메뉴 건너뛰기




Volumn 137, Issue 3, 2014, Pages 873-886

High molecular mass assemblies of amyloid-β oligomers bind prion protein in patients with Alzheimer's disease

Author keywords

Alzheimer's disease; amyloid neurodegeneration; amyloid oligomers; prion protein

Indexed keywords

AMYLOID BETA PROTEIN; AMYLOID BETA PROTEIN[1-42]; OLIGOMER; PRION PROTEIN;

EID: 84894555460     PISSN: 00068950     EISSN: 14602156     Source Type: Journal    
DOI: 10.1093/brain/awt375     Document Type: Article
Times cited : (97)

References (40)
  • 2
    • 84883460724 scopus 로고    scopus 로고
    • Roles of endoproteolytic alpha-cleavage and shedding of the prion protein in neurodegeneration
    • Altmeppen HC, Prox J, Puig B, Dohler F, Falker C, Krasemann S, et al. Roles of endoproteolytic alpha-cleavage and shedding of the prion protein in neurodegeneration. FEBS J 2013; 280: 4338-47.
    • (2013) FEBS J , vol.280 , pp. 4338-4347
    • Altmeppen, H.C.1    Prox, J.2    Puig, B.3    Dohler, F.4    Falker, C.5    Krasemann, S.6
  • 3
    • 79956302348 scopus 로고    scopus 로고
    • Alzheimer's disease brain-derived amyloid-beta-mediated inhibition of LTP in vivo is prevented by immunotargeting cellular prion protein
    • Barry AE, Klyubin I, Mc Donald JM, Mably AJ, Farrell MA, Scott M, et al. Alzheimer's disease brain-derived amyloid-beta-mediated inhibition of LTP in vivo is prevented by immunotargeting cellular prion protein. J Neurosci 2011; 31: 7259-63.
    • (2011) J Neurosci , vol.31 , pp. 7259-7263
    • Barry, A.E.1    Klyubin, I.2    Mc Donald, J.M.3    Mably, A.J.4    Farrell, M.A.5    Scott, M.6
  • 4
    • 84857834839 scopus 로고    scopus 로고
    • The prion protein unstructured N-terminal region is a broad-spectrum molecular sensor with diverse and contrasting potential functions
    • Beland M, Roucou X. The prion protein unstructured N-terminal region is a broad-spectrum molecular sensor with diverse and contrasting potential functions. J Neurochem 2012; 120: 853-68.
    • (2012) J Neurochem , vol.120 , pp. 853-868
    • Beland, M.1    Roucou, X.2
  • 5
    • 77956965281 scopus 로고    scopus 로고
    • Prion protein in Alzheimer's pathogenesis: A hot and controversial issue
    • Benilova I, De Strooper B. Prion protein in Alzheimer's pathogenesis: a hot and controversial issue. EMBO Mol Med 2010; 2: 289-90.
    • (2010) EMBO Mol Med , vol.2 , pp. 289-290
    • Benilova, I.1    De Strooper, B.2
  • 6
    • 76449085569 scopus 로고    scopus 로고
    • Gamma-secretases: From cell biology to therapeutic strategies
    • Bergmans BA, De Strooper B. gamma-secretases: from cell biology to therapeutic strategies. Lancet Neurol 2010; 9: 215-26.
    • (2010) Lancet Neurol , vol.9 , pp. 215-226
    • Bergmans, B.A.1    De Strooper, B.2
  • 7
    • 33845892752 scopus 로고    scopus 로고
    • Systematic meta-analyses of Alzheimer disease genetic association studies: The AlzGene database
    • Bertram L, McQueen MB, Mullin K, Blacker D, Tanzi RE. Systematic meta-analyses of Alzheimer disease genetic association studies: the AlzGene database. Nat Genet 2007; 39: 17-23.
    • (2007) Nat Genet , vol.39 , pp. 17-23
    • Bertram, L.1    McQueen, M.B.2    Mullin, K.3    Blacker, D.4    Tanzi, R.E.5
  • 9
    • 0025863618 scopus 로고
    • Neuropathological stageing of Alzheimer-related changes
    • Braak H, Braak E. Neuropathological stageing of Alzheimer-related changes. Acta Neuropathol 1991; 82: 239-59.
    • (1991) Acta Neuropathol , vol.82 , pp. 239-259
    • Braak, H.1    Braak, E.2
  • 10
    • 77956197815 scopus 로고    scopus 로고
    • Interaction between human prion protein and amyloid-beta (Abeta) oligomers: Role of N-terminal residues
    • Chen S, Yadav SP, Surewicz WK. Interaction between human prion protein and amyloid-beta (Abeta) oligomers: role OF N-terminal residues. J Biol Chem 2010; 285: 26377-83.
    • (2010) J Biol Chem , vol.285 , pp. 26377-26383
    • Chen, S.1    Yadav, S.P.2    Surewicz, W.K.3
  • 12
    • 34249672242 scopus 로고    scopus 로고
    • Abeta oligomers induce neuronal oxidative stress through an N-methyl-D-aspartate receptor-dependent mechanism that is blocked by the Alzheimer drug memantine
    • De Felice FG, Velasco PT, Lambert MP, Viola K, Fernandez SJ, Ferreira ST, et al. Abeta oligomers induce neuronal oxidative stress through an N-methyl-D-aspartate receptor-dependent mechanism that is blocked by the Alzheimer drug memantine. J Biol Chem 2007; 282: 11590-601.
    • (2007) J Biol Chem , vol.282 , pp. 11590-11601
    • De Felice, F.G.1    Velasco, P.T.2    Lambert, M.P.3    Viola, K.4    Fernandez, S.J.5    Ferreira, S.T.6
  • 13
    • 49849091894 scopus 로고    scopus 로고
    • Association between deposition of beta-amyloid and pathological prion protein in sporadic Creutzfeldt-Jakob disease
    • Debatin L, Streffer J, Geissen M, Matschke J, Aguzzi A, Glatzel M. Association between deposition of beta-amyloid and pathological prion protein in sporadic Creutzfeldt-Jakob disease. Neurodegener Dis 2008; 5: 347-54.
    • (2008) Neurodegener Dis , vol.5 , pp. 347-354
    • Debatin, L.1    Streffer, J.2    Geissen, M.3    Matschke, J.4    Aguzzi, A.5    Glatzel, M.6
  • 16
    • 84875174182 scopus 로고    scopus 로고
    • An N-terminal fragment of the prion protein binds to amyloid-beta oligomers and inhibits their neurotoxicity in vivo
    • Fluharty BR, Biasini E, Stravalaci M, Sclip A, Diomede L, Balducci C, et al. An N-terminal fragment of the prion protein binds to amyloid-beta oligomers and inhibits their neurotoxicity in vivo. J Biol Chem 2013; 288: 7857-66.
    • (2013) J Biol Chem , vol.288 , pp. 7857-7866
    • Fluharty, B.R.1    Biasini, E.2    Stravalaci, M.3    Sclip, A.4    Diomede, L.5    Balducci, C.6
  • 18
    • 79958249995 scopus 로고    scopus 로고
    • Interaction between prion protein and toxic amyloid beta assemblies can be therapeutically targeted at multiple sites
    • Freir DB, Nicoll AJ, Klyubin I, Panico S, Mc Donald JM, Risse E, et al. Interaction between prion protein and toxic amyloid beta assemblies can be therapeutically targeted at multiple sites. Nat Commun 2011; 2: 336.
    • (2011) Nat Commun , vol.2 , pp. 336
    • Freir, D.B.1    Nicoll, A.J.2    Klyubin, I.3    Panico, S.4    Mc Donald, J.M.5    Risse, E.6
  • 19
    • 34447092796 scopus 로고    scopus 로고
    • Understanding the natural variability of prion diseases
    • Geissen M, Krasemann S, Matschke J, Glatzel M. Understanding the natural variability of prion diseases. Vaccine 2007; 25: 5631-6.
    • (2007) Vaccine , vol.25 , pp. 5631-5636
    • Geissen, M.1    Krasemann, S.2    Matschke, J.3    Glatzel, M.4
  • 22
    • 72149127389 scopus 로고    scopus 로고
    • The alpha-secretase-derived N-terminal product of cellular prion N1, displays neuroprotective function in vitro and in vivo
    • Guillot-Sestier MV, Sunyach C, Druon C, Scarzello S, Checler F. The alpha-secretase-derived N-terminal product of cellular prion, N1, displays neuroprotective function in vitro and in vivo. J Biol Chem 2009; 284: 35973-86.
    • (2009) J Biol Chem , vol.284 , pp. 35973-35986
    • Guillot-Sestier, M.V.1    Sunyach, C.2    Druon, C.3    Scarzello, S.4    Checler, F.5
  • 23
    • 84856845217 scopus 로고    scopus 로고
    • Alpha-Secretase-derived fragment of cellular prion, N1, protects against monomeric and oligomeric amyloid beta (Abeta)-associated cell death
    • Guillot-Sestier MV, Sunyach C, Ferreira ST, Marzolo MP, Bauer C, Thevenet A, et al. alpha-Secretase-derived fragment of cellular prion, N1, protects against monomeric and oligomeric amyloid beta (Abeta)-associated cell death. J Biol Chem 2012; 287: 5021-32.
    • (2012) J Biol Chem , vol.287 , pp. 5021-5032
    • Guillot-Sestier, M.V.1    Sunyach, C.2    Ferreira, S.T.3    Marzolo, M.P.4    Bauer, C.5    Thevenet, A.6
  • 24
    • 27744605030 scopus 로고    scopus 로고
    • Clean Western blot signals from immunoprecipitated samples
    • Lal A, Haynes SR, Gorospe M. Clean Western blot signals from immunoprecipitated samples. Mol Cell Probes 2005; 19: 385-8.
    • (2005) Mol Cell Probes , vol.19 , pp. 385-388
    • Lal, A.1    Haynes, S.R.2    Gorospe, M.3
  • 25
    • 84869992747 scopus 로고    scopus 로고
    • The complex PrP(c)-Fyn couples human oligomeric Abeta with pathological tau changes in Alzheimer's disease
    • Larson M, Sherman MA, Amar F, Nuvolone M, Schneider JA, Bennett DA, et al. The complex PrP(c)-Fyn couples human oligomeric Abeta with pathological tau changes in Alzheimer's disease. J Neurosci 2012; 32: 16857-71a.
    • (2012) J Neurosci , vol.32 , pp. 16857-16871
    • Larson, M.1    Sherman, M.A.2    Amar, F.3    Nuvolone, M.4    Schneider, J.A.5    Bennett, D.A.6
  • 26
    • 61349201380 scopus 로고    scopus 로고
    • Cellular prion protein mediates impairment of synaptic plasticity by amyloidbeta oligomers
    • Lauren J, Gimbel DA, Nygaard HB, Gilbert JW, Strittmatter SM. Cellular prion protein mediates impairment of synaptic plasticity by amyloidbeta oligomers. Nature 2009; 457: 1128-32.
    • (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
  • 28
    • 70450257636 scopus 로고    scopus 로고
    • Isolation and characterization of patient-derived, toxic, high mass amyloid beta-protein (Abeta) assembly from Alzheimer disease brains
    • Noguchi A, Matsumura S, Dezawa M, Tada M, Yanazawa M, Ito A, et al. Isolation and characterization of patient-derived, toxic, high mass amyloid beta-protein (Abeta) assembly from Alzheimer disease brains. J Biol Chem 2009; 284: 32895-905.
    • (2009) J Biol Chem , vol.284 , pp. 32895-32905
    • Noguchi, A.1    Matsumura, S.2    Dezawa, M.3    Tada, M.4    Yanazawa, M.5    Ito, A.6
  • 30
    • 79956110918 scopus 로고    scopus 로고
    • The cellular prion protein mediates neurotoxic signalling of beta-sheet-rich conformers independent of prion replication
    • Resenberger UK, Harmeier A, Woerner AC, Goodman JL, Muller V, Krishnan R, et al. The cellular prion protein mediates neurotoxic signalling of beta-sheet-rich conformers independent of prion replication. EMBO J 2011; 30: 2057-70.
    • (2011) EMBO J , vol.30 , pp. 2057-2070
    • Resenberger, U.K.1    Harmeier, A.2    Woerner, A.C.3    Goodman, J.L.4    Muller, V.5    Krishnan, R.6
  • 31
    • 84875981923 scopus 로고    scopus 로고
    • Prion proteinmediated toxicity of amyloid-beta oligomers requires lipid rafts and the transmembrane LRP1
    • Rushworth JV, Griffiths HH, Watt NT, Hooper NM. Prion proteinmediated toxicity of amyloid-beta oligomers requires lipid rafts and the transmembrane LRP1. J Biol Chem 2013; 288: 8935-51.
    • (2013) J Biol Chem , vol.288 , pp. 8935-8951
    • Rushworth, J.V.1    Griffiths, H.H.2    Watt, N.T.3    Hooper, N.M.4
  • 34
    • 84866065959 scopus 로고    scopus 로고
    • Alzheimer amyloid-beta oligomer bound to postsynaptic prion protein activates Fyn to impair neurons
    • Um JW, Nygaard HB, Heiss JK, Kostylev MA, Stagi M, Vortmeyer A, et al. Alzheimer amyloid-beta oligomer bound to postsynaptic prion protein activates Fyn to impair neurons. Nat Neurosci 2012; 15: 1227-35.
    • (2012) Nat Neurosci , vol.15 , pp. 1227-1235
    • Um, J.W.1    Nygaard, H.B.2    Heiss, J.K.3    Kostylev, M.A.4    Stagi, M.5    Vortmeyer, A.6
  • 35
    • 84874585213 scopus 로고    scopus 로고
    • Amyloid-beta induced signaling by cellular prion protein and Fyn kinase in Alzheimer disease
    • Um JW, Strittmatter SM. Amyloid-beta induced signaling by cellular prion protein and Fyn kinase in Alzheimer disease. Prion 2013; 7: 37-41.
    • (2013) Prion , vol.7 , pp. 37-41
    • Um, J.W.1    Strittmatter, S.M.2
  • 36
    • 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, et al. Naturally secreted oligomers of amyloid beta protein potently inhibit hippocampal long-term potentiation in vivo. Nature 2002; 416: 535-9.
    • (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
  • 37
    • 0024550204 scopus 로고
    • Identification, biogenesis, and localization of precursors of Alzheimer's disease A4 amyloid protein
    • Weidemann A, Konig G, Bunke D, Fischer P, Salbaum JM, Masters CL, et al. Identification, biogenesis, and localization of precursors of Alzheimer's disease A4 amyloid protein. Cell 1989; 57: 115-26.
    • (1989) Cell , vol.57 , pp. 115-126
    • Weidemann, A.1    Konig, G.2    Bunke, D.3    Fischer, P.4    Salbaum, J.M.5    Masters, C.L.6
  • 38
    • 84866542395 scopus 로고    scopus 로고
    • The P's and Q's of cellular PrP-Abeta interactions
    • Westaway D, Jhamandas JH. The P's and Q's of cellular PrP-Abeta interactions. Prion 2012; 6: 359-63.
    • (2012) Prion , vol.6 , pp. 359-363
    • Westaway, D.1    Jhamandas, J.H.2
  • 39
    • 84877144645 scopus 로고    scopus 로고
    • The cellular prion protein traps Alzheimer's Abeta in an oligomeric form and disassembles amyloid fibers
    • Younan ND, Sarell CJ, Davies P, Brown DR, Viles JH. The cellular prion protein traps Alzheimer's Abeta in an oligomeric form and disassembles amyloid fibers. FASEB J 2013; 27: 1847-58.
    • (2013) FASEB J , vol.27 , pp. 1847-1858
    • Younan, N.D.1    Sarell, C.J.2    Davies, P.3    Brown, D.R.4    Viles, J.H.5
  • 40
    • 79955393816 scopus 로고    scopus 로고
    • Amyloidbeta42 interacts mainly with insoluble prion protein in the Alzheimer brain
    • Zou WQ, Xiao X, Yuan J, Puoti G, Fujioka H, Wang X, et al. Amyloidbeta42 interacts mainly with insoluble prion protein in the Alzheimer brain. J Biol Chem 2011; 286: 15095-105.
    • (2011) J Biol Chem , vol.286 , pp. 15095-15105
    • Zou, W.Q.1    Xiao, X.2    Yuan, J.3    Puoti, G.4    Fujioka, H.5    Wang, X.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.