., Fauq A., and Rosenberry T.L. Unmasking tandem site interaction in human acetylcholinesterase. Substrate activation with cationic acetanilide substrate. Biochemistry 42 (2003) 5438-5452
    • (2003) Biochemistry , vol.42 , pp. 5438-5452
    • Johnson, J.L.1    Cusack, B.2    Davies, M.P.3    Fauq, A.4    Rosenberry, T.L.5
  • 8
    • 0033735721 scopus 로고    scopus 로고
    • Interactions of the organophosphates paraoxon and methyl paraoxon with mouse brain acetylcholinesterase
    • Kardos S.A., and Sultatos L.G. Interactions of the organophosphates paraoxon and methyl paraoxon with mouse brain acetylcholinesterase. Toxicol. Sci. 58 (2000) 118-126
    • (2000) Toxicol. Sci. , vol.58 , pp. 118-126
    • Kardos, S.A.1    Sultatos, L.G.2
  • 9
    • 4344616457 scopus 로고    scopus 로고
    • Comparison of chlorpyrifos-oxon and paraoxon acetylcholinesterase inhibition dynamics: potential role of a peripheral binding site
    • Kousba S.A., Sultatos L.G., Poet T.S., and Timchalk C. Comparison of chlorpyrifos-oxon and paraoxon acetylcholinesterase inhibition dynamics: potential role of a peripheral binding site. Toxicol. Sci. 80 (2004) 239-248
    • (2004) Toxicol. Sci. , vol.80 , pp. 239-248
    • Kousba, S.A.1    Sultatos, L.G.2    Poet, T.S.3    Timchalk, C.4
  • 10
    • 0022453407 scopus 로고
    • Determination of rate constants for the irreversible inhibition of acetylcholine esterase by continuously monitoring the substrate reaction in the presence of the inhibitor
    • Lin W., and Tsou C.L. Determination of rate constants for the irreversible inhibition of acetylcholine esterase by continuously monitoring the substrate reaction in the presence of the inhibitor. Biochim. Biophys. Acta 870 (1986) 185-190
    • (1986) Biochim. Biophys. Acta , vol.870 , pp. 185-190
    • Lin, W.1    Tsou, C.L.2
  • 11
    • 0001242480 scopus 로고
    • Affinity and phosphorylation constants for the inhibition of esterases by organophosphates
    • Main A.R. Affinity and phosphorylation constants for the inhibition of esterases by organophosphates. Sci. 144 (1964) 992-993
    • (1964) Sci. , vol.144 , pp. 992-993
    • Main, A.R.1
  • 12
    • 0034604236 scopus 로고    scopus 로고
    • Acetylthiocholine binds to Asp74 at the peripheral site of human acetylcholinesterase as the first step in the catalytic pathway
    • Mallender W.D., Szegletes T., and Rosenberry T.L. Acetylthiocholine binds to Asp74 at the peripheral site of human acetylcholinesterase as the first step in the catalytic pathway. Biochemistry 39 26 (2000) 7753-7763
    • (2000) Biochemistry , vol.39 , Issue.26 , pp. 7753-7763
    • Mallender, W.D.1    Szegletes, T.2    Rosenberry, T.L.3
  • 13
    • 0034697035 scopus 로고    scopus 로고
    • Exploration of the Drosophila acetylcholinesterase substrate activation site using a reversible inhibitor (Triton X-100) and mutated enzymes
    • Marcel V.S., Estrada-Mondaca S., Magne F., Stojan J., Klaebe A., and Fournier D. Exploration of the Drosophila acetylcholinesterase substrate activation site using a reversible inhibitor (Triton X-100) and mutated enzymes. J. Biol. Chem. 275 (2000) 11603-11609
    • (2000) J. Biol. Chem. , vol.275 , pp. 11603-11609
    • Marcel, V.S.1    Estrada-Mondaca, S.2    Magne, F.3    Stojan, J.4    Klaebe, A.5    Fournier, D.6
  • 14
    • 0034495240 scopus 로고    scopus 로고
    • Rates of spontaneous reactivation and aging of acetylcholinesterase in human erythrocytes after inhibition by organophosphorus pesticides
    • Masson H.J., Sains C., Stevenson A.J., and Rawbone R. Rates of spontaneous reactivation and aging of acetylcholinesterase in human erythrocytes after inhibition by organophosphorus pesticides. Hum. Exp. Toxicol. 19 (2000) 511-516
    • (2000) Hum. Exp. Toxicol. , vol.19 , pp. 511-516
    • Masson, H.J.1    Sains, C.2    Stevenson, A.J.3    Rawbone, R.4
  • 16
    • 0033002756 scopus 로고    scopus 로고
    • The influence of peripheral site ligands on the reaction of symmetric and chiral organophosphates with wildtype and mutant acetylcholinesterases
    • Radić Z., and Taylor P. The influence of peripheral site ligands on the reaction of symmetric and chiral organophosphates with wildtype and mutant acetylcholinesterases. Chem.-Biol. Interact. 119-120 (1999) 111-117
    • (1999) Chem.-Biol. Interact. , vol.119-120 , pp. 111-117
    • Radić, Z.1    Taylor, P.2
  • 17
    • 0012512277 scopus 로고    scopus 로고
    • Peripheral site ligands accelerate inhibition of acetylcholinesterase by neutral organophosphates
    • Radić Z., and Taylor P. Peripheral site ligands accelerate inhibition of acetylcholinesterase by neutral organophosphates. J. Appl. Toxicol. 21 (2001) S13-S14
    • (2001) J. Appl. Toxicol. , vol.21
    • Radić, Z.1    Taylor, P.2
  • 18
    • 0027517144 scopus 로고
    • Three distinct domains in the cholinesterase molecules confer selectivity for acetyl- and butyrylcholinesterase inhibitors
    • Radić Z., Pickering N.A., Vellom D.C., Camp S., and Taylor P. Three distinct domains in the cholinesterase molecules confer selectivity for acetyl- and butyrylcholinesterase inhibitors. Biochemistry 32 (1993) 12074-12084
    • (1993) Biochemistry , vol.32 , pp. 12074-12084
    • Radić, Z.1    Pickering, N.A.2    Vellom, D.C.3    Camp, S.4    Taylor, P.5
  • 19
    • 33645121825 scopus 로고    scopus 로고
    • Concentration-dependent kinetics of acetylcholinesterase inhibition by the organophosphate paraoxon
    • Rosenfeld C.A., and Sultatos L.G. Concentration-dependent kinetics of acetylcholinesterase inhibition by the organophosphate paraoxon. Toxicol. Sci. 90 2 (2006) 460-469
    • (2006) Toxicol. Sci. , vol.90 , Issue.2 , pp. 460-469
    • Rosenfeld, C.A.1    Sultatos, L.G.2
  • 20
    • 0034769403 scopus 로고    scopus 로고
    • Interactions of rat brain acetylcholinesterase with the detergent Triton X-100 and the organophosphate paraoxon
    • Rosenfeld C., Kousba A., and Sultatos L.G. Interactions of rat brain acetylcholinesterase with the detergent Triton X-100 and the organophosphate paraoxon. Toxicol. Sci. 63 (2001) 208-213
    • (2001) Toxicol. Sci. , vol.63 , pp. 208-213
    • Rosenfeld, C.1    Kousba, A.2    Sultatos, L.G.3
  • 21
    • 0032573399 scopus 로고    scopus 로고
    • A putative kinetic model for substrate metabolisation by Drosophila acetylcholinesterase
    • Stojan J., Marcel V., Estrada-Mondaca S., Klaebe A., Masson P., and Fournier D. A putative kinetic model for substrate metabolisation by Drosophila acetylcholinesterase. FEBS Lett. 440 (1998) 85-88
    • (1998) FEBS Lett. , vol.440 , pp. 85-88
    • Stojan, J.1    Marcel, V.2    Estrada-Mondaca, S.3    Klaebe, A.4    Masson, P.5    Fournier, D.6
  • 22
    • 0025778840 scopus 로고
    • Atomic structure of acetylcholinesterase from Torpedo californica: a prototypic acetylcholine-binding protein
    • Sussman J.L., Harel M., Frolow F., Oefner C., Goldman A., Toker L., and Silman I. Atomic structure of acetylcholinesterase from Torpedo californica: a prototypic acetylcholine-binding protein. Science 253 (1991) 872-879
    • (1991) Science , vol.253 , pp. 872-879
    • Sussman, J.L.1    Harel, M.2    Frolow, F.3    Oefner, C.4    Goldman, A.5    Toker, L.6    Silman, I.7
  • 23
    • 0033524414 scopus 로고    scopus 로고
    • Substrate binding to the peripheral site of acetylcholinesterase initiates enzymatic catalysis. Substrate inhibition arises as a secondary effect
    • Szegletes T., Mallender W.D., Thomas P.J., and Rosenberry T.L. Substrate binding to the peripheral site of acetylcholinesterase initiates enzymatic catalysis. Substrate inhibition arises as a secondary effect. Biochemistry 38 (1999) 122-133
    • (1999) Biochemistry , vol.38 , pp. 122-133
    • Szegletes, T.1    Mallender, W.D.2    Thomas, P.J.3    Rosenberry, T.L.4
  • 24
    • 0028174977 scopus 로고
    • The cholinesterases: from genes to proteins
    • Taylor P., and Radić Z. The cholinesterases: from genes to proteins. Annu. Rev. Pharmacol. Toxicol. 34 (1994) 281-320
    • (1994) Annu. Rev. Pharmacol. Toxicol. , vol.34 , pp. 281-320
    • Taylor, P.1    Radić, Z.2
  • 25
    • 0036191658 scopus 로고    scopus 로고
    • A physiologically based pharmacokinetic and pharmacodynamic (PBPK/PD) model for the organophosphate insecticide chlorpyrifos in rats and humans
    • Timchalk C., Nolan R.J., Mendrala A.L., Dittenber D.A., Brzak K.A., and Mattsson J.L. A physiologically based pharmacokinetic and pharmacodynamic (PBPK/PD) model for the organophosphate insecticide chlorpyrifos in rats and humans. Toxicol. Sci. 66 1 (2002) 34-53
    • (2002) Toxicol. Sci. , vol.66 , Issue.1 , pp. 34-53
    • Timchalk, C.1    Nolan, R.J.2    Mendrala, A.L.3    Dittenber, D.A.4    Brzak, K.A.5    Mattsson, J.L.6
  • 26
    • 0028110103 scopus 로고
    • Quantal acetylcholine release at the vertebrate neuromuscular junction
    • Van Der Kloot W., and Molgó J. Quantal acetylcholine release at the vertebrate neuromuscular junction. Physiol. Rev. 74 (1994) 899-991
    • (1994) Physiol. Rev. , vol.74 , pp. 899-991
    • Van Der Kloot, W.1    Molgó, J.2
  • 27
    • 0032892487 scopus 로고    scopus 로고
    • Dimethylphosphoryl-inhibited human cholinesterases: inhibition, reactivation, and aging kinetics
    • Worek F., Diepold C., and Eyer P. Dimethylphosphoryl-inhibited human cholinesterases: inhibition, reactivation, and aging kinetics. Arch. Toxicol. 73 (1999) 7-14
    • (1999) Arch. Toxicol. , vol.73 , pp. 7-14
    • Worek, F.1    Diepold, C.2    Eyer, P.3


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