메뉴 건너뛰기




Volumn 65, Issue 3, 2003, Pages 407-416

β-Amyloid aggregation induced by human acetylcholinesterase: Inhibition studies

Author keywords

Amyloid (1 40); Acetylcholinesterase inhibitors; Alzheimer's disease; Fibrillogenesis; Human recombinant acetylcholinesterase; Mechanism of action

Indexed keywords

ACETYLCHOLINESTERASE; AMYLOID BETA PROTEIN; CHOLINESTERASE INHIBITOR; DECAMETHONIUM; DONEPEZIL; EDROPHONIUM; PHYSOSTIGMINE; PROPIDIUM IODIDE; TACRINE; THIOFLAVINE;

EID: 0037298750     PISSN: 00062952     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-2952(02)01514-9     Document Type: Article
Times cited : (555)

References (42)
  • 1
    • 0033036158 scopus 로고    scopus 로고
    • Cholinergic therapies in Alzheimer's disease
    • Siddiqui M.F., Levey A.I. Cholinergic therapies in Alzheimer's disease. Drugs Fut. 24:1999;417-424.
    • (1999) Drugs Fut. , vol.24 , pp. 417-424
    • Siddiqui, M.F.1    Levey, A.I.2
  • 2
    • 0019972810 scopus 로고
    • The cholinergic hypothesis of geriatric memory dysfunction
    • Bartus R.T., Dean L.D. III, Beer B., Lippa A.S. The cholinergic hypothesis of geriatric memory dysfunction. Science. 217:1982;408-417.
    • (1982) Science , vol.217 , pp. 408-417
    • Bartus, R.T.1    Dean L.D. III2    Beer, B.3    Lippa, A.S.4
  • 3
    • 0001517609 scopus 로고    scopus 로고
    • Mechanism of action of cholinesterase inhibitors
    • Giacobini E, editor. London: Martin Dunitz Ltd
    • Reiner E, Radić Z. Mechanism of action of cholinesterase inhibitors. In: Giacobini E, editor. Cholinesterases and cholinesterase inhibitors. London: Martin Dunitz Ltd.; 2000. p. 103-19.
    • (2000) Cholinesterases and cholinesterase inhibitors , pp. 103-119
    • Reiner, E.1    Radić, Z.2
  • 4
    • 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 N.C., Alvarez A., Pérez C.A., Moreno R.D., Vicente M., Linker C., Casanueva O.I., Soto C., Garrido J. Acetylcholinesterase accelerates assembly of amyloid-β-peptides into Alzheimer's fibrils: possible role of the peripheral site of the enzyme. Neuron. 16:1996;881-891.
    • (1996) Neuron , vol.16 , pp. 881-891
    • Inestrosa, N.C.1    Alvarez, A.2    Pérez, C.A.3    Moreno, R.D.4    Vicente, M.5    Linker, C.6    Casanueva, O.I.7    Soto, C.8    Garrido, J.9
  • 5
    • 0033600274 scopus 로고    scopus 로고
    • Translating cell biology into therapeutic advances in Alzheimer's disease
    • Selkoe D.J. Translating cell biology into therapeutic advances in Alzheimer's disease. Nature. 399:1999;A23-A31.
    • (1999) Nature , vol.399 , pp. 23-A31
    • Selkoe, D.J.1
  • 7
    • 0035950225 scopus 로고    scopus 로고
    • Clearing the brain's amyloid cobwebs
    • Selkoe D.J. Clearing the brain's amyloid cobwebs. Neuron. 32:2001;177-180.
    • (2001) Neuron , vol.32 , pp. 177-180
    • Selkoe, D.J.1
  • 8
    • 0033621165 scopus 로고    scopus 로고
    • Amyloid diseases: Abnormal protein aggregation in neurodegeneration
    • Koo E.H., Lansbury P.T., Kelly J.W. Amyloid diseases: abnormal protein aggregation in neurodegeneration. Proc. Natl. Acad. Sci. U.S.A. 96:1999;9989-9990.
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 9989-9990
    • Koo, E.H.1    Lansbury, P.T.2    Kelly, J.W.3
  • 9
    • 0035949487 scopus 로고    scopus 로고
    • Presenilin, notch and the genesis and treatment of Alzheimer's disease
    • Selkoe D.J. Presenilin, notch and the genesis and treatment of Alzheimer's disease. Proc. Natl. Acad. Sci. U.S.A. 98:2001;11039-11041.
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 11039-11041
    • Selkoe, D.J.1
  • 10
    • 0035807054 scopus 로고    scopus 로고
    • A structural motif of acetylcholinesterase that promotes amyloid β-peptide fibril formation
    • De Ferrari G.V., Canales M.A., Shin I., Weiner L.M., Silman I., Inestrosa N.C. A structural motif of acetylcholinesterase that promotes amyloid β-peptide fibril formation. Biochemistry. 40:2001;10447-10457.
    • (2001) Biochemistry , vol.40 , pp. 10447-10457
    • De Ferrari, G.V.1    Canales, M.A.2    Shin, I.3    Weiner, L.M.4    Silman, I.5    Inestrosa, N.C.6
  • 11
    • 0031444010 scopus 로고    scopus 로고
    • Atomic force microscopic imaging of seeded fibril formation and fibril branching by the Alzheimer's amyloid-beta protein
    • Harper J.D., Lieber C.M., Lansbury P.T. Atomic force microscopic imaging of seeded fibril formation and fibril branching by the Alzheimer's amyloid-beta protein. Chem. Biol. 4:1997;951-959.
    • (1997) Chem. Biol. , vol.4 , pp. 951-959
    • Harper, J.D.1    Lieber, C.M.2    Lansbury, P.T.3
  • 13
    • 0025826915 scopus 로고
    • Kinetic analysis of amyloid fibril polymerization in vitro
    • Naiki H., Higuchi K., Nakakuki K., Takeda T. Kinetic analysis of amyloid fibril polymerization in vitro. Lab. Invest. 65:1991;104-110.
    • (1991) Lab. Invest. , vol.65 , pp. 104-110
    • Naiki, H.1    Higuchi, K.2    Nakakuki, K.3    Takeda, T.4
  • 14
    • 0027502784 scopus 로고
    • Thioflavin T interaction with synthetic Alzheimer's disease beta-amyloid peptides: Detection of amyloid aggregation in solution
    • LeVine H. Thioflavin T interaction with synthetic Alzheimer's disease beta-amyloid peptides: detection of amyloid aggregation in solution. Protein Sci. 2:1993;404-410.
    • (1993) Protein Sci. , vol.2 , pp. 404-410
    • LeVine, H.1
  • 15
    • 0032849874 scopus 로고    scopus 로고
    • Quantification of beta-sheet amyloid fibril structures with thioflavin T
    • LeVine H. III Quantification of beta-sheet amyloid fibril structures with thioflavin T. Methods Enzymol. 309:1999;274-284.
    • (1999) Methods Enzymol. , vol.309 , pp. 274-284
    • LeVine H. III1
  • 17
    • 0028980362 scopus 로고
    • The alpha-helical to beta-strand transition in the amino-terminal fragment of the amyloid beta-peptide modulates amyloid formation
    • Soto C., Castano E.M., Frangione B., Inestrosa N.C. The alpha-helical to beta-strand transition in the amino-terminal fragment of the amyloid beta-peptide modulates amyloid formation. J. Biol. Chem. 270:1995;3063-3067.
    • (1995) J. Biol. Chem. , vol.270 , pp. 3063-3067
    • Soto, C.1    Castano, E.M.2    Frangione, B.3    Inestrosa, N.C.4
  • 18
    • 0031034117 scopus 로고    scopus 로고
    • Direct conversion of an oligopeptide from a β-sheet to an α-helix: A model for amyloid formation
    • Hang S., Rich A. Direct conversion of an oligopeptide from a β-sheet to an α-helix: a model for amyloid formation. Proc. Natl. Acad. Sci. U.S.A. 94:1997;23-28.
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 23-28
    • Hang, S.1    Rich, A.2
  • 19
    • 0028176595 scopus 로고
    • Measurement of the β-sheet-forming propensities of amino acids
    • Minor D.L., Kim P.S. Measurement of the β-sheet-forming propensities of amino acids. Nature. 367:1994;660-663.
    • (1994) Nature , vol.367 , pp. 660-663
    • Minor, D.L.1    Kim, P.S.2
  • 20
    • 0028279006 scopus 로고
    • Importance of environment in determining secondary structure of in proteins
    • Waterhous D.V., Johnson W.C. Jr. Importance of environment in determining secondary structure of in proteins. Biochemistry. 33:1994;2121-2128.
    • (1994) Biochemistry , vol.33 , pp. 2121-2128
    • Waterhous, D.V.1    Johnson W.C., Jr.2
  • 21
    • 0021871802 scopus 로고
    • Circular dichroism studies of acetylcholinesterase conformation: Comparison of the 11 S and 5.6 S species and the differences induced by inhibitory ligands
    • Manavalan P., Taylor P., Johnson W.C. Jr. Circular dichroism studies of acetylcholinesterase conformation: comparison of the 11 S and 5.6 S species and the differences induced by inhibitory ligands. Biochim. Biophys. Acta. 829:1985;365-370.
    • (1985) Biochim. Biophys. Acta , vol.829 , pp. 365-370
    • Manavalan, P.1    Taylor, P.2    Johnson W.C., Jr.3
  • 23
    • 0033551440 scopus 로고    scopus 로고
    • Assembly of A beta amyloid protofibrils: An in vitro model for a possible early event in Alzheimer's disease
    • Harper J.D., Wong S.S., Lieber C.M., Lansbury P.T. Jr. Assembly of A beta amyloid protofibrils: an in vitro model for a possible early event in Alzheimer's disease. Biochemistry. 38:1999;8972-8980.
    • (1999) Biochemistry , vol.38 , pp. 8972-8980
    • Harper, J.D.1    Wong, S.S.2    Lieber, C.M.3    Lansbury P.T., Jr.4
  • 24
    • 0001885399 scopus 로고    scopus 로고
    • Cholinesterase inhibitors: From the Calabar Bean to Alzheimer's therapy
    • Giacobini E, editor. London, UK: Martin Dunitz Ltd
    • Giacobini E. Cholinesterase inhibitors: From the Calabar Bean to Alzheimer's therapy. In: Giacobini E, editor. Cholinesterases and Cholinesterase Inhibitors. London, UK: Martin Dunitz Ltd.; 2000. p. 181-226.
    • (2000) Cholinesterases and Cholinesterase Inhibitors , pp. 181-226
    • Giacobini, E.1
  • 26
    • 0034467344 scopus 로고    scopus 로고
    • Comparison of inhibitory activities of donepezil and other cholinesterase inhibitors on acetylcholinesterase and butyrylcholinesterase in vitro
    • Ogura H., Kosasa T., Kuriya Y., Yamanishi Y. Comparison of inhibitory activities of donepezil and other cholinesterase inhibitors on acetylcholinesterase and butyrylcholinesterase in vitro. Methods Find Exp. Clin. Pharmacol. 22:2000;609-613.
    • (2000) Methods Find Exp. Clin. Pharmacol. , vol.22 , pp. 609-613
    • Ogura, H.1    Kosasa, T.2    Kuriya, Y.3    Yamanishi, Y.4
  • 29
    • 0032190343 scopus 로고    scopus 로고
    • The aromatic patch of three proximal residues in the human acetylcholinesterase active centre allows for versatile interaction modes with inhibitors
    • Ariel N., Ordentlich A., Barak D., Bino T., Velan B., Shafferman A. The aromatic patch of three proximal residues in the human acetylcholinesterase active centre allows for versatile interaction modes with inhibitors. Biochem. J. 335:1998;95-102.
    • (1998) Biochem. J. , vol.335 , pp. 95-102
    • Ariel, N.1    Ordentlich, A.2    Barak, D.3    Bino, T.4    Velan, B.5    Shafferman, A.6
  • 31
    • 0016823110 scopus 로고
    • Interaction of fluorescence probes with acetylcholinesterase. The site and specificity of propidium binding
    • Taylor P., Lappi S. Interaction of fluorescence probes with acetylcholinesterase. The site and specificity of propidium binding. Biochemistry. 6:1975;1989-1997.
    • (1975) Biochemistry , vol.6 , pp. 1989-1997
    • Taylor, P.1    Lappi, S.2
  • 32
    • 0029092671 scopus 로고
    • Fasciculin 2 binds to a peripheral site on acetylcholinesterase and inhibits substrate hydrolysis by slowing a step involving proton transfer during enzyme acylation
    • Eastman J., Wilson E.J., Cervenansky C., Rosenberry T.L. Fasciculin 2 binds to a peripheral site on acetylcholinesterase and inhibits substrate hydrolysis by slowing a step involving proton transfer during enzyme acylation. J. Biol. Chem. 270:1995;19694-19701.
    • (1995) J. Biol. Chem. , vol.270 , pp. 19694-19701
    • Eastman, J.1    Wilson, E.J.2    Cervenansky, C.3    Rosenberry, T.L.4
  • 33
    • 0035727888 scopus 로고    scopus 로고
    • Donepezil for Alzheimer's disease: Pharmacodynamic, pharmacokinetic, and clinical profiles
    • Shigeta M., Homma A. Donepezil for Alzheimer's disease: pharmacodynamic, pharmacokinetic, and clinical profiles. CNS Drug Rev. 7:2001;353-368.
    • (2001) CNS Drug Rev. , vol.7 , pp. 353-368
    • Shigeta, M.1    Homma, A.2
  • 34
    • 0031910978 scopus 로고    scopus 로고
    • Donepezil use in Alzheimer's disease
    • Barner E.L., Gray S.L. Donepezil use in Alzheimer's disease. Ann. Pharmacother. 32:1998;70-77.
    • (1998) Ann. Pharmacother. , vol.32 , pp. 70-77
    • Barner, E.L.1    Gray, S.L.2
  • 35
    • 0033043305 scopus 로고    scopus 로고
    • A comparative study in rats of the in vitro and in vivo pharmacology of the acetylcholinesterase inhibitors tacrine, donepezil and NXX-066
    • Snape M.F., Misra A., Murray T.K., De Souza R.J., Williams J.L., Cross A.J., Green A.R. A comparative study in rats of the in vitro and in vivo pharmacology of the acetylcholinesterase inhibitors tacrine, donepezil and NXX-066. Neuropharmacology. 38:1999;181-193.
    • (1999) Neuropharmacology , vol.38 , pp. 181-193
    • Snape, M.F.1    Misra, A.2    Murray, T.K.3    De Souza, R.J.4    Williams, J.L.5    Cross, A.J.6    Green, A.R.7
  • 36
    • 0032101015 scopus 로고    scopus 로고
    • Comparative studies of huperzine A, E2020, and tacrine on behavior and cholinesterase activities
    • Cheng D.H., Tang X.C. Comparative studies of huperzine A, E2020, and tacrine on behavior and cholinesterase activities. Pharmacol. Biochem. Behav. 60:1998;377-386.
    • (1998) Pharmacol. Biochem. Behav. , vol.60 , pp. 377-386
    • Cheng, D.H.1    Tang, X.C.2
  • 37
    • 0014024408 scopus 로고
    • Carbamylation and binding constants for the inhibition of acetylcholinesterase by physostigmine
    • Main A.R., Hastings F.L. Carbamylation and binding constants for the inhibition of acetylcholinesterase by physostigmine. Science. 154:1966;400-402.
    • (1966) Science , vol.154 , pp. 400-402
    • Main, A.R.1    Hastings, F.L.2
  • 39
    • 0036639707 scopus 로고    scopus 로고
    • Novel therapeutic strategies provide the real test for the amyloid hypothesis of Alzheimer's disease
    • Dominguez D.I., De Strooper B. Novel therapeutic strategies provide the real test for the amyloid hypothesis of Alzheimer's disease. Trends Pharmacol. Sci. 23:2002;324-330.
    • (2002) Trends Pharmacol. Sci. , vol.23 , pp. 324-330
    • Dominguez, D.I.1    De Strooper, B.2
  • 41
    • 0000432021 scopus 로고
    • Cholinergic agents: Synthesis and acetylcholinesterase inhibitory activity of some ω-[N-methyl-N-(3-alkylcarbamoyloxyphenyl)methyl]aminoalkoxyxanthen-9- ones
    • Valenti P., Rampa A., Bisi A., Fabbri G., Andrisano V., Cavrini V. Cholinergic agents: synthesis and acetylcholinesterase inhibitory activity of some ω-[N-methyl-N-(3-alkylcarbamoyloxyphenyl)methyl]aminoalkoxyxanthen-9- ones. Med. Chem. Res. 5:1995;255-264.
    • (1995) Med. Chem. Res. , vol.5 , pp. 255-264
    • Valenti, P.1    Rampa, A.2    Bisi, A.3    Fabbri, G.4    Andrisano, V.5    Cavrini, V.6
  • 42
    • 15444346099 scopus 로고    scopus 로고
    • Acetylcholinesterase inhibitors: Synthesis and structure-activity relationships of ω-[N-methyl-N-(3-alkylcarbamoyloxyphenyl)-methyl]aminoalkoxyheteroaryl derivatives
    • Rampa A., Bisi A., Valenti P., Recanatini M., Cavalli A., Andrisano V., Cavrini V., Fin L., Buriani A., Giusti P. Acetylcholinesterase inhibitors: synthesis and structure-activity relationships of ω-[N-methyl-N-(3-alkylcarbamoyloxyphenyl)-methyl]aminoalkoxyheteroaryl derivatives. J. Med. Chem. 41:1998;3976-3986.
    • (1998) J. Med. Chem. , vol.41 , pp. 3976-3986
    • Rampa, A.1    Bisi, A.2    Valenti, P.3    Recanatini, M.4    Cavalli, A.5    Andrisano, V.6    Cavrini, V.7    Fin, L.8    Buriani, A.9    Giusti, P.10


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.