메뉴 건너뛰기




Volumn 288, Issue 11, 2013, Pages 7857-7866

An N-terminal fragment of the prion protein binds to amyloid-β oligomers and inhibits their neurotoxicity in vivo

Author keywords

[No Author keywords available]

Indexed keywords

ALZHEIMER DISEASE; CELLULAR PRION PROTEINS; COGNITIVE DEFICITS; HIPPOCAMPAL NEURONS; NEUROTOXIC EFFECTS; POSITIVELY CHARGED; POTENT INHIBITOR; THERAPEUTIC AGENTS;

EID: 84875174182     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.423954     Document Type: Article
Times cited : (161)

References (34)
  • 1
    • 84858225391 scopus 로고    scopus 로고
    • 2012 Alzheimer's disease facts and figures
    • Alzheimer's Association
    • Alzheimer's Association (2012) 2012 Alzheimer's disease facts and figures. Alzheimers Dement. 8, 131-168
    • (2012) Alzheimers Dement , vol.8 , pp. 131-168
  • 3
    • 44549087765 scopus 로고    scopus 로고
    • Soluble oligomers of the amyloid β-protein impair synaptic plasticity and behavior
    • Selkoe, D. J. (2008) Soluble oligomers of the amyloid β-protein impair synaptic plasticity and behavior. Behav. Brain Res. 192, 106-113
    • (2008) Behav. Brain Res. , vol.192 , pp. 106-113
    • Selkoe, D.J.1
  • 4
    • 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
  • 5
    • 77956197815 scopus 로고    scopus 로고
    • Interaction between human prion protein and amyloid-β (Aβ) oligomers: Role of N-terminal residues
    • Chen, S., Yadav, S. P., and Surewicz, W. K. (2010) Interaction between human prion protein and amyloid-β (Aβ) oligomers: role of N-terminal residues. 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
  • 12
    • 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
  • 13
    • 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
  • 15
    • 77955617917 scopus 로고    scopus 로고
    • The prion protein as a receptor for amyloid-β
    • discussion E4-E5
    • Kessels, H. W., Nguyen, L. N., Nabavi, S., and Malinow, R. (2010) The prion protein as a receptor for amyloid-β. Nature 466, E3-E4; discussion E4-E5
    • (2010) Nature , vol.466
    • Kessels, H.W.1    Nguyen, L.N.2    Nabavi, S.3    Malinow, R.4
  • 16
    • 79960660843 scopus 로고    scopus 로고
    • Ablation of cellular prion protein does not ameliorate abnormal neural network activity or cognitive dysfunction in the J20 line of human amyloid precursor protein transgenic mice
    • Cissé, M., Sanchez, P. E., Kim, D. H., Ho, K., Yu, G. Q., and Mucke, L. (2011) Ablation of cellular prion protein does not ameliorate abnormal neural network activity or cognitive dysfunction in the J20 line of human amyloid precursor protein transgenic mice. J. Neurosci. 31, 10427-10431
    • (2011) J. Neurosci. , vol.31 , pp. 10427-10431
    • Cissé, M.1    Sanchez, P.E.2    Kim, D.H.3    Ho, K.4    Yu, G.Q.5    Mucke, L.6
  • 17
    • 0035851151 scopus 로고    scopus 로고
    • The disintegrins ADAM10 and TACE contribute to the constitutive and phorbol esterregulated normal cleavage of the cellular prion protein
    • Vincent, B., Paitel, E., Saftig, P., Frobert, Y., Hartmann, D., De Strooper, B., Grassi, J., Lopez-Perez, E., and Checler, F. (2001) The disintegrins ADAM10 and TACE contribute to the constitutive and phorbol esterregulated normal cleavage of the cellular prion protein. J. Biol. Chem. 276, 37743-37746
    • (2001) J. Biol. Chem. , vol.276 , pp. 37743-37746
    • Vincent, B.1    Paitel, E.2    Saftig, P.3    Frobert, Y.4    Hartmann, D.5    De Strooper, B.6    Grassi, J.7    Lopez-Perez, E.8    Checler, F.9
  • 19
    • 0027405573 scopus 로고
    • Processing of a cellular prion protein: Identification of Nand C-terminal cleavage sites
    • Harris, D. A., Huber, M. T., van Dijken, P., Shyng, S. L., Chait, B. T., and Wang, R. (1993) Processing of a cellular prion protein: identification of Nand C-terminal cleavage sites. Biochemistry 32, 1009-1016
    • (1993) Biochemistry , vol.32 , pp. 1009-1016
    • Harris, D.A.1    Huber, M.T.2    Van Dijken, P.3    Shyng, S.L.4    Chait, B.T.5    Wang, R.6
  • 20
    • 84866930442 scopus 로고    scopus 로고
    • Soluble prion protein inhibits amyloid-β (Aβ) fibrillization and toxicity
    • Nieznanski, K., Choi, J. K., Chen, S., Surewicz, K., and Surewicz, W. K. (2012) Soluble prion protein inhibits amyloid-β (Aβ) fibrillization and toxicity. J. Biol. Chem. 287, 33104-33108
    • (2012) J. Biol. Chem. , vol.287 , pp. 33104-33108
    • Nieznanski, K.1    Choi, J.K.2    Chen, S.3    Surewicz, K.4    Surewicz, W.K.5
  • 21
    • 0030810150 scopus 로고    scopus 로고
    • Human prion proteins expressed in Escherichia coli and purified by high-affinity column refolding
    • Zahn, R., von Schroetter, C., and Wüthrich, K. (1997) Human prion proteins expressed in Escherichia coli and purified by high-affinity column refolding. FEBS Lett. 417, 400-404
    • (1997) FEBS Lett , vol.417 , pp. 400-404
    • Zahn, R.1    Von Schroetter, C.2    Wüthrich, K.3
  • 23
    • 0035282948 scopus 로고    scopus 로고
    • Hippocampal synaptic plasticity involves competition between Ca2/calmodulin-dependent protein kinase II and postsynaptic density 95 for binding to the NR2A subunit of theNMDAreceptor
    • Gardoni, F., Schrama, L. H., Kamal, A., Gispen, W. H., Cattabeni, F., and Di Luca, M. (2001) Hippocampal synaptic plasticity involves competition between Ca2/calmodulin-dependent protein kinase II and postsynaptic density 95 for binding to the NR2A subunit of theNMDAreceptor. J. Neurosci. 21, 1501-1509
    • (2001) J. Neurosci. , vol.21 , pp. 1501-1509
    • Gardoni, F.1    Schrama, L.H.2    Kamal, A.3    Gispen, W.H.4    Cattabeni, F.5    Di Luca, M.6
  • 24
    • 78650626543 scopus 로고    scopus 로고
    • Use of surface plasmon resonance to study the elongation kinetics and the binding properties of the highly amyloidogenic Aβ(1-42) peptide, synthesized by depsi-peptide technique
    • Stravalaci, M., Beeg, M., Salmona, M., and Gobbi, M. (2011) Use of surface plasmon resonance to study the elongation kinetics and the binding properties of the highly amyloidogenic Aβ(1-42) peptide, synthesized by depsi-peptide technique. Biosens. Bioelectron. 26, 2772-2775
    • (2011) Biosens. Bioelectron. , vol.26 , pp. 2772-2775
    • Stravalaci, M.1    Beeg, M.2    Salmona, M.3    Gobbi, M.4
  • 26
    • 0014086078 scopus 로고
    • Thioflavin T for amyloid detection
    • Saeed, S. M., and Fine, G. (1967) Thioflavin T for amyloid detection. Am. J. Clin. Pathol. 47, 588-593
    • (1967) Am. J. Clin. Pathol. , vol.47 , pp. 588-593
    • Saeed, S.M.1    Fine, G.2
  • 27
    • 79955972936 scopus 로고    scopus 로고
    • Insight into amyloid structure using chemical probes
    • Reinke, A. A., and Gestwicki, J. E. (2011) Insight into amyloid structure using chemical probes. Chem. Biol. Drug Des. 77, 399-411
    • (2011) Chem. Biol. Drug Des. , vol.77 , pp. 399-411
    • Reinke, A.A.1    Gestwicki, J.E.2
  • 29
    • 72149127389 scopus 로고    scopus 로고
    • The α-secretase-derived N-terminal product of cellular prion, N1, displays neuroprotective function in vitro and in vivo
    • Guillot-Sestier, M. V., Sunyach, C., Druon, C., Scarzello, S., and Checler, F. (2009) The α-secretase-derived N-terminal product of cellular prion, N1, displays neuroprotective function in vitro and in vivo. J. Biol. Chem. 284, 35973-35986
    • (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
  • 30
    • 84856845217 scopus 로고    scopus 로고
    • α-Secretase-derived fragment of cellular prion, N1, protects against monomeric and oligomeric amyloid-β (Aβ)-associated cell death
    • Guillot-Sestier, M. V., Sunyach, C., Ferreira, S. T., Marzolo, M. P., Bauer, C., Thevenet, A., and Checler, F. (2012) α-Secretase-derived fragment of cellular prion, N1, protects against monomeric and oligomeric amyloid-β (Aβ)-associated cell death. J. Biol. Chem. 287, 5021-5032
    • (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    Checler, F.7
  • 31
    • 80052501210 scopus 로고    scopus 로고
    • Resolving controversies on the path to Alzheimer's therapeutics
    • Selkoe, D. J. (2011) Resolving controversies on the path to Alzheimer's therapeutics. Nat. Med. 17, 1060-1065
    • (2011) Nat. Med. , vol.17 , pp. 1060-1065
    • Selkoe, D.J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.