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Volumn 274, Issue 7, 2007, Pages 1849-1861

Mechanisms of cholinesterase inhibition by inorganic mercury

Author keywords

Aggregation; Cholinesterase; Inhibition; Mercury; Metals

Indexed keywords

ACETYLCHOLINESTERASE; BIOLOGICAL MARKER; CHOLINESTERASE; MERCURY; THIOL DERIVATIVE;

EID: 33947265213     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2007.05732.x     Document Type: Article
Times cited : (88)

References (62)
  • 1
    • 0038160331 scopus 로고    scopus 로고
    • Environmental exposure to mercury and its toxicopathologic implications for public health
    • Tchounwou PB, Ayensu WK, Ninashvili N & Sutton D (2003) Environmental exposure to mercury and its toxicopathologic implications for public health. Environ Toxicol 18, 149-175.
    • (2003) Environ Toxicol , vol.18 , pp. 149-175
    • Tchounwou, P.B.1    Ayensu, W.K.2    Ninashvili, N.3    Sutton, D.4
  • 2
    • 0038240633 scopus 로고    scopus 로고
    • Bacterial mercury resistance from atoms to ecosystems
    • Barkay T, Miller SM & Summers AO (2003) Bacterial mercury resistance from atoms to ecosystems. FEMS Microbiol Rev 27, 355-384.
    • (2003) FEMS Microbiol Rev , vol.27 , pp. 355-384
    • Barkay, T.1    Miller, S.M.2    Summers, A.O.3
  • 4
    • 0034006391 scopus 로고    scopus 로고
    • Molecular interactions with mercury in the kidney
    • Zalups RK (2000) Molecular interactions with mercury in the kidney. Pharmacol Rev 52, 113-143.
    • (2000) Pharmacol Rev , vol.52 , pp. 113-143
    • Zalups, R.K.1
  • 6
    • 0036070699 scopus 로고    scopus 로고
    • Modulation of neuronal nicotinic acetylcholine receptors by mercury
    • Mirzoian A & Luetje CW (2002) Modulation of neuronal nicotinic acetylcholine receptors by mercury. J Pharmacol Exp Ther 302, 560-567.
    • (2002) J Pharmacol Exp Ther , vol.302 , pp. 560-567
    • Mirzoian, A.1    Luetje, C.W.2
  • 7
    • 0038208095 scopus 로고    scopus 로고
    • Contrasting changes of sensitivity by lymphocytes and neutrophils
    • Lalancette A, Morin Y, Measures L & Fournier M (2003) Contrasting changes of sensitivity by lymphocytes and neutrophils. Dev Comp Immunol 27, 735-747.
    • (2003) Dev Comp Immunol , vol.27 , pp. 735-747
    • Lalancette, A.1    Morin, Y.2    Measures, L.3    Fournier, M.4
  • 8
    • 1842844346 scopus 로고    scopus 로고
    • In vitro effects of cadmium and mercury on Pacific oyster Crassostrea gigas (Thunberg), haemocytes
    • Gagnaire B, Thomas-Guyon H & Renault T (2004) In vitro effects of cadmium and mercury on Pacific oyster Crassostrea gigas (Thunberg), haemocytes. Fish Shellfish Immun 16, 501-512.
    • (2004) Fish Shellfish Immun , vol.16 , pp. 501-512
    • Gagnaire, B.1    Thomas-Guyon, H.2    Renault, T.3
  • 9
    • 1242292924 scopus 로고    scopus 로고
    • Short-and long-term effects of T-cell modulating agents in experimental autoimmunity
    • Mellergård J, Havarinasab S & Hultman P (2004) Short-and long-term effects of T-cell modulating agents in experimental autoimmunity. Toxicology 196, 197-209.
    • (2004) Toxicology , vol.196 , pp. 197-209
    • Mellergård, J.1    Havarinasab, S.2    Hultman, P.3
  • 10
    • 0025607340 scopus 로고
    • Use of the fish enzyme system in monitoring water quality: Effects of mercury on tissue enzymes
    • Gill TS, Pande J & Tewari H (1990) Use of the fish enzyme system in monitoring water quality: effects of mercury on tissue enzymes. Comp Biochem Physiol 97C, 287-292.
    • (1990) Comp Biochem Physiol , vol.97 C , pp. 287-292
    • Gill, T.S.1    Pande, J.2    Tewari, H.3
  • 11
    • 0026555743 scopus 로고
    • Comparative study on the inhibition of acetylcholinesterase activity in the freshwater fish Cyprinus carpio by mercury and zinc
    • Suresh A, Sivaramakrishna B, Victoriamma PC & Radhakrishnaiah K (1992) Comparative study on the inhibition of acetylcholinesterase activity in the freshwater fish Cyprinus carpio by mercury and zinc. Biochem Int 26, 367-375.
    • (1992) Biochem Int , vol.26 , pp. 367-375
    • Suresh, A.1    Sivaramakrishna, B.2    Victoriamma, P.C.3    Radhakrishnaiah, K.4
  • 12
    • 0027985365 scopus 로고
    • 2+) in various body parts: Its impact on cholinesterase activity and binding glycoproteins in the grasshopper Aiolopus thalassinus adults
    • 2+) in various body parts: its impact on cholinesterase activity and binding glycoproteins in the grasshopper Aiolopus thalassinus adults. Ecotox Environ Safe 29, 148-164.
    • (1994) Ecotox Environ Safe , vol.29 , pp. 148-164
    • Schmidt, G.H.1    Ibrahim, N.M.2
  • 13
    • 0028982323 scopus 로고
    • Inhibition of acetylcholinesterase activity in the central nervous system of the red swamp crayfish, Procambarus clarkia, by mercury, cadmium, and lead
    • Devi M & Fingerman M (1995) Inhibition of acetylcholinesterase activity in the central nervous system of the red swamp crayfish, Procambarus clarkia, by mercury, cadmium, and lead. Bull Environ Contam Toxicol 55, 746-750.
    • (1995) Bull Environ Contam Toxicol , vol.55 , pp. 746-750
    • Devi, M.1    Fingerman, M.2
  • 14
    • 0032883278 scopus 로고    scopus 로고
    • Biological effects in Tilapia nilotica fish as indicators of pollution by cadmium and mercury
    • El-Demerdash FM & Elagamy EI (1999) Biological effects in Tilapia nilotica fish as indicators of pollution by cadmium and mercury. Int J Environ Health Res 9, 173-186.
    • (1999) Int J Environ Health Res , vol.9 , pp. 173-186
    • El-Demerdash, F.M.1    Elagamy, E.I.2
  • 15
    • 0034895224 scopus 로고    scopus 로고
    • Effects of selenium and mercury on the enzymatic activities and lipid peroxidation in brain, liver, and blood of rats
    • El-Demerdash FM (2001) Effects of selenium and mercury on the enzymatic activities and lipid peroxidation in brain, liver, and blood of rats. J Environ Sci Health 36B, 489-499.
    • (2001) J Environ Sci Health , vol.36 B , pp. 489-499
    • El-Demerdash, F.M.1
  • 16
    • 0343814563 scopus 로고
    • Implicaciones toxicologicas de las enzimas colinesterasas
    • Repetto M, ed pp, Diaz de Santos SA, Madrid
    • Sanz P & Repetto M (1995) Implicaciones toxicologicas de las enzimas colinesterasas. In Toxicologia Avanzada (Repetto M, ed) pp. 117-145. Diaz de Santos SA, Madrid.
    • (1995) Toxicologia Avanzada , pp. 117-145
    • Sanz, P.1    Repetto, M.2
  • 18
    • 0014076037 scopus 로고
    • Fish brain cholinesterase: Its inhibition by carbamates and automatic assay
    • Abou-Donia MB & Menzel DB (1967) Fish brain cholinesterase: its inhibition by carbamates and automatic assay. Comp Biochem Physiol 21, 99-104.
    • (1967) Comp Biochem Physiol , vol.21 , pp. 99-104
    • Abou-Donia, M.B.1    Menzel, D.B.2
  • 19
    • 0019771386 scopus 로고
    • Activation and inactivation of acetylcholinesterase by metal ions
    • Tomlinson G, Mutus B & McLennan I (1981) Activation and inactivation of acetylcholinesterase by metal ions. Can J Biochem 59, 728-735.
    • (1981) Can J Biochem , vol.59 , pp. 728-735
    • Tomlinson, G.1    Mutus, B.2    McLennan, I.3
  • 20
    • 0030941069 scopus 로고    scopus 로고
    • Evaluation of liver and brain esterases in the spotted gar fish (Lepisosteus oculatus) as biomarkers of effect in the lower Mississippi River basin
    • Huang TL, Obih PO, Jaiswal R, Hartley WR & Thiyagarajah A (1997) Evaluation of liver and brain esterases in the spotted gar fish (Lepisosteus oculatus) as biomarkers of effect in the lower Mississippi River basin. Bull Environ Contam Toxicol 58, 688-695.
    • (1997) Bull Environ Contam Toxicol , vol.58 , pp. 688-695
    • Huang, T.L.1    Obih, P.O.2    Jaiswal, R.3    Hartley, W.R.4    Thiyagarajah, A.5
  • 22
    • 28244482330 scopus 로고    scopus 로고
    • Do metals inhibit acetylcholinesterase (AChE)? Implementation of assay conditions for the use of AChE activity as a biomarker of metal toxicity
    • Frasco MF, Fournier D, Carvalho F & Guilhermino L (2005) Do metals inhibit acetylcholinesterase (AChE)? Implementation of assay conditions for the use of AChE activity as a biomarker of metal toxicity. Biomarkers 10, 360-375.
    • (2005) Biomarkers , vol.10 , pp. 360-375
    • Frasco, M.F.1    Fournier, D.2    Carvalho, F.3    Guilhermino, L.4
  • 24
    • 0028595911 scopus 로고
    • A metastable state of Torpedo californica acetylcholinesterase generated by modification with organomercurials
    • Kreimer DI, Dolginova EA, Raves M, Sussman JL, Silman I & Weiner L (1994) A metastable state of Torpedo californica acetylcholinesterase generated by modification with organomercurials. Biochemistry 33, 14407-14418.
    • (1994) Biochemistry , vol.33 , pp. 14407-14418
    • Kreimer, D.I.1    Dolginova, E.A.2    Raves, M.3    Sussman, J.L.4    Silman, I.5    Weiner, L.6
  • 25
    • 0029983402 scopus 로고    scopus 로고
    • Cocaine and butyrylcholinesterase (BChE): Determination of enzymatic parameters
    • Mattes C, Bradley R, Slaughter E & Browne S (1996) Cocaine and butyrylcholinesterase (BChE): determination of enzymatic parameters. Life Sci 58, 257-261.
    • (1996) Life Sci , vol.58 , pp. 257-261
    • Mattes, C.1    Bradley, R.2    Slaughter, E.3    Browne, S.4
  • 26
    • 0001061041 scopus 로고
    • Turnover number of acetylcholinesterase
    • Wilson IB & Harrison MA (1961) Turnover number of acetylcholinesterase. J Biol Chem 236, 2292-2295.
    • (1961) J Biol Chem , vol.236 , pp. 2292-2295
    • Wilson, I.B.1    Harrison, M.A.2
  • 28
    • 0027217179 scopus 로고
    • Dissection of the human acetylcholinesterase active center determinants of substrate specificity. Identification of residues constituting the anionic site, the hydrophobic site, and the acyl pocket
    • Ordentlich A, Barak D, Kronman C, Flashner Y, Leitner M, Segall Y, Ariel N, Cohen S, Velan B & Shafferman A (1993) Dissection of the human acetylcholinesterase active center determinants of substrate specificity. Identification of residues constituting the anionic site, the hydrophobic site, and the acyl pocket. J Biol Chem 268, 17083-17095.
    • (1993) J Biol Chem , vol.268 , pp. 17083-17095
    • Ordentlich, A.1    Barak, D.2    Kronman, C.3    Flashner, Y.4    Leitner, M.5    Segall, Y.6    Ariel, N.7    Cohen, S.8    Velan, B.9    Shafferman, A.10
  • 29
    • 0027459560 scopus 로고
    • Amino acid residues controlling acetylcholinesterase and butyrylcholinesterase specificity
    • Vellom DC, Radic Z, Li Y, Pickering NA, Camp S & Taylor P (1993) Amino acid residues controlling acetylcholinesterase and butyrylcholinesterase specificity. Biochemistry 32, 12-17.
    • (1993) Biochemistry , vol.32 , pp. 12-17
    • Vellom, D.C.1    Radic, Z.2    Li, Y.3    Pickering, N.A.4    Camp, S.5    Taylor, P.6
  • 30
    • 0025778840 scopus 로고
    • Atomic structure of acetylcholinesterase from Torpedo californica: A prototypic acetylcholine-binding protein
    • Sussman JL, Harel M, Frolow F, Oefner C, Goldman A, Toker L & Silman I (1991) Atomic structure of acetylcholinesterase from Torpedo californica: a prototypic acetylcholine-binding protein. Science 253, 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
  • 31
    • 0142039868 scopus 로고    scopus 로고
    • Crystal structure of human butyrylcholinesterase and of its complexes with substrate and products
    • Nicolet Y, Lockridge O, Masson P, Fontecilla-Camps JC & Nachon F (2003) Crystal structure of human butyrylcholinesterase and of its complexes with substrate and products. J Biol Chem 278, 41141-41147.
    • (2003) J Biol Chem , vol.278 , pp. 41141-41147
    • Nicolet, Y.1    Lockridge, O.2    Masson, P.3    Fontecilla-Camps, J.C.4    Nachon, F.5
  • 33
    • 0025170611 scopus 로고
    • Torpedo acetylcholinesterase is inactivated by thiol reagents
    • Steinberg N, Roth E & Silman I (1990) Torpedo acetylcholinesterase is inactivated by thiol reagents. Biochem Int 21, 1043-1050.
    • (1990) Biochem Int , vol.21 , pp. 1043-1050
    • Steinberg, N.1    Roth, E.2    Silman, I.3
  • 34
    • 84987573902 scopus 로고
    • Biosensor for detection of organophosphate and carbamate insecticide
    • Marty J-L, Sode K & Karube L (1992) Biosensor for detection of organophosphate and carbamate insecticide. Electroanalysis 4, 249-252.
    • (1992) Electroanalysis , vol.4 , pp. 249-252
    • Marty, J.-L.1    Sode, K.2    Karube, L.3
  • 36
    • 0018787051 scopus 로고
    • Chemical modification of the active site sulfhydryl group of saccharopine dehydrogenase (L-lysine-forming)
    • Ogawa H, Okamoto M & Fujioka M (1979) Chemical modification of the active site sulfhydryl group of saccharopine dehydrogenase (L-lysine-forming). J Biol Chem 254, 7030-7035.
    • (1979) J Biol Chem , vol.254 , pp. 7030-7035
    • Ogawa, H.1    Okamoto, M.2    Fujioka, M.3
  • 37
    • 0025744894 scopus 로고
    • Reactivity of the essential thiol of Klebsiella aerogenes urease. Effect of pH and ligands on thiol modification
    • Todd MJ & Hausinger RP (1991) Reactivity of the essential thiol of Klebsiella aerogenes urease. Effect of pH and ligands on thiol modification. J Biol Chem 266, 10260-10267.
    • (1991) J Biol Chem , vol.266 , pp. 10260-10267
    • Todd, M.J.1    Hausinger, R.P.2
  • 38
    • 0035232960 scopus 로고    scopus 로고
    • Kinetics of inactivation of glutamate decarboxylase by cysteine-specific reagents
    • McCormick SJ & Tunnicliff G (2001) Kinetics of inactivation of glutamate decarboxylase by cysteine-specific reagents. Acta Biochim Pol 48, 573-578.
    • (2001) Acta Biochim Pol , vol.48 , pp. 573-578
    • McCormick, S.J.1    Tunnicliff, G.2
  • 39
    • 0027265211 scopus 로고
    • An electrostatic mechanism for substrate guidance down the aromatic gorge of acetylcholinesterase
    • Ripoll DR, Faerman CH, Axelsen PH, Silman I & Sussman JL (1993) An electrostatic mechanism for substrate guidance down the aromatic gorge of acetylcholinesterase. Proc Natl Acad Sci USA 90, 5128-5132.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 5128-5132
    • Ripoll, D.R.1    Faerman, C.H.2    Axelsen, P.H.3    Silman, I.4    Sussman, J.L.5
  • 40
    • 33748456474 scopus 로고    scopus 로고
    • The hydration of the neurotransmitter acetylcholine in aqueous solution
    • Hulme EC, Soper AK, McLain SE & Finney JL (2006) The hydration of the neurotransmitter acetylcholine in aqueous solution. Biophys J 91, 2371-2380.
    • (2006) Biophys J , vol.91 , pp. 2371-2380
    • Hulme, E.C.1    Soper, A.K.2    McLain, S.E.3    Finney, J.L.4
  • 41
    • 0024978434 scopus 로고
    • Chemical modification of chalcone isomerase by mercurials and tetrathionate. Evidence for a single cysteine residue in the active site
    • Bednar RA, Fried WB, Lock YW & Pramanik B (1989) Chemical modification of chalcone isomerase by mercurials and tetrathionate. Evidence for a single cysteine residue in the active site. J Biol Chem 264, 14272-14276.
    • (1989) J Biol Chem , vol.264 , pp. 14272-14276
    • Bednar, R.A.1    Fried, W.B.2    Lock, Y.W.3    Pramanik, B.4
  • 43
    • 0014483561 scopus 로고
    • Reaction of disulfides with mercuric ions
    • Brown PR & Edwards JO (1969) Reaction of disulfides with mercuric ions. Biochemistry 8, 1200-1202.
    • (1969) Biochemistry , vol.8 , pp. 1200-1202
    • Brown, P.R.1    Edwards, J.O.2
  • 45
    • 19244375608 scopus 로고    scopus 로고
    • Influence of heavy metal ions on antibodies and immune complexes investigated by dynamic light scattering and enzyme-linked immunosorbent assay
    • Bauer R, Muller A, Richter M, Schneider K, Frey J & Engelhardt W (1997) Influence of heavy metal ions on antibodies and immune complexes investigated by dynamic light scattering and enzyme-linked immunosorbent assay. Biochim Biophys Acta 1334, 98-108.
    • (1997) Biochim Biophys Acta , vol.1334 , pp. 98-108
    • Bauer, R.1    Muller, A.2    Richter, M.3    Schneider, K.4    Frey, J.5    Engelhardt, W.6
  • 46
    • 0033564726 scopus 로고    scopus 로고
    • Copper( II)-induced self-oligomerization of alpha-synuclein
    • Paik SR, Shin HJ, Chang CS & Kim J (1999) Copper( II)-induced self-oligomerization of alpha-synuclein. Biochem J 340, 821-828.
    • (1999) Biochem J , vol.340 , pp. 821-828
    • Paik, S.R.1    Shin, H.J.2    Chang, C.S.3    Kim, J.4
  • 48
    • 7544235535 scopus 로고    scopus 로고
    • Inhibition of the Escherichia coli RecA protein: Zinc(II), copper(II) and mercury(II) trap RecA as inactive aggregates
    • Lee AM & Singleton SF (2004) Inhibition of the Escherichia coli RecA protein: zinc(II), copper(II) and mercury(II) trap RecA as inactive aggregates. J Inorg Biochem 98, 1981-1986.
    • (2004) J Inorg Biochem , vol.98 , pp. 1981-1986
    • Lee, A.M.1    Singleton, S.F.2
  • 54
    • 0037415394 scopus 로고    scopus 로고
    • Serum albumin binding at cytotoxic concentrations of chemicals as determined with a cell proliferation assay
    • Gülden M, Mörchel S & Seibert H (2003) Serum albumin binding at cytotoxic concentrations of chemicals as determined with a cell proliferation assay. Toxicol Lett 137, 159-168.
    • (2003) Toxicol Lett , vol.137 , pp. 159-168
    • Gülden, M.1    Mörchel, S.2    Seibert, H.3
  • 55
    • 0034307502 scopus 로고    scopus 로고
    • A method to estimate acetylcholinesterase-active sites and turnover in insects
    • Charpentier A, Menozzi P, Marcel V, Villatte F & Fournier D (2000) A method to estimate acetylcholinesterase-active sites and turnover in insects. Anal Biochem 285, 76-81.
    • (2000) Anal Biochem , vol.285 , pp. 76-81
    • Charpentier, A.1    Menozzi, P.2    Marcel, V.3    Villatte, F.4    Fournier, D.5
  • 56
    • 2642670423 scopus 로고    scopus 로고
    • Analysis of progress curves in an acetylcholinesterase reaction: A numerical integration treatment
    • Stojan J (1997) Analysis of progress curves in an acetylcholinesterase reaction: a numerical integration treatment. J Chem Inf Comput Sci 37, 1025-1027.
    • (1997) J Chem Inf Comput Sci , vol.37 , pp. 1025-1027
    • Stojan, J.1
  • 57
    • 0027879008 scopus 로고
    • Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants
    • Kabsch W (1993) Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants. J Appl Crystallogr 26, 795-800.
    • (1993) J Appl Crystallogr , vol.26 , pp. 795-800
    • Kabsch, W.1
  • 58
    • 13244281317 scopus 로고    scopus 로고
    • Coot: Model-building tools for molecular graphics
    • Emsley P & Cowtan K (2004) Coot: model-building tools for molecular graphics. Acta Crystallogr D60, 2126-2132.
    • (2004) Acta Crystallogr , vol.D60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 60
  • 61
    • 0028103275 scopus 로고
    • The CCP4 Suite: Programs for proteins crystallography
    • Collaborative Computational Project Number 4
    • Collaborative Computational Project Number 4 (1994) The CCP4 Suite: Programs for proteins crystallography. Acta Crystallogr D50, 760-763.
    • (1994) Acta Crystallogr , vol.D50 , pp. 760-763


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