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Volumn 288, Issue 13, 2013, Pages 8935-8951

Prion protein-mediated toxicity of amyloid-β oligomers requires lipid rafts and the transmembrane LRP1

Author keywords

[No Author keywords available]

Indexed keywords

ALZHEIMER DISEASE; AMYLOID PRECURSOR PROTEINS; CELLULAR PRION PROTEINS; COLOCALIZATION; EPIGALLOCATECHIN GALLATE; GREEN TEA POLYPHENOLS; LOW DENSITY LIPOPROTEINS; POTENTIAL TARGETS;

EID: 84875981923     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.400358     Document Type: Article
Times cited : (130)

References (72)
  • 1
    • 33745893779 scopus 로고    scopus 로고
    • Alzheimer disease: Progress or profit?
    • Mount, C., and Downton, C. (2006) Alzheimer disease: progress or profit? Nat. Med. 12, 780-784
    • (2006) Nat. Med. , vol.12 , pp. 780-784
    • Mount, C.1    Downton, C.2
  • 3
    • 77951776829 scopus 로고    scopus 로고
    • Alzheimer's disease: Strategies for disease modification
    • Citron, M. (2010) Alzheimer's disease: strategies for disease modification. Nat. Rev. Drug Discov. 9, 387-398
    • (2010) Nat. Rev. Drug Discov. , vol.9 , pp. 387-398
    • Citron, M.1
  • 4
    • 67651180986 scopus 로고    scopus 로고
    • The amyloid hypothesis for Alzheimer's disease: A critical reappraisal
    • Hardy, J. (2009) The amyloid hypothesis for Alzheimer's disease: a critical reappraisal. J. Neurochem. 110, 1129-1134
    • (2009) J. Neurochem. , vol.110 , pp. 1129-1134
    • Hardy, J.1
  • 8
    • 0037041426 scopus 로고    scopus 로고
    • Naturally secreted oligomers of amyloid β protein potently inhibit hippocampal long-term potentiation in vivo
    • Walsh, D. M., Klyubin, I., Fadeeva, J. V., Cullen, W. K., Anwyl, R., Wolfe, M. S., Rowan, M. J., and Selkoe, D. J. (2002) Naturally secreted oligomers of amyloid β 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
  • 11
    • 61349201380 scopus 로고    scopus 로고
    • Cellular prion protein mediates impairment of synaptic plasticity by amyloid-β oligomers
    • Laurén, J., Gimbel, D. A., Nygaard, H. B., Gilbert, J. W., and Strittmatter, S. M. (2009) Cellular prion protein mediates impairment of synaptic plasticity by amyloid-β oligomers. Nature 457, 1128-1132
    • (2009) Nature , vol.457 , pp. 1128-1132
    • Laurén, J.1    Gimbel, D.A.2    Nygaard, H.B.3    Gilbert, J.W.4    Strittmatter, S.M.5
  • 13
    • 33645290776 scopus 로고    scopus 로고
    • The prion protein and lipid rafts
    • Taylor, D. R., and Hooper, N. M. (2006) The prion protein and lipid rafts. Mol. Membr. Biol. 23, 89-99
    • (2006) Mol. Membr. Biol. , vol.23 , pp. 89-99
    • Taylor, D.R.1    Hooper, N.M.2
  • 14
    • 77956197815 scopus 로고    scopus 로고
    • Interaction between human prion protein and amyloid-β (Aβ) oligomers
    • Chen, S., Yadav, S. P., and Surewicz, W. K. (2010) Interaction between human prion protein and amyloid-β (Aβ) oligomers. J. Biol. Chem. 285, 26377-26383
    • (2010) J. Biol. Chem. , vol.285 , pp. 26377-26383
    • Chen, S.1    Yadav, S.P.2    Surewicz, W.K.3
  • 15
    • 77957778860 scopus 로고    scopus 로고
    • Anti-PrPC monoclonal antibody infusion as a novel treatment for cognitive deficits in an Alzheimer's disease model mouse
    • Chung, E., Ji, Y., Sun, Y., Kascsak, R. J., Kascsak, R. B., Mehta, P. D., Strittmatter, S. M., and Wisniewski, T. (2010) Anti-PrPC monoclonal antibody infusion as a novel treatment for cognitive deficits in an Alzheimer's disease model mouse. BMC Neurosci. 11, 130
    • (2010) BMC Neurosci. , vol.11 , pp. 130
    • Chung, E.1    Ji, Y.2    Sun, Y.3    Kascsak, R.J.4    Kascsak, R.B.5    Mehta, P.D.6    Strittmatter, S.M.7    Wisniewski, T.8
  • 16
    • 79956302348 scopus 로고    scopus 로고
    • Alzheimer's disease brainderived amyloid-β-mediated inhibition of LTP in vivo is prevented by immunotargeting cellular prion protein
    • Barry, A. E., Klyubin, I.,McDonald, J. M., Mably, A. J., Farrell, M. A., Scott, M., Walsh, D. M., and Rowan, M. J. (2011) Alzheimer's disease brainderived amyloid-β-mediated inhibition of LTP in vivo is prevented by immunotargeting cellular prion protein. J. Neurosci. 31, 7259-7263
    • (2011) J. Neurosci. , vol.31 , pp. 7259-7263
    • Barry, A.E.1    Klyubin, I.2    McDonald, J.M.3    Mably, A.J.4    Farrell, M.A.5    Scott, M.6    Walsh, D.M.7    Rowan, M.J.8
  • 18
    • 80055071341 scopus 로고    scopus 로고
    • Amyloid-β-induced synapse damage is mediated via cross-linkage of cellular prion proteins
    • Bate, C., and Williams, A. (2011) Amyloid-β-induced synapse damage is mediated via cross-linkage of cellular prion proteins. J. Biol. Chem. 286, 37955-37963
    • (2011) J. Biol. Chem. , vol.286 , pp. 37955-37963
    • Bate, C.1    Williams, A.2
  • 22
    • 77955617917 scopus 로고    scopus 로고
    • The prion protein as a receptor for amyloid-β
    • Kessels, H. W., Nguyen, L. N., Nabavi, S., and Malinow, R. (2010) The prion protein as a receptor for amyloid-β. Nature 466, E3-4
    • (2010) Nature , vol.466
    • Kessels, H.W.1    Nguyen, L.N.2    Nabavi, S.3    Malinow, R.4
  • 23
    • 26244462301 scopus 로고    scopus 로고
    • Proteolytic mechanisms in amyloid-β metabolism: Therapeutic implications for Alzheimer's disease
    • Vardy, E. R., Catto, A. J., and Hooper, N. M. (2005) Proteolytic mechanisms in amyloid-β metabolism: therapeutic implications for Alzheimer's disease. Trends Mol. Med. 11, 464-472
    • (2005) Trends Mol. Med. , vol.11 , pp. 464-472
    • Vardy, E.R.1    Catto, A.J.2    Hooper, N.M.3
  • 26
    • 74249114011 scopus 로고    scopus 로고
    • Prion protein and Alzheimer disease
    • Kellett, K. A., and Hooper, N. M. (2009) Prion protein and Alzheimer disease. Prion 3, 190-194
    • (2009) Prion , vol.3 , pp. 190-194
    • Kellett, K.A.1    Hooper, N.M.2
  • 27
    • 34248190279 scopus 로고    scopus 로고
    • Aβ oligomers-a decade of discovery
    • Walsh, D. M., and Selkoe, D. J. (2007)Aβ oligomers-a decade of discovery. J. Neurochem. 101, 1172-1184
    • (2007) J. Neurochem. , vol.101 , pp. 1172-1184
    • Walsh, D.M.1    Selkoe, D.J.2
  • 28
    • 57649148788 scopus 로고    scopus 로고
    • Structural classification of toxic amyloid oligomers
    • Glabe, C. G. (2008) Structural classification of toxic amyloid oligomers. J. Biol. Chem. 283, 29639-29643
    • (2008) J. Biol. Chem. , vol.283 , pp. 29639-29643
    • Glabe, C.G.1
  • 30
    • 33749507375 scopus 로고    scopus 로고
    • Conformation-dependent anti-amyloid oligomer antibodies
    • Kayed, R., and Glabe, C. G. (2006) Conformation-dependent anti-amyloid oligomer antibodies. Methods Enzymol. 413, 326-344
    • (2006) Methods Enzymol. , vol.413 , pp. 326-344
    • Kayed, R.1    Glabe, C.G.2
  • 31
  • 32
    • 68149162581 scopus 로고    scopus 로고
    • Soluble fibrillar oligomer levels are elevated in Alzheimer's disease brain and correlate with cognitive dysfunction
    • Tomic, J. L., Pensalfini, A., Head, E., and Glabe, C. G. (2009) Soluble fibrillar oligomer levels are elevated in Alzheimer's disease brain and correlate with cognitive dysfunction. Neurobiol. Dis. 35, 352-358
    • (2009) Neurobiol. Dis. , vol.35 , pp. 352-358
    • Tomic, J.L.1    Pensalfini, A.2    Head, E.3    Glabe, C.G.4
  • 36
    • 0035799312 scopus 로고    scopus 로고
    • Ablation of the metal ion-induced endocytosis of the prion protein by disease-associated mutation of the octarepeat region
    • Perera, W. S., and Hooper, N. M. (2001) Ablation of the metal ion-induced endocytosis of the prion protein by disease-associated mutation of the octarepeat region. Curr. Biol. 11, 519-523
    • (2001) Curr. Biol. , vol.11 , pp. 519-523
    • Perera, W.S.1    Hooper, N.M.2
  • 37
    • 0030027934 scopus 로고    scopus 로고
    • Bicistronic vector for the creation of stable mammalian cell lines that predisposes all antibiotic-resistant cells to express recombinant protein
    • Rees, S., Coote, J., Stables, J., Goodson, S., Harris, S., and Lee, M. G. (1996) Bicistronic vector for the creation of stable mammalian cell lines that predisposes all antibiotic-resistant cells to express recombinant protein. BioTechniques 20, 102-104
    • (1996) BioTechniques , vol.20 , pp. 102-104
    • Rees, S.1    Coote, J.2    Stables, J.3    Goodson, S.4    Harris, S.5    Lee, M.G.6
  • 40
    • 27944486535 scopus 로고    scopus 로고
    • Assigning functions to distinct regions of theNterminus of the prion protein that are involved in its copper-stimulated, clathrin-dependent endocytosis
    • Taylor, D. R., Watt, N. T., Perera, W. S., and Hooper, N. M. (2005) Assigning functions to distinct regions of theNterminus of the prion protein that are involved in its copper-stimulated, clathrin-dependent endocytosis. J. Cell Sci. 118, 5141-5153
    • (2005) J. Cell Sci. , vol.118 , pp. 5141-5153
    • Taylor, D.R.1    Watt, N.T.2    Perera, W.S.3    Hooper, N.M.4
  • 41
    • 84861914969 scopus 로고    scopus 로고
    • Neurotoxicity and memory deficits induced by soluble low-molecular-weight amyloid-β1-42 oligomers are revealed in vivo by using a novel animal model
    • Brouillette, J., Caillierez, R., Zommer, N., Alves-Pires, C., Benilova, I., Blum, D., De Strooper, B., and Buée, L. (2012) Neurotoxicity and memory deficits induced by soluble low-molecular-weight amyloid-β1-42 oligomers are revealed in vivo by using a novel animal model. J. Neurosci. 32, 7852-7861
    • (2012) J. Neurosci. , vol.32 , pp. 7852-7861
    • Brouillette, J.1    Caillierez, R.2    Zommer, N.3    Alves-Pires, C.4    Benilova, I.5    Blum, D.6    De Strooper, B.7    Buée, L.8
  • 43
    • 0036882127 scopus 로고    scopus 로고
    • Overexpression of PrPc triggers caspase 3 activation: Potentiation by proteasome inhibitors and blockade by anti-PrP antibodies
    • Paitel, E., Alves da Costa, C., Vilette, D., Grassi, J., and Checler, F. (2002) Overexpression of PrPc triggers caspase 3 activation: potentiation by proteasome inhibitors and blockade by anti-PrP antibodies. J. Neurochem. 83, 1208-1214
    • (2002) J. Neurochem. , vol.83 , pp. 1208-1214
    • Paitel, E.1    Alves Da Costa, C.2    Vilette, D.3    Grassi, J.4    Checler, F.5
  • 47
    • 43249114144 scopus 로고    scopus 로고
    • Membrane-bound β-amyloid oligomers are recruited into lipid rafts by a Fyn-dependent mechanism
    • Williamson, R., Usardi, A., Hanger, D. P., and Anderton, B. H. (2008) Membrane-bound β-amyloid oligomers are recruited into lipid rafts by a Fyn-dependent mechanism. FASEB J. 22, 1552-1559
    • (2008) FASEB J. , vol.22 , pp. 1552-1559
    • Williamson, R.1    Usardi, A.2    Hanger, D.P.3    Anderton, B.H.4
  • 48
    • 33846953615 scopus 로고    scopus 로고
    • The low-density lipoprotein receptor- related protein 1 (LRP1) mediates the endocytosis of the cellular prion protein
    • Taylor, D. R., and Hooper, N. M. (2007) The low-density lipoprotein receptor- related protein 1 (LRP1) mediates the endocytosis of the cellular prion protein. Biochem. J. 402, 17-23
    • (2007) Biochem. J. , vol.402 , pp. 17-23
    • Taylor, D.R.1    Hooper, N.M.2
  • 50
    • 70450273117 scopus 로고    scopus 로고
    • Receptor-associated protein interacts with amyloid-β peptide and promotes its cellular uptake
    • Kanekiyo, T., and Bu, G. (2009) Receptor-associated protein interacts with amyloid-β peptide and promotes its cellular uptake. J. Biol. Chem. 284, 33352-33359
    • (2009) J. Biol. Chem. , vol.284 , pp. 33352-33359
    • Kanekiyo, T.1    Bu, G.2
  • 53
    • 0035970784 scopus 로고    scopus 로고
    • Differential expression of cellular prion protein in mouse brain as detected with multiple anti-PrP monoclonal antibodies
    • Liu, T., Zwingman, T., Li, R., Pan, T., Wong, B. S., Petersen, R. B., Gambetti, P., Herrup, K., and Sy, M. S. (2001) Differential expression of cellular prion protein in mouse brain as detected with multiple anti-PrP monoclonal antibodies. Brain Res. 896, 118-129
    • (2001) Brain Res. , vol.896 , pp. 118-129
    • Liu, T.1    Zwingman, T.2    Li, R.3    Pan, T.4    Wong, B.S.5    Petersen, R.B.6    Gambetti, P.7    Herrup, K.8    Sy, M.S.9
  • 54
    • 77955328980 scopus 로고    scopus 로고
    • Fynβ-amyloid: A toxic triad
    • Haass, C., and Mandelkow, E. (2010) Fynβ-amyloid: a toxic triad. Cell 142, 356-358
    • (2010) Cell , vol.142 , pp. 356-358
    • Haass, C.1    Mandelkow, E.2
  • 56
    • 79952141276 scopus 로고    scopus 로고
    • The role of lipid rafts in prion protein biology
    • Lewis, V., and Hooper, N. M. (2011) The role of lipid rafts in prion protein biology. Front. Biosci. 16, 151-168
    • (2011) Front. Biosci. , vol.16 , pp. 151-168
    • Lewis, V.1    Hooper, N.M.2
  • 58
    • 50949097728 scopus 로고    scopus 로고
    • Oligomer-specific Aβ toxicity in cell models is mediated by selective uptake
    • Chafekar, S. M., Baas, F., and Scheper, W. (2008) Oligomer-specific Aβ toxicity in cell models is mediated by selective uptake. Biochim. Biophys. Acta 1782, 523-531
    • (2008) Biochim. Biophys. Acta , vol.1782 , pp. 523-531
    • Chafekar, S.M.1    Baas, F.2    Scheper, W.3
  • 60
    • 0036607597 scopus 로고    scopus 로고
    • The low-density lipoprotein receptor gene family: A cellular Swiss army knife?
    • Nykjaer, A., and Willnow, T. E. (2002) The low-density lipoprotein receptor gene family: a cellular Swiss army knife? Trends Cell Biol. 12, 273-280
    • (2002) Trends Cell Biol. , vol.12 , pp. 273-280
    • Nykjaer, A.1    Willnow, T.E.2
  • 61
    • 79551565625 scopus 로고    scopus 로고
    • Heparan sulphate proteoglycan and the low-density lipoprotein receptorrelated protein 1 constitute major pathways for neuronal amyloid-β uptake
    • Kanekiyo, T., Zhang, J., Liu, Q., Liu, C.-C., Zhang, L., and Bu, G. (2011) Heparan sulphate proteoglycan and the low-density lipoprotein receptorrelated protein 1 constitute major pathways for neuronal amyloid-β uptake. J. Neurosci. 31, 1644-1651
    • (2011) J. Neurosci. , vol.31 , pp. 1644-1651
    • Kanekiyo, T.1    Zhang, J.2    Liu, Q.3    Liu, C.-C.4    Zhang, L.5    Bu, G.6
  • 62
    • 77955604553 scopus 로고    scopus 로고
    • Low-density lipoprotein receptor-related protein 1 (LRP1) mediates neuronal Aβ42 uptake and lysosomal trafficking
    • Fuentealba, R. A., Liu, Q., Zhang, J., Kanekiyo, T., Hu, X., Lee, J. M., LaDu, M. J., and Bu, G. (2010) Low-density lipoprotein receptor-related protein 1 (LRP1) mediates neuronal Aβ42 uptake and lysosomal trafficking. PLoS One 5, e11884
    • (2010) PLoS One , vol.5
    • Fuentealba, R.A.1    Liu, Q.2    Zhang, J.3    Kanekiyo, T.4    Hu, X.5    Lee, J.M.6    Ladu, M.J.7    Bu, G.8
  • 63
    • 28044434891 scopus 로고    scopus 로고
    • The low-density lipoprotein receptorrelated protein-1 associates transiently with lipid rafts
    • Wu, L., and Gonias, S. L. (2005) The low-density lipoprotein receptorrelated protein-1 associates transiently with lipid rafts. J. Cell. Biochem. 96, 1021-1033
    • (2005) J. Cell. Biochem. , vol.96 , pp. 1021-1033
    • Wu, L.1    Gonias, S.L.2
  • 64
    • 61349138103 scopus 로고    scopus 로고
    • Alzheimer's disease: A prion protein connection
    • Cisse, M., and Mucke, L. (2009) Alzheimer's disease: A prion protein connection. Nature 457, 1090-1091
    • (2009) Nature , vol.457 , pp. 1090-1091
    • Cisse, M.1    Mucke, L.2
  • 66
    • 77953658771 scopus 로고    scopus 로고
    • Deleterious effects of amyloid β oligomers acting as an extracellular scaffold for mGluR5
    • Renner, M., Lacor, P. N., Velasco, P. T., Xu, J., Contractor, A., Klein, W. L., and Triller, A. (2010) Deleterious effects of amyloid β oligomers acting as an extracellular scaffold for mGluR5. Neuron 66, 739-754
    • (2010) Neuron , vol.66 , pp. 739-754
    • Renner, M.1    Lacor, P.N.2    Velasco, P.T.3    Xu, J.4    Contractor, A.5    Klein, W.L.6    Triller, A.7
  • 68
    • 0037316675 scopus 로고    scopus 로고
    • Tethering theNterminus of the prion protein compromises the cellular response to oxidative stress
    • Zeng, F., Watt, N. T., Walmsley, A. R., and Hooper, N. M. (2003) Tethering theNterminus of the prion protein compromises the cellular response to oxidative stress. J. Neurochem. 84, 480-490
    • (2003) J. Neurochem. , vol.84 , pp. 480-490
    • Zeng, F.1    Watt, N.T.2    Walmsley, A.R.3    Hooper, N.M.4
  • 70
    • 79951761390 scopus 로고    scopus 로고
    • The culprit behind amyloid β peptide related neurotoxicity in Alzheimer's disease: Oligomer size or conformation?
    • Broersen, K., Rousseau, F., and Schymkowitz, J. (2010) The culprit behind amyloid β peptide related neurotoxicity in Alzheimer's disease: oligomer size or conformation? Alzheimers Res. Ther. 2, 12-26
    • (2010) Alzheimers Res. Ther. , vol.2 , pp. 12-26
    • Broersen, K.1    Rousseau, F.2    Schymkowitz, J.3
  • 72
    • 12844257374 scopus 로고    scopus 로고
    • Cellular prion protein neuroprotective function: Implications in prion diseases
    • Roucou, X., and LeBlanc, A. C. (2005) Cellular prion protein neuroprotective function: implications in prion diseases. J. Mol. Med. 83, 3-11
    • (2005) J. Mol. Med. , vol.83 , pp. 3-11
    • Roucou, X.1    Leblanc, A.C.2


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