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Volumn 29, Issue 19, 2010, Pages 3408-3420

Neurotoxicity of Alzheimer's disease Aβ peptides is induced by small changes in the Aβ42 to Aβ40 ratio

Author keywords

Alzheimer's disease; b amyloid peptides; microelectrode array; neurotoxicity; oligomer

Indexed keywords

AMYLOID; AMYLOID BETA PROTEIN[1-40]; AMYLOID BETA PROTEIN[1-42]; OLIGOMER; AMYLOID BETA PROTEIN; AMYLOID BETA-PROTEIN (1-42); FLUORESCENT DYE; PEPTIDE FRAGMENT; PROTEIN BINDING; THIAZOLE DERIVATIVE; THIOFLAVINE;

EID: 77957785420     PISSN: 02614189     EISSN: 14602075     Source Type: Journal    
DOI: 10.1038/emboj.2010.211     Document Type: Article
Times cited : (439)

References (56)
  • 2
    • 0029969354 scopus 로고    scopus 로고
    • Glutamine synthetase-induced enhancement of beta-amyloid peptide A beta (1-40) neurotoxicity accompanied by abrogation of fibril formation and A beta fragmentation
    • Aksenov MY, Aksenova MV, Butterfield DA, Hensley K, Vigo-Pelfrey C, Carney JM (1996) Glutamine synthetase-induced enhancement of beta-amyloid peptide A beta (1-40) neurotoxicity accompanied by abrogation of fibril formation and A beta fragmentation. J Neurochem 66: 2050-2056
    • (1996) J Neurochem , vol.66 , pp. 2050-2056
    • Aksenov, M.Y.1    Aksenova, M.V.2    Butterfield, D.A.3    Hensley, K.4    Vigo-Pelfrey, C.5    Carney, J.M.6
  • 3
    • 0036441486 scopus 로고    scopus 로고
    • A cell biological perspective on Alzheimer's disease
    • Annaert W, De Strooper B (2002) A cell biological perspective on Alzheimer's disease. Annu Rev Cell Dev Biol 18: 25-51
    • (2002) Annu Rev Cell Dev Biol , vol.18 , pp. 25-51
    • Annaert, W.1    De Strooper, B.2
  • 5
    • 34249696007 scopus 로고    scopus 로고
    • Rapid, concurrent alterations in pre-and postsynaptic structure induced by naturally-secreted amyloid-beta protein
    • Calabrese B, Shaked GM, Tabarean IV, Braga J, Koo EH, Halpain S (2007) Rapid, concurrent alterations in pre-and postsynaptic structure induced by naturally-secreted amyloid-beta protein. Mol Cell Neurosci 35: 183-193
    • (2007) Mol Cell Neurosci , vol.35 , pp. 183-193
    • Calabrese, B.1    Shaked, G.M.2    Tabarean, I.V.3    Braga, J.4    Koo, E.H.5    Halpain, S.6
  • 7
    • 0017250407 scopus 로고
    • Infrared spectra and resonance interaction of amide-I vibration of the paraellel-chain pleated sheets
    • Chirgadze YN, Nevskaya NA (1976) Infrared spectra and resonance interaction of amide-I vibration of the paraellel-chain pleated sheets. Biopolymers 15: 627-636
    • (1976) Biopolymers , vol.15 , pp. 627-636
    • Chirgadze, Y.N.1    Nevskaya, N.A.2
  • 10
    • 33947201115 scopus 로고    scopus 로고
    • Loss-of-function presenilin mutations in Alzheimer disease. Talking Point on the role of presenilin mutations in Alzheimer disease
    • De Strooper B (2007) Loss-of-function presenilin mutations in Alzheimer disease. Talking Point on the role of presenilin mutations in Alzheimer disease. EMBO Rep 8: 141-146
    • (2007) EMBO Rep , vol.8 , pp. 141-146
    • De Strooper, B.1
  • 11
    • 77951060145 scopus 로고    scopus 로고
    • Proteases and proteolysis in Alzheimer disease: A multifactorial view on the disease process
    • De Strooper B (2010) Proteases and proteolysis in Alzheimer disease: a multifactorial view on the disease process. Physiol Rev 90: 465-494
    • (2010) Physiol Rev , vol.90 , pp. 465-494
    • De Strooper, B.1
  • 13
    • 0037294045 scopus 로고    scopus 로고
    • Co-incorporation of A beta 40 and A beta 42 to form mixed pre-fibrillar aggregates
    • Frost D, Gorman PM, Yip CM, Chakrabartty A (2003) Co-incorporation of A beta 40 and A beta 42 to form mixed pre-fibrillar aggregates. Eur J Biochem 270: 654-663
    • (2003) Eur J Biochem , vol.270 , pp. 654-663
    • Frost, D.1    Gorman, P.M.2    Yip, C.M.3    Chakrabartty, A.4
  • 14
    • 0042838303 scopus 로고    scopus 로고
    • Alzheimer's disease-affected brain: Presence of oligomeric A beta ligands (ADDLs) suggests a molecular basis for reversible memory loss
    • Gong Y, Chang L, Viola KL, Lacor PN, Lambert MP, Finch CE, Krafft GA, Klein WL (2003) Alzheimer's disease-affected brain: presence of oligomeric A beta ligands (ADDLs) suggests a molecular basis for reversible memory loss. Proc Natl Acad Sci USA 100: 10417-10422
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 10417-10422
    • Gong, Y.1    Chang, L.2    Viola, K.L.3    Lacor, P.N.4    Lambert, M.P.5    Finch, C.E.6    Krafft, G.A.7    Klein, W.L.8
  • 15
    • 0028723860 scopus 로고
    • Determination of soluble and membrane protein structure by Fourier transform infrared spectroscopy. II. Experimental aspects, side chain structure, and H/D exchange
    • Goormaghtigh E, Cabiaux V, Ruysschaert JM (1994) Determination of soluble and membrane protein structure by Fourier transform infrared spectroscopy. II. Experimental aspects, side chain structure, and H/D exchange. Subcell Biochem 23: 363-403
    • (1994) Subcell Biochem , vol.23 , pp. 363-403
    • Goormaghtigh, E.1    Cabiaux, V.2    Ruysschaert, J.M.3
  • 16
    • 0027333557 scopus 로고
    • Cellular processing of beta-amyloid precursor protein and the genesis of amyloid beta-peptide
    • Haass C, Selkoe DJ (1993) Cellular processing of beta-amyloid precursor protein and the genesis of amyloid beta-peptide. Cell 75: 1039-1042
    • (1993) Cell , vol.75 , pp. 1039-1042
    • Haass, C.1    Selkoe, D.J.2
  • 17
    • 0037135111 scopus 로고    scopus 로고
    • The amyloid hypothesis of Alzheimer's disease: Progress and problems on the road to therapeutics
    • Hardy J, Selkoe DJ (2002) The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics. Science 297: 353-356
    • (2002) Science , vol.297 , pp. 353-356
    • Hardy, J.1    Selkoe, D.J.2
  • 18
    • 0030908095 scopus 로고    scopus 로고
    • Models of amyloid seeding in Alzheimer's disease and scrapie: Mechanistic truths and physiological consequences of the time-dependent solubility of amyloid proteins
    • Harper JD, Lansbury Jr PT (1997) Models of amyloid seeding in Alzheimer's disease and scrapie: mechanistic truths and physiological consequences of the time-dependent solubility of amyloid proteins. Annu Rev Biochem 66: 385-407
    • (1997) Annu Rev Biochem , vol.66 , pp. 385-407
    • Harper, J.D.1    Lansbury Jr., P.T.2
  • 19
    • 0033570337 scopus 로고    scopus 로고
    • Protofibrillar intermediates of amyloid beta-protein induce acute electrophysiological changes and progressive neurotoxicity in cortical neurons
    • Hartley DM, Walsh DM, Ye CP, Diehl T, Vasquez S, Vassilev PM, Teplow DB, Selkoe DJ (1999) Protofibrillar intermediates of amyloid beta-protein induce acute electrophysiological changes and progressive neurotoxicity in cortical neurons. J Neurosci 19: 8876-8884
    • (1999) J Neurosci , vol.19 , pp. 8876-8884
    • Hartley, D.M.1    Walsh, D.M.2    Ye, C.P.3    Diehl, T.4    Vasquez, S.5    Vassilev, P.M.6    Teplow, D.B.7    Selkoe, D.J.8
  • 21
    • 73949089674 scopus 로고    scopus 로고
    • Amyloid seeds formed by cellular uptake, concentration, and aggregation of the amyloid-beta peptide
    • Hu X, Crick SL, Bu G, Frieden C, Pappu RV, Lee JM (2009) Amyloid seeds formed by cellular uptake, concentration, and aggregation of the amyloid-beta peptide. Proc Natl Acad Sci USA 106: 20324-20329
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 20324-20329
    • Hu, X.1    Crick, S.L.2    Bu, G.3    Frieden, C.4    Pappu, R.V.5    Lee, J.M.6
  • 22
    • 57149145222 scopus 로고    scopus 로고
    • The ratio of monomeric to aggregated forms of Abeta40 and Abeta42 is an important determinant of amyloid-beta aggregation, fibrillogen-esis, and toxicity
    • Jan A, Gokce O, Luthi-Carter R, Lashuel HA (2008) The ratio of monomeric to aggregated forms of Abeta40 and Abeta42 is an important determinant of amyloid-beta aggregation, fibrillogen-esis, and toxicity. J Biol Chem 283: 28176-28189
    • (2008) J Biol Chem , vol.283 , pp. 28176-28189
    • Jan, A.1    Gokce, O.2    Luthi-Carter, R.3    Lashuel, H.A.4
  • 23
    • 0027195933 scopus 로고
    • Seeding 'one-dimensional crystallization' of amyloid: A pathogenic mechanism in Alzheimer's disease and scrapie?
    • Jarrett JT, Lansbury Jr PT. (1993) Seeding 'one-dimensional crystallization' of amyloid: a pathogenic mechanism in Alzheimer's disease and scrapie? Cell 73: 1055-1058
    • (1993) Cell , vol.73 , pp. 1055-1058
    • Jarrett, J.T.1    Lansbury Jr., P.T.2
  • 24
    • 33744957163 scopus 로고    scopus 로고
    • Equimolar production of amyloid beta-protein and amyloid precursor protein intracellular domain from beta-carboxyl-terminal fragment by gamma-secretase
    • Kakuda N, Funamoto S, Yagishita S, Takami M, Osawa S, Dohmae N, Ihara Y (2006) Equimolar production of amyloid beta-protein and amyloid precursor protein intracellular domain from beta-carboxyl-terminal fragment by gamma-secretase. J Biol Chem 281: 14776-14786
    • (2006) J Biol Chem , vol.281 , pp. 14776-14786
    • Kakuda, N.1    Funamoto, S.2    Yagishita, S.3    Takami, M.4    Osawa, S.5    Dohmae, N.6    Ihara, Y.7
  • 28
    • 33846633336 scopus 로고    scopus 로고
    • Abeta oligomer-induced aberrations in synapse composition, shape, and density provide a molecular basis for loss of connectivity in Alzheimer's disease
    • Lacor PN, Buniel MC, Furlow PW, Clemente AS, Velasco PT, Wood M, Viola KL, Klein WL (2007) Abeta oligomer-induced aberrations in synapse composition, shape, and density provide a molecular basis for loss of connectivity in Alzheimer's disease. J Neurosci 27: 796-807
    • (2007) J Neurosci , vol.27 , pp. 796-807
    • Lacor, P.N.1    Buniel, M.C.2    Furlow, P.W.3    Clemente, A.S.4    Velasco, P.T.5    Wood, M.6    Viola, K.L.7    Klein, W.L.8
  • 31
    • 61349201380 scopus 로고    scopus 로고
    • Cellular prion protein mediates impairment of synaptic plasticity by amyloid-beta oligomers
    • Lauren J, Gimbel DA, Nygaard HB, Gilbert JW, Strittmatter SM (2009) Cellular prion protein mediates impairment of synaptic plasticity by amyloid-beta oligomers. Nature 457: 1128-1132
    • (2009) Nature , vol.457 , pp. 1128-1132
    • Lauren, J.1    Gimbel, D.A.2    Nygaard, H.B.3    Gilbert, J.W.4    Strittmatter, S.M.5
  • 35
    • 70349295278 scopus 로고    scopus 로고
    • Structure-neurotoxicity relationships of amyloid beta-protein oligomers
    • Ono K, Condron MM, Teplow DB (2009) Structure-neurotoxicity relationships of amyloid beta-protein oligomers. Proc Natl Acad Sci USA 106: 14745-14750
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 14745-14750
    • Ono, K.1    Condron, M.M.2    Teplow, D.B.3
  • 36
    • 0028885682 scopus 로고
    • Amino-terminal deletions enhance aggregation of beta-amyloid peptides in vitro
    • Pike CJ, Overman MJ, Cotman CW (1995) Amino-terminal deletions enhance aggregation of beta-amyloid peptides in vitro. J Biol Chem 270: 23895-23898
    • (1995) J Biol Chem , vol.270 , pp. 23895-23898
    • Pike, C.J.1    Overman, M.J.2    Cotman, C.W.3
  • 37
    • 0018899387 scopus 로고
    • Recording action potentials from cultured neurons with extracellular microcircuit electrodes
    • Pine J (1980) Recording action potentials from cultured neurons with extracellular microcircuit electrodes. J Neurosci Methods 2: 19-31
    • (1980) J Neurosci Methods , vol.2 , pp. 19-31
    • Pine, J.1
  • 38
    • 0035975664 scopus 로고    scopus 로고
    • A new approach to neural cell culture for long-term studies
    • Potter SM, DeMarse TB (2001) A new approach to neural cell culture for long-term studies. J Neurosci Methods 110: 17-24
    • (2001) J Neurosci Methods , vol.110 , pp. 17-24
    • Potter, S.M.1    De Marse, T.B.2
  • 39
    • 0032989712 scopus 로고    scopus 로고
    • Tangles and plaques in nondemented aging and 'preclinical' Alzheimer's disease
    • Price JL, Morris JC (1999) Tangles and plaques in nondemented aging and 'preclinical' Alzheimer's disease. Ann Neurol 45: 358-368
    • (1999) Ann Neurol , vol.45 , pp. 358-368
    • Price, J.L.1    Morris, J.C.2
  • 42
    • 0030582387 scopus 로고    scopus 로고
    • Amino-and carboxyl-terminal heterogeneity of beta-amyloid peptides deposited in human brain
    • Saido TC, Yamao-Harigaya W, Iwatsubo T, Kawashima S (1996) Amino-and carboxyl-terminal heterogeneity of beta-amyloid peptides deposited in human brain. Neurosci Lett 215: 173-176
    • (1996) Neurosci Lett , vol.215 , pp. 173-176
    • Saido, T.C.1    Yamao-Harigaya, W.2    Iwatsubo, T.3    Kawashima, S.4
  • 49
    • 0028322017 scopus 로고
    • An increased percentage of long amyloid beta protein secreted by familial amyloid beta protein precursor (beta APP717) mutants
    • Suzuki N, Cheung TT, Cai XD, Odaka A, Otvos Jr L, Eckman C, Golde TE, Younkin SG (1994) An increased percentage of long amyloid beta protein secreted by familial amyloid beta protein precursor (beta APP717) mutants. Science 264: 1336-1340
    • (1994) Science , vol.264 , pp. 1336-1340
    • Suzuki, N.1    Cheung, T.T.2    Cai, X.D.3    Odaka, A.4    Otvos Jr., L.5    Eckman, C.6    Golde, T.E.7    Younkin, S.G.8
  • 50
    • 0025987048 scopus 로고
    • Physical basis of cognitive alterations in Alzheimer's disease: Synapse loss is the major correlate of cognitive impairment
    • Terry RD, Masliah E, Salmon DP, Butters N, DeTeresa R, Hill R, Hansen LA, Katzman R (1991) Physical basis of cognitive alterations in Alzheimer's disease: synapse loss is the major correlate of cognitive impairment. Ann Neurol 30: 572-580
    • (1991) Ann Neurol , vol.30 , pp. 572-580
    • Terry, R.D.1    Masliah, E.2    Salmon, D.P.3    Butters, N.4    Deteresa, R.5    Hill, R.6    Hansen, L.A.7    Katzman, R.8
  • 52
    • 0037041426 scopus 로고    scopus 로고
    • Naturally secreted oligomers of amyloid beta protein potently inhibit hippocampal long-term potentiation in vivo
    • Walsh DM, Klyubin I, Fadeeva JV, Cullen WK, Anwyl R, Wolfe MS, Rowan MJ, Selkoe DJ (2002) Naturally secreted oligomers of amyloid beta protein potently inhibit hippocampal long-term potentiation in vivo. Nature 416: 535-539
    • (2002) Nature , vol.416 , pp. 535-539
    • Walsh, D.M.1    Klyubin, I.2    Fadeeva, J.V.3    Cullen, W.K.4    Anwyl, R.5    Wolfe, M.S.6    Rowan, M.J.7    Selkoe, D.J.8
  • 53
    • 77957795492 scopus 로고    scopus 로고
    • Wild-type presenilin 1 protects against Alzheimer's disease mutation-induced amyloid pathology
    • Wang R, Wang B, He W, Zheng H (2006) Wild-type presenilin 1 protects against Alzheimer's disease mutation-induced amyloid pathology. J Biol Chem 29: 29
    • (2006) J Biol Chem , vol.29 , pp. 29
    • Wang, R.1    Wang, B.2    He, W.3    Zheng, H.4
  • 54
    • 18944407388 scopus 로고    scopus 로고
    • Nucleation-dependent polymerization is an essential component of amyloid-mediated neuronal cell death
    • Wogulis M, Wright S, Cunningham D, Chilcote T, Powell K, Rydel RE (2005) Nucleation-dependent polymerization is an essential component of amyloid-mediated neuronal cell death. J Neurosci 25: 1071-1080
    • (2005) J Neurosci , vol.25 , pp. 1071-1080
    • Wogulis, M.1    Wright, S.2    Cunningham, D.3    Chilcote, T.4    Powell, K.5    Rydel, R.E.6
  • 55
    • 34248586543 scopus 로고    scopus 로고
    • Abeta40 protects non-toxic Abeta42 monomer from aggregation
    • Yan Y, Wang C (2007) Abeta40 protects non-toxic Abeta42 monomer from aggregation. J Mol Biol 369: 909-916
    • (2007) J Mol Biol , vol.369 , pp. 909-916
    • Yan, Y.1    Wang, C.2
  • 56
    • 0037931149 scopus 로고    scopus 로고
    • Specific compositions of amyloid-beta peptides as the determinant of toxic beta-aggregation
    • Yoshiike Y, Chui DH, Akagi T, Tanaka N, Takashima A (2003) Specific compositions of amyloid-beta peptides as the determinant of toxic beta-aggregation. J Biol Chem 278: 23648-23655
    • (2003) J Biol Chem , vol.278 , pp. 23648-23655
    • Yoshiike, Y.1    Chui, D.H.2    Akagi, T.3    Tanaka, N.4    Takashima, A.5


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