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Volumn 3, Issue 3, 1998, Pages 247-255

Toxic effects of acetylcholinesterase on neuronal and glial-like cells in vitro

Author keywords

Acetylcholinesterase; Alzheimer's disease; Neurotoxicity; Non cholinergic action; Senile plaques

Indexed keywords

ACETYLCHOLINE; ACETYLCHOLINESTERASE; AMYLOID; AMYLOID BETA PROTEIN; NEUROTRANSMITTER;

EID: 0031782138     PISSN: 13594184     EISSN: None     Source Type: Journal    
DOI: 10.1038/sj.mp.4000383     Document Type: Article
Times cited : (57)

References (52)
  • 1
    • 0001921207 scopus 로고
    • Neuropsychological features of memory disorders in Alzheimer disease
    • Terry RD, Katzman R, Bick KL (eds). Raven Press: New York
    • Bondi MW, Salmon DP, Butters NM. Neuropsychological features of memory disorders in Alzheimer disease. In: Terry RD, Katzman R, Bick KL (eds). Alzheimer Disease. Raven Press: New York, 1994, pp 41-63.
    • (1994) Alzheimer Disease , pp. 41-63
    • Bondi, M.W.1    Salmon, D.P.2    Butters, N.M.3
  • 2
    • 0021145680 scopus 로고
    • Alzheimer's disease: Cell-specific pathology isolates the hippocampal formation
    • Hyman BT, Van Hoosen GW, Damasio AR, Barnes CL. Alzheimer's disease: cell-specific pathology isolates the hippocampal formation. Science 1984; 225: 1168-1170.
    • (1984) Science , vol.225 , pp. 1168-1170
    • Hyman, B.T.1    Van Hoosen, G.W.2    Damasio, A.R.3    Barnes, C.L.4
  • 3
    • 0029784838 scopus 로고    scopus 로고
    • Amyloid β-protein and the genetics of Alzheimer's disease
    • Selkoe DJ. Amyloid β-protein and the genetics of Alzheimer's disease. J Biol Chem 1996; 271: 18295-18298.
    • (1996) J Biol Chem , vol.271 , pp. 18295-18298
    • Selkoe, D.J.1
  • 4
    • 0020072221 scopus 로고
    • Alzheimer's disease and senile dementia: Loss of neurons in the basal forebrain
    • Whitehouse PJ, Price DL, Struble RG, Coyle JT, DeLong MR. Alzheimer's disease and senile dementia: loss of neurons in the basal forebrain. Science 1982; 215: 1237-1239.
    • (1982) Science , vol.215 , pp. 1237-1239
    • Whitehouse, P.J.1    Price, D.L.2    Struble, R.G.3    Coyle, J.T.4    DeLong, M.R.5
  • 5
    • 0030320768 scopus 로고    scopus 로고
    • Unraveling the molecular pathway of Alzheimer's disease: Research about presenilins gathers momentum
    • Sandbrink R, Beyreuther K. Unraveling the molecular pathway of Alzheimer's disease: research about presenilins gathers momentum. Mol Psychiatry 1996; 1: 438-444.
    • (1996) Mol Psychiatry , vol.1 , pp. 438-444
    • Sandbrink, R.1    Beyreuther, K.2
  • 6
    • 0031038918 scopus 로고    scopus 로고
    • Alzheimer's disease: Genotypes, phenotype, and treatments
    • Selkoe DJ. Alzheimer's disease: genotypes, phenotype, and treatments. Science 1997; 275: 630-631.
    • (1997) Science , vol.275 , pp. 630-631
    • Selkoe, D.J.1
  • 7
    • 0030922421 scopus 로고    scopus 로고
    • Presenilins: Genes for life and death
    • Haass C. Presenilins: genes for life and death. Neuron 1997; 18: 687-690.
    • (1997) Neuron , vol.18 , pp. 687-690
    • Haass, C.1
  • 8
    • 0029896354 scopus 로고    scopus 로고
    • Mechanisms of neuronal degeneration in Alzheimer's disease
    • Yankner BA. Mechanisms of neuronal degeneration in Alzheimer's disease. Neuron 1996; 16: 921-932.
    • (1996) Neuron , vol.16 , pp. 921-932
    • Yankner, B.A.1
  • 9
    • 0028031486 scopus 로고
    • Structural determinants of the Alzheimer's amyloid β-peptide
    • Soto C, Brañes MC, Alvarez J, Inostrosa NC. Structural determinants of the Alzheimer's amyloid β-peptide. J Neurochem 1994; 63: 1191-1198.
    • (1994) J Neurochem , vol.63 , pp. 1191-1198
    • Soto, C.1    Brañes, M.C.2    Alvarez, J.3    Inostrosa, N.C.4
  • 11
    • 0029977348 scopus 로고    scopus 로고
    • Non-classical actions of cholinesterases: Role in cellular differentiation, tumorigenesis and Alzheimer's disease
    • Greenfield S. Non-classical actions of cholinesterases: role in cellular differentiation, tumorigenesis and Alzheimer's disease. Neurochem Int 1996; 28: 485-490.
    • (1996) Neurochem Int , vol.28 , pp. 485-490
    • Greenfield, S.1
  • 12
    • 0029863697 scopus 로고    scopus 로고
    • Acetylcholinesterase accelerates assembly of amyloid-β-peptides into Alzheimer's fibrils: Possible role of the peripheral site of the enzyme
    • Inestrosa NC, Alvarez A, Pérez C, Moreno D, Vicente M, Linker C et al. Acetylcholinesterase accelerates assembly of amyloid-β-peptides into Alzheimer's fibrils: possible role of the peripheral site of the enzyme. Neuron 1996; 16: 1-20.
    • (1996) Neuron , vol.16 , pp. 1-20
    • Inestrosa, N.C.1    Alvarez, A.2    Pérez, C.3    Moreno, D.4    Vicente, M.5    Linker, C.6
  • 13
    • 0030276257 scopus 로고    scopus 로고
    • Acetylcholinesterase is a senile plaque component that promotes assembly of amyloid β-peptide into Alzheimer's filaments
    • Inestrosa NC, Alvarez A, Calderón FH. Acetylcholinesterase is a senile plaque component that promotes assembly of amyloid β-peptide into Alzheimer's filaments. Mol Psychiatry 1996; 1: 359-361.
    • (1996) Mol Psychiatry , vol.1 , pp. 359-361
    • Inestrosa, N.C.1    Alvarez, A.2    Calderón, F.H.3
  • 15
    • 0029670364 scopus 로고    scopus 로고
    • 4) acetylcholinesterase: Structure, localization, and physiological regulation
    • 4) acetylcholinesterase: structure, localization, and physiological regulation. J Neurochem 1996; 66: 1335-1346.
    • (1996) J Neurochem , vol.66 , pp. 1335-1346
    • Fernandez, H.L.1    Moreno, R.2    Inestrosa, N.C.3
  • 16
    • 0024318506 scopus 로고
    • Distribution and anchoring of molecular forms of acetylcholinesterase
    • Inestrosa NC, Perelman A. Distribution and anchoring of molecular forms of acetylcholinesterase. Trends Pharmacol Sci 1989; 10: 325-329.
    • (1989) Trends Pharmacol Sci , vol.10 , pp. 325-329
    • Inestrosa, N.C.1    Perelman, A.2
  • 18
    • 0002037940 scopus 로고
    • Cholinorgic systems and related neuropathological predilection patterns in Alzheimer disease
    • Terry RD, Katzman R, Bick KL (eds). Raven Press: New York
    • Geula C, Mesulam MM. Cholinorgic systems and related neuropathological predilection patterns in Alzheimer disease. In: Terry RD, Katzman R, Bick KL (eds). Alzheimer Disease. Raven Press: New York, 1994, pp 263-269.
    • (1994) Alzheimer Disease , pp. 263-269
    • Geula, C.1    Mesulam, M.M.2
  • 20
    • 0029360450 scopus 로고
    • Transgenic expression of human acetylcholinesterase induces progressive cognitive deterioration in mice
    • Beeri R, Andres C, Lev-Lehman E, Timberg R, Huberman T, Shani M et al. Transgenic expression of human acetylcholinesterase induces progressive cognitive deterioration in mice. Curr Biol 1995; 5: 1063-1071.
    • (1995) Curr Biol , vol.5 , pp. 1063-1071
    • Beeri, R.1    Andres, C.2    Lev-Lehman, E.3    Timberg, R.4    Huberman, T.5    Shani, M.6
  • 21
    • 0020545113 scopus 로고
    • Molecular forms of acetylcholinesterase in senile dementia of Alzheimer's type: Selective loss of the intermediate (10S) form
    • Atack JR, Perry EK, Bonham JR, Perry RH, Tomlinson BE, Blessed G et al. Molecular forms of acetylcholinesterase in senile dementia of Alzheimer's type: selective loss of the intermediate (10S) form. Neurosci Lett 1983; 40: 199-204.
    • (1983) Neurosci Lett , vol.40 , pp. 199-204
    • Atack, J.R.1    Perry, E.K.2    Bonham, J.R.3    Perry, R.H.4    Tomlinson, B.E.5    Blessed, G.6
  • 22
    • 0022616905 scopus 로고
    • Distribution of the molecular forms of acetylcholinesterase in human brain: Alterations in dementia of the Alzheimer type
    • Fishman EB, Siek GC, MacCallum RD, Bird ED, Volicer L, Marquis JK. Distribution of the molecular forms of acetylcholinesterase in human brain: alterations in dementia of the Alzheimer type. Ann Neurol 1986; 19: 246-252.
    • (1986) Ann Neurol , vol.19 , pp. 246-252
    • Fishman, E.B.1    Siek, G.C.2    MacCallum, R.D.3    Bird, E.D.4    Volicer, L.5    Marquis, J.K.6
  • 24
    • 0026794041 scopus 로고
    • Changes in acetylcholinesterase and butyrylcholinesterase in Alzheimer's disease resemble embryonic development. A study of molecular forms
    • Arendt T, Brückner MK, Lange M, Bigl V. Changes in acetylcholinesterase and butyrylcholinesterase in Alzheimer's disease resemble embryonic development. A study of molecular forms. Neurochem Int 1992; 21: 381-396.
    • (1992) Neurochem Int , vol.21 , pp. 381-396
    • Arendt, T.1    Brückner, M.K.2    Lange, M.3    Bigl, V.4
  • 25
    • 0026499929 scopus 로고
    • Ultrastructural localization of acetylcholinesterase in neurofibrillary tangles, neuropil and senile plaques in aged and Alzheimer's brain
    • Gómez-Ramos P, Mufson EJ, Morán MA. Ultrastructural localization of acetylcholinesterase in neurofibrillary tangles, neuropil and senile plaques in aged and Alzheimer's brain. Brain Res 1992; 569: 229-237.
    • (1992) Brain Res , vol.569 , pp. 229-237
    • Gómez-Ramos, P.1    Mufson, E.J.2    Morán, M.A.3
  • 26
    • 0026443031 scopus 로고
    • Acetylcholinesterase and its association with heparan sulphate proteoglycans in cortical amyloid deposits of Alzheimer's disease
    • Kalaria RN, Kroon SN, Grahovac I, Perry G. Acetylcholinesterase and its association with heparan sulphate proteoglycans in cortical amyloid deposits of Alzheimer's disease. Neuroscience 1992; 51: 177-184.
    • (1992) Neuroscience , vol.51 , pp. 177-184
    • Kalaria, R.N.1    Kroon, S.N.2    Grahovac, I.3    Perry, G.4
  • 27
    • 0027514286 scopus 로고
    • Colocalization of cholinesterases with β-amyloid protein in aged and Alzheimer's brain
    • Morán MA, Mufson EJ. Gómez-Ramos P. Colocalization of cholinesterases with β-amyloid protein in aged and Alzheimer's brain. Acta Neuropathol 1993; 85: 362-369.
    • (1993) Acta Neuropathol , vol.85 , pp. 362-369
    • Morán, M.A.1    Mufson, E.J.2    Gómez-Ramos, P.3
  • 28
    • 0029897490 scopus 로고    scopus 로고
    • Non-classical actions of cholinesterases: Role in cellular differentiation, tumorigenesis and Alzheimer's disease
    • Small DH, Michaelson S, Sberna G. Non-classical actions of cholinesterases: role in cellular differentiation, tumorigenesis and Alzheimer's disease. Neurochem Int 1996; 28: 453-483.
    • (1996) Neurochem Int , vol.28 , pp. 453-483
    • Small, D.H.1    Michaelson, S.2    Sberna, G.3
  • 29
    • 0028148003 scopus 로고
    • Acetylcholinesterase provides deeper insights into Alzheimer's disease
    • Shen ZX. Acetylcholinesterase provides deeper insights into Alzheimer's disease. Med Hypoth 1994; 43: 21-30.
    • (1994) Med Hypoth , vol.43 , pp. 21-30
    • Shen, Z.X.1
  • 30
    • 0021754096 scopus 로고
    • Alzheimer's disease and acetylcholinesterase-containing neurons
    • Smith AD, Cuello AC. Alzheimer's disease and acetylcholinesterase-containing neurons. Lancet 1984; I: 513.
    • (1984) Lancet , vol.1 , pp. 513
    • Smith, A.D.1    Cuello, A.C.2
  • 32
    • 0030601933 scopus 로고    scopus 로고
    • Amyloid precursor protein fragment and acetylcholinesterase increase with cell confluence and differentiation in a neuronal cell line
    • Bronfman FC, Fernández HL, Inestrosa NC. Amyloid precursor protein fragment and acetylcholinesterase increase with cell confluence and differentiation in a neuronal cell line. Exp Cell Res 1996; 229: 93-99.
    • (1996) Exp Cell Res , vol.229 , pp. 93-99
    • Bronfman, F.C.1    Fernández, H.L.2    Inestrosa, N.C.3
  • 33
    • 0016687593 scopus 로고
    • Differentiation of neuroblastoma cells in culture
    • Prasad KN. Differentiation of neuroblastoma cells in culture. Biol Rev 1975; 50: 129-265.
    • (1975) Biol Rev , vol.50 , pp. 129-265
    • Prasad, K.N.1
  • 35
    • 0023219731 scopus 로고
    • Acetylcholinesterase from bovine caudate nucleus is attached to membranes by a novel subunit distinct from those of acetylcholinesterase in other tissues
    • Inestrosa NC, Roberts WL, Marshall T, Rosenberry TL. Acetylcholinesterase from bovine caudate nucleus is attached to membranes by a novel subunit distinct from those of acetylcholinesterase in other tissues. J Biol Chem 1987; 262: 4441-4444.
    • (1987) J Biol Chem , vol.262 , pp. 4441-4444
    • Inestrosa, N.C.1    Roberts, W.L.2    Marshall, T.3    Rosenberry, T.L.4
  • 37
    • 0020321505 scopus 로고
    • Association of the synaptic form of acetylcholinesterase with extracellular matrix in cultured mouse muscle cells
    • Inestrosa NC, Silberstein L, Hall ZW. Association of the synaptic form of acetylcholinesterase with extracellular matrix in cultured mouse muscle cells. Cell 1982; 29: 71-79.
    • (1982) Cell , vol.29 , pp. 71-79
    • Inestrosa, N.C.1    Silberstein, L.2    Hall, Z.W.3
  • 38
    • 0023221068 scopus 로고
    • Quantitative determination of glutamate mediated cortical neuronal injury in cell culture by lactate dehydrogenase efflux assay
    • Koh JY, Choi DW. Quantitative determination of glutamate mediated cortical neuronal injury in cell culture by lactate dehydrogenase efflux assay. J Neurosci Meth 1987; 20: 83-90.
    • (1987) J Neurosci Meth , vol.20 , pp. 83-90
    • Koh, J.Y.1    Choi, D.W.2
  • 39
    • 0021061819 scopus 로고
    • Rapid colorimetric assay for cellular growth and survival: Application to proliferation and cytotoxic assays
    • Mosmann T. Rapid colorimetric assay for cellular growth and survival: application to proliferation and cytotoxic assays. J Immunol Meth 1983; 65: 55-63.
    • (1983) J Immunol Meth , vol.65 , pp. 55-63
    • Mosmann, T.1
  • 40
    • 0026648674 scopus 로고
    • Identification of programmed cell death in situ via specific labeling of DNA fragmentation
    • Gavrieli Y, Sherman Y, Ben-Sasson SA. Identification of programmed cell death in situ via specific labeling of DNA fragmentation. J Cell Biol 1992; 119: 493-501.
    • (1992) J Cell Biol , vol.119 , pp. 493-501
    • Gavrieli, Y.1    Sherman, Y.2    Ben-Sasson, S.A.3
  • 43
    • 0000694113 scopus 로고
    • Acetylcholinesterase: Structure and use as a model for specific cation-protein interactions
    • Sussman JL, Silman I. Acetylcholinesterase: structure and use as a model for specific cation-protein interactions. Curr Opin Struct Biol 1992; 2: 721-729.
    • (1992) Curr Opin Struct Biol , vol.2 , pp. 721-729
    • Sussman, J.L.1    Silman, I.2
  • 44
    • 0028177161 scopus 로고
    • Differential effects of 'peripheral' site ligands on Torpedo and chicken acetylcholinesterase
    • Eichler J, Anselmet A, Sussman JL, Massoulie J, Silman I. Differential effects of 'peripheral' site ligands on Torpedo and chicken acetylcholinesterase. Mol Pharmacol 1994; 45: 335-340.
    • (1994) Mol Pharmacol , vol.45 , pp. 335-340
    • Eichler, J.1    Anselmet, A.2    Sussman, J.L.3    Massoulie, J.4    Silman, I.5
  • 45
    • 0027198071 scopus 로고
    • Cholinesterases regulate neurite growth of chick nerve cells in vitro by means of a non-enzymatic mechanism
    • Layer PG, Weikert T, Alber R. Cholinesterases regulate neurite growth of chick nerve cells in vitro by means of a non-enzymatic mechanism. Cell Tissue Res 1993; 273: 219-226.
    • (1993) Cell Tissue Res , vol.273 , pp. 219-226
    • Layer, P.G.1    Weikert, T.2    Alber, R.3
  • 46
    • 0028934738 scopus 로고
    • Uptake of acetylcholinesterase by neurons in the substantia nigra
    • Dickie BGM, Budd TC, Vaux D, Greenfield SA. Uptake of acetylcholinesterase by neurons in the substantia nigra. Eur J Neurosci 1995; 7: 351-357.
    • (1995) Eur J Neurosci , vol.7 , pp. 351-357
    • Dickie, B.G.M.1    Budd, T.C.2    Vaux, D.3    Greenfield, S.A.4
  • 47
    • 0028363462 scopus 로고
    • Acetylcholinesterase activation of peritoneal macrophages is independent of catalytic activity
    • Klegeris A, Budd TC, Greenfield SA. Acetylcholinesterase activation of peritoneal macrophages is independent of catalytic activity. Cell Molec Neurobiol 1994; 14: 89-98.
    • (1994) Cell Molec Neurobiol , vol.14 , pp. 89-98
    • Klegeris, A.1    Budd, T.C.2    Greenfield, S.A.3
  • 48
    • 0029868722 scopus 로고    scopus 로고
    • Acetylcholinesterase-induced respiratory burst in macrophages: Evidence for the involvement of the macrophage mannose-fucose receptor
    • Klegoris A, Budd TC, Greenfield SA. Acetylcholinesterase-induced respiratory burst in macrophages: evidence for the involvement of the macrophage mannose-fucose receptor. Biochem Biophys Acta 1996; 1289: 159-168.
    • (1996) Biochem Biophys Acta , vol.1289 , pp. 159-168
    • Klegoris, A.1    Budd, T.C.2    Greenfield, S.A.3
  • 50
    • 0028577208 scopus 로고
    • Immunohistochemical evidence for apoptosis in Alzheimer's disease
    • Su JH, Anderson AJ, Cummings BJ, Cotman CW. Immunohistochemical evidence for apoptosis in Alzheimer's disease. NeuroReport 1994; 5: 2529-2533.
    • (1994) NeuroReport , vol.5 , pp. 2529-2533
    • Su, J.H.1    Anderson, A.J.2    Cummings, B.J.3    Cotman, C.W.4
  • 51
    • 0000354585 scopus 로고
    • Structural basis of the cognitive alterations in Alzheimer disease
    • Terry RD, Katzman R, Bick KL (eds). Raven Press: New York
    • Terry RD, Masliah E, Hansen LA. Structural basis of the cognitive alterations in Alzheimer disease. In: Terry RD, Katzman R, Bick KL (eds). Alzheimer Disease. Raven Press: New York, 1994, pp 179-196.
    • (1994) Alzheimer Disease , pp. 179-196
    • Terry, R.D.1    Masliah, E.2    Hansen, L.A.3
  • 52
    • 0027250825 scopus 로고
    • Beta-amyloid peptides induce degeneration of cultured rat microglia
    • Korotzer AR, Pike CJ, Cotman CW. Beta-amyloid peptides induce degeneration of cultured rat microglia. Brain Res 1993; 624: 121-125.
    • (1993) Brain Res , vol.624 , pp. 121-125
    • Korotzer, A.R.1    Pike, C.J.2    Cotman, C.W.3


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