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Volumn 109, Issue 5, 2012, Pages 1737-1742

Aβ neurotoxicity depends on interactions between copper ions, prion protein,and N-methyl-D-aspartate receptors

Author keywords

5XFAD mouse; A oligomer; Alzheimer's disease; Cu; NMDA receptor

Indexed keywords

AMYLOID BETA PROTEIN[1-42]; COPPER ION; GLYCINE; N METHYL DEXTRO ASPARTIC ACID; N METHYL DEXTRO ASPARTIC ACID RECEPTOR; PRION PROTEIN;

EID: 84863116075     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1110789109     Document Type: Article
Times cited : (210)

References (56)
  • 1
    • 36649008903 scopus 로고    scopus 로고
    • Hippocampal long-term synaptic plasticity and signal amplification of NMDA receptors
    • MacDonald JF, Jackson MF, Beazely MA (2006) Hippocampal long-term synaptic plasticity and signal amplification of NMDA receptors. Crit Rev Neurobiol 18(1-2):71-84. (Pubitemid 350194079)
    • (2006) Critical Reviews in Neurobiology , vol.18 , Issue.1-2 , pp. 71-84
    • MacDonald, J.F.1    Jackson, M.F.2    Beazely, M.A.3
  • 2
    • 54049087697 scopus 로고    scopus 로고
    • Regulation of NMDA receptor subunit expression and its implications for LTD, LTP, and metaplasticity
    • Yashiro K, Philpot BD (2008) Regulation of NMDA receptor subunit expression and its implications for LTD, LTP, and metaplasticity. Neuropharmacology 55:1081-1094.
    • (2008) Neuropharmacology , vol.55 , pp. 1081-1094
    • Yashiro, K.1    Philpot, B.D.2
  • 3
    • 0024521588 scopus 로고
    • Regulation of NMDA receptor desensitization in mouse hippocampal neurons by glycine
    • DOI 10.1038/338425a0
    • Mayer ML, Vyklicky LJ, Jr., Clements J (1989) Regulation of NMDA receptor desensitization in mouse hippocampal neurons by glycine. Nature 338:425-427. (Pubitemid 19089323)
    • (1989) Nature , vol.338 , Issue.6214 , pp. 425-427
    • Mayer, M.L.1    Vyklicky Jr., L.2    Clements, J.3
  • 4
    • 0025247748 scopus 로고
    • Glycine decreases desensitization of N-methyl-D-aspartate (NMDA) receptors expressed in Xenopus oocytes and is required for NMDA responses
    • Lerma J, Zukin RS, Bennett MV (1990) Glycine decreases desensitization of N-methyl-D-aspartate (NMDA) receptors expressed in Xenopus oocytes and is required for NMDA responses. Proc Natl Acad Sci USA 87:2354-2358.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 2354-2358
    • Lerma, J.1    Zukin, R.S.2    Bennett, M.V.3
  • 5
    • 46849097142 scopus 로고    scopus 로고
    • NMDA receptors in clinical neurology: excitatory times ahead
    • DOI 10.1016/S1474-4422(08)70165-0, PII S1474442208701650
    • Kalia LV, Kalia SK, Salter MW (2008) NMDA receptors in clinical neurology: Excitatory times ahead. Lancet Neurol 7:742-755. (Pubitemid 351957932)
    • (2008) The Lancet Neurology , vol.7 , Issue.8 , pp. 742-755
    • Kalia, L.V.1    Kalia, S.K.2    Salter, M.W.3
  • 6
    • 0028762647 scopus 로고
    • Excitatory amino acids as a final common pathway for neurologic disorders
    • Lipton SA, Rosenberg PA (1994) Excitatory amino acids as a final common pathway for neurologic disorders. N Engl J Med 330:613-622.
    • (1994) N Engl J Med , vol.330 , pp. 613-622
    • Lipton, S.A.1    Rosenberg, P.A.2
  • 7
    • 77954132249 scopus 로고    scopus 로고
    • Amyloid-β-induced neuronal dysfunction in Alzheimer's disease: From synapses toward neural networks
    • Palop JJ, Mucke L (2010) Amyloid-β-induced neuronal dysfunction in Alzheimer's disease: From synapses toward neural networks. Nat Neurosci 13:812-818.
    • (2010) Nat Neurosci , vol.13 , pp. 812-818
    • Palop, J.J.1    Mucke, L.2
  • 8
    • 64049098761 scopus 로고    scopus 로고
    • Neuropathology and cognitive impairment in Alzheimer disease: A complex but coherent relationship
    • Nelson PT, Braak H, Markesbery WR (2009) Neuropathology and cognitive impairment in Alzheimer disease: A complex but coherent relationship. J Neuropathol Exp Neurol 68(1):1-14.
    • (2009) J Neuropathol Exp Neurol , vol.68 , Issue.1 , pp. 1-14
    • Nelson, P.T.1    Braak, H.2    Markesbery, W.R.3
  • 10
    • 34248190279 scopus 로고    scopus 로고
    • A β oligomers: A decade of discovery
    • Walsh DM, Selkoe DJ (2007) A β 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
  • 11
    • 77649202326 scopus 로고    scopus 로고
    • Protein aggregation diseases: Pathogenicity and therapeutic perspectives
    • Aguzzi A, O'Connor T (2010) Protein aggregation diseases: Pathogenicity and therapeutic perspectives. Nat Rev Drug Discov 9:237-248.
    • (2010) Nat Rev Drug Discov , vol.9 , pp. 237-248
    • Aguzzi, A.1    O'Connor, T.2
  • 12
    • 61349201380 scopus 로고    scopus 로고
    • Cellular prion protein mediates impairment of synaptic plasticity by amyloid-β oligomers
    • Laurén J, Gimbel DA, Nygaard HB, Gilbert JW, Strittmatter SM (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
    • 79956302348 scopus 로고    scopus 로고
    • Alzheimer's disease brain-derived amyloid-β-mediated inhibition of LTP in vivo is prevented by immunotargeting cellular prion protein
    • Barry AE, et al. (2011) Alzheimer's disease brain-derived 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
  • 14
    • 77951876319 scopus 로고    scopus 로고
    • Memory impairment in transgenic Alzheimer mice requires cellular prion protein
    • Gimbel DA, et al. (2010) Memory impairment in transgenic Alzheimer mice requires cellular prion protein. J Neurosci 30:6367-6374.
    • (2010) J Neurosci , vol.30 , pp. 6367-6374
    • Gimbel, D.A.1
  • 15
    • 79958249995 scopus 로고    scopus 로고
    • Interaction between prion protein and toxic amyloid β assemblies can be therapeutically targeted at multiple sites
    • Freir DB, et al. (2011) Interaction between prion protein and toxic amyloid β assemblies can be therapeutically targeted at multiple sites. Nat Commun 2:336.
    • (2011) Nat Commun , vol.2 , pp. 336
    • Freir, D.B.1
  • 16
    • 0030841116 scopus 로고    scopus 로고
    • Uncompetitive NMDA receptor antagoists attenuate NMDA-induced impairment of passive avoidance learning and LTP
    • DOI 10.1016/S0028-3908(97)00070-1, PII S0028390897000701
    • Zajaczkowski W, Frankiewicz T, Parsons CG, Danysz W (1997) Uncompetitive NMDA receptor antagonists attenuate NMDA-induced impairment of passive avoidance learning and LTP. Neuropharmacology 36:961-971. (Pubitemid 27300126)
    • (1997) Neuropharmacology , vol.36 , Issue.7 , pp. 961-971
    • Zajaczkowski, W.1    Frankiewicz, T.2    Parsons, C.G.3    Danysz, W.4
  • 17
    • 43149109488 scopus 로고    scopus 로고
    • Prion protein attenuates excitotoxicity by inhibiting NMDA receptors
    • Khosravani H, et al. (2008) Prion protein attenuates excitotoxicity by inhibiting NMDA receptors. J Cell Biol 181:551-565.
    • (2008) J Cell Biol , vol.181 , pp. 551-565
    • Khosravani, H.1
  • 19
    • 0037174618 scopus 로고    scopus 로고
    • Alzheimer's disease is a synaptic failure
    • Selkoe DJ (2002) Alzheimer's disease is a synaptic failure. Science 298:789-791.
    • (2002) Science , vol.298 , pp. 789-791
    • Selkoe, D.J.1
  • 20
    • 0037010123 scopus 로고    scopus 로고
    • Why glycine transporters have different stoichiometries
    • DOI 10.1016/S0014-5793(02)03251-9, PII S0014579302032519
    • Supplisson S, Roux MJ (2002) Why glycine transporters have different stoichiometries. FEBS Lett 529(1):93-101. (Pubitemid 35283917)
    • (2002) FEBS Letters , vol.529 , Issue.1 , pp. 93-101
    • Supplisson, S.1    Roux, M.J.2
  • 21
    • 56049092225 scopus 로고    scopus 로고
    • Allosteric modulation of NMDA receptor via elevation of brain glycine and D-serine: The therapeutic potentials for schizophrenia
    • Yang CR, Svensson KA (2008) Allosteric modulation of NMDA receptor via elevation of brain glycine and D-serine: The therapeutic potentials for schizophrenia. Pharmacol Ther 120:317-332.
    • (2008) Pharmacol Ther , vol.120 , pp. 317-332
    • Yang, C.R.1    Svensson, K.A.2
  • 22
    • 67449084098 scopus 로고    scopus 로고
    • β-Amyloid impairs AMPA receptor trafficking and function by reducing Ca2+/calmodulin-dependent protein kinase II synaptic distribution
    • Gu Z, Liu W, Yan Z (2009) β-Amyloid impairs AMPA receptor trafficking and function by reducing Ca2+/calmodulin-dependent protein kinase II synaptic distribution. J Biol Chem 284:10639-10649.
    • (2009) J Biol Chem , vol.284 , pp. 10639-10649
    • Gu, Z.1    Liu, W.2    Yan, Z.3
  • 23
    • 84863118777 scopus 로고
    • Optical resolution of aspartic acid by using copper complexes of optically active amino acids
    • Harada K, Fujii N (1983) Optical resolution of aspartic acid by using copper complexes of optically active amino acids. Bull Chem Soc Jpn 56:653-654.
    • (1983) Bull Chem Soc Jpn , vol.56 , pp. 653-654
    • Harada, K.1    Fujii, N.2
  • 24
    • 0015218695 scopus 로고
    • Ternary coordination complexes between glycine, copper (II), and glycine peptides in aqueous solution
    • Martin RP, Mosoni L, Sarkar B (1971) Ternary coordination complexes between glycine, copper (II), and glycine peptides in aqueous solution. J Biol Chem 246:5944-5951.
    • (1971) J Biol Chem , vol.246 , pp. 5944-5951
    • Martin, R.P.1    Mosoni, L.2    Sarkar, B.3
  • 25
    • 0029964789 scopus 로고    scopus 로고
    • Copper modulation of NMDA responses in mouse and rat cultured hippocampal neurons
    • Vlachová V, Zemková H, Vyklický LJ, Jr. (1996) Copper modulation of NMDA responses in mouse and rat cultured hippocampal neurons. Eur J Neurosci 8:2257-2264.
    • (1996) Eur J Neurosci , vol.8 , pp. 2257-2264
    • Vlachová, V.1    Zemková, H.2    Vyklický Jr., L.J.3
  • 26
    • 0033844944 scopus 로고    scopus 로고
    • Characterization of copper interactions with Alzheimer amyloid beta peptides: Identification of an attomolar-affinity copper binding site on amyloid beta1-42
    • DOI 10.1046/j.1471-4159.2000.0751219.x
    • Atwood CS, et al. (2000) Characterization of copper interactions with Alzheimer amyloid beta peptides: Identification of an attomolar-affinity copper binding site on amyloid beta1-42. J Neurochem 75:1219-1233. (Pubitemid 30660512)
    • (2000) Journal of Neurochemistry , vol.75 , Issue.3 , pp. 1219-1233
    • Atwood, C.S.1    Scarpa, R.C.2    Huang, X.3    Moir, R.D.4    Jones, W.D.5    Fairlie, D.P.6    Tanzi, R.E.7    Bush, A.I.8
  • 27
    • 72049102879 scopus 로고    scopus 로고
    • Copper in the brain and Alzheimer's disease
    • Hung YH, Bush AI, Cherny RA (2010) Copper in the brain and Alzheimer's disease. J Biol Inorg Chem 15(1):61-76.
    • (2010) J Biol Inorg Chem , vol.15 , Issue.1 , pp. 61-76
    • Hung, Y.H.1    Bush, A.I.2    Cherny, R.A.3
  • 28
    • 0020582608 scopus 로고
    • Bathocuproine sulphonate: A tissue culture-compatible indicator of copper-mediated toxicity
    • Mohindru A, Fisher JM, Rabinovitz M (1983) Bathocuproine sulphonate: A tissue culture-compatible indicator of copper-mediated toxicity. Nature 303(5912):64-65. (Pubitemid 13125073)
    • (1983) Nature , vol.303 , Issue.5912 , pp. 64-65
    • Mohindru, A.1    Fisher, J.M.2    Rabinovitz, M.3
  • 29
    • 0023253615 scopus 로고
    • Zinc selectively blocks the action of N-methyl-D-aspartate on cortical neurons
    • Peters S, Koh J, Choi DW (1987) Zinc selectively blocks the action of N-methyl-Daspartate on cortical neurons. Science 236:589-593. (Pubitemid 17069929)
    • (1987) Science , vol.236 , Issue.4801 , pp. 589-593
    • Peters, S.1    Koh, J.2    Choi, D.W.3
  • 30
    • 0030997418 scopus 로고    scopus 로고
    • Differential sensitivity of recombinant N-methyl-D-aspartate receptor subtypes to zinc inhibition
    • Chen N, Moshaver A, Raymond LA (1997) Differential sensitivity of recombinant Nmethyl- D-aspartate receptor subtypes to zinc inhibition. Mol Pharmacol 51:1015-1023. (Pubitemid 27249135)
    • (1997) Molecular Pharmacology , vol.51 , Issue.6 , pp. 1015-1023
    • Chen, N.1    Moshaver, A.2    Raymond, L.A.3
  • 31
    • 33646856612 scopus 로고    scopus 로고
    • Copper homeostasis in the CNS: A novel link between the NMDA receptor and copper homeostasis in the hippocampus
    • DOI 10.1385/MN:33:2:81
    • Schlief ML, Gitlin JD (2006) Copper homeostasis in the CNS: A novel link between the NMDA receptor and copper homeostasis in the hippocampus. Mol Neurobiol 33(2):81-90. (Pubitemid 43780368)
    • (2006) Molecular Neurobiology , vol.33 , Issue.2 , pp. 81-90
    • Schlief, M.L.1    Gitlin, J.D.2
  • 33
    • 0035254585 scopus 로고    scopus 로고
    • Prion and prejudice: Normal protein and the synapse
    • Brown DR (2001) Prion and prejudice: Normal protein and the synapse. Trends Neurosci 24(2):85-90.
    • (2001) Trends Neurosci , vol.24 , Issue.2 , pp. 85-90
    • Brown, D.R.1
  • 35
    • 0027997387 scopus 로고
    • Prion protein is necessary for normal synaptic function
    • Collinge J, et al. (1994) Prion protein is necessary for normal synaptic function. Nature 370:295-297.
    • (1994) Nature , vol.370 , pp. 295-297
    • Collinge, J.1
  • 38
    • 66149161888 scopus 로고    scopus 로고
    • Copper(II) binding to amyloid-β fibrils of Alzheimer's disease reveals a picomolar affinity: Stoichiometry and coordination geometry are independent of Abeta oligomeric form
    • Sarell CJ, Syme CD, Rigby SE, Viles JH (2009) Copper(II) binding to amyloid-β fibrils of Alzheimer's disease reveals a picomolar affinity: Stoichiometry and coordination geometry are independent of Abeta oligomeric form. Biochemistry 48:4388-4402.
    • (2009) Biochemistry , vol.48 , pp. 4388-4402
    • Sarell, C.J.1    Syme, C.D.2    Rigby, S.E.3    Viles, J.H.4
  • 40
    • 0038176528 scopus 로고    scopus 로고
    • In vitro characterization of conditions for amyloid-beta peptide oligomerization and fibrillogenesis
    • DOI 10.1074/jbc.M210207200
    • Stine WBJ, Jr., Dahlgren KN, Krafft GA, LaDu MJ (2003) In vitro characterization of conditions for amyloid-β peptide oligomerization and fibrillogenesis. J Biol Chem 278:11612-11622. (Pubitemid 36792723)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.13 , pp. 11612-11622
    • Stine Jr., W.B.1    Dahlgren, K.N.2    Krafft, G.A.3    LaDu, M.J.4
  • 42
    • 79251552792 scopus 로고    scopus 로고
    • Metabotropic glutamate receptors transduce signals for neurite outgrowth after binding of the prion protein to laminin γ1 chain
    • Beraldo FH, et al. (2011) Metabotropic glutamate receptors transduce signals for neurite outgrowth after binding of the prion protein to laminin γ1 chain. FASEB J 25:265-279.
    • (2011) FASEB J , vol.25 , pp. 265-279
    • Beraldo, F.H.1
  • 43
    • 77954687479 scopus 로고    scopus 로고
    • Cellular copper distribution: A mechanistic systems biology approach
    • Banci L, Bertini I, Cantini F, Ciofi-Baffoni S (2010) Cellular copper distribution: A mechanistic systems biology approach. Cell Mol Life Sci 67:2563-2589.
    • (2010) Cell Mol Life Sci , vol.67 , pp. 2563-2589
    • Banci, L.1    Bertini, I.2    Cantini, F.3    Ciofi-Baffoni, S.4
  • 44
    • 0031464954 scopus 로고    scopus 로고
    • Suppression of long-term potentiation in hippocampal slices by copper
    • DOI 10.1002/(SICI)1098-1063(1997)7:6<666::AID-HIPO8>3.0.CO;2-C
    • Doreulee N, Yanovsky Y, Haas HL (1997) Suppression of long-term potentiation in hippocampal slices by copper. Hippocampus 7:666-669. (Pubitemid 28021651)
    • (1997) Hippocampus , vol.7 , Issue.6 , pp. 666-669
    • Doreulee, N.1    Yanovsky, Y.2    Haas, H.L.3
  • 45
    • 52249115856 scopus 로고    scopus 로고
    • Clusters of hyperactive neurons near amyloid plaques in a mouse model of Alzheimer's disease
    • Busche MA, et al. (2008) Clusters of hyperactive neurons near amyloid plaques in a mouse model of Alzheimer's disease. Science 321:1686-1689.
    • (2008) Science , vol.321 , pp. 1686-1689
    • Busche, M.A.1
  • 46
    • 79956110918 scopus 로고    scopus 로고
    • The cellular prion protein mediates neurotoxic signalling of β-sheet-rich conformers independent of prion replication
    • Resenberger UK, et al. (2011) The cellular prion protein mediates neurotoxic signalling of β-sheet-rich conformers independent of prion replication. EMBO J 30:2057-2070.
    • (2011) EMBO J , vol.30 , pp. 2057-2070
    • Resenberger, U.K.1
  • 47
    • 76649093635 scopus 로고    scopus 로고
    • Synthetic amyloid-β oligomers impair long-term memory independently of cellular prion protein
    • Balducci C, et al. (2010) Synthetic amyloid-β oligomers impair long-term memory independently of cellular prion protein. Proc Natl Acad Sci USA 107:2295-2300.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 2295-2300
    • Balducci, C.1
  • 48
    • 77956165325 scopus 로고    scopus 로고
    • Prion protein and Abeta-related synaptic toxicity impairment
    • Calella AM, et al. (2010) Prion protein and Abeta-related synaptic toxicity impairment. EMBO Mol Med 2:306-314.
    • (2010) EMBO Mol Med , vol.2 , pp. 306-314
    • Calella, A.M.1
  • 49
    • 77955617917 scopus 로고    scopus 로고
    • The prion protein as a receptor for amyloid-beta
    • discussion E4-E5
    • Kessels HW, Nguyen LN, Nabavi S, Malinow R (2010) The prion protein as a receptor for amyloid-beta. 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
  • 50
    • 33644957833 scopus 로고    scopus 로고
    • Temporal memory deficits in Alzheimer's mouse models: Rescue by genetic deletion of BACE1
    • Ohno M, et al. (2006) Temporal memory deficits in Alzheimer's mouse models: Rescue by genetic deletion of BACE1. Eur J Neurosci 23:251-260.
    • (2006) Eur J Neurosci , vol.23 , pp. 251-260
    • Ohno, M.1
  • 51
    • 77955841406 scopus 로고    scopus 로고
    • Candidate anti-A beta fluorene compounds selected from analogs of amyloid imaging agents
    • Hong HS, et al. (2010) Candidate anti-A beta fluorene compounds selected from analogs of amyloid imaging agents. Neurobiol Aging 31:1690-1699.
    • (2010) Neurobiol Aging , vol.31 , pp. 1690-1699
    • Hong, H.S.1
  • 52
    • 0000999342 scopus 로고
    • Spectrophotometric determination of serum copper with biscyclohexanoneoxalyldihydrazone
    • Peterson RE, Bollier ME (1955) Spectrophotometric determination of serum copper with biscyclohexanoneoxalyldihydrazone. Anal Chem 27:1195-1197.
    • (1955) Anal Chem , vol.27 , pp. 1195-1197
    • Peterson, R.E.1    Bollier, M.E.2
  • 53
    • 56549089911 scopus 로고    scopus 로고
    • The interaction of biological and noxious transition metals with the zinc probes FluoZin-3 and Newport Green
    • Zhao J, Bertoglio BA, Devinney MJJ, Jr., Dineley KE, Kay AR (2009) The interaction of biological and noxious transition metals with the zinc probes FluoZin-3 and Newport Green. Anal Biochem 384(1):34-41.
    • (2009) Anal Biochem , vol.384 , Issue.1 , pp. 34-41
    • Zhao, J.1    Bertoglio, B.A.2    Devinney Jr., M.J.J.3    Dineley, K.E.4    Kay, A.R.5
  • 54
    • 0242476277 scopus 로고
    • 4- reduction of a sterically constrained bis(substituted phenanthroline) complex of copper(II) in aqueous solution
    • 4- reduction of a sterically constrained bis(substituted phenanthroline) complex of copper(II) in aqueous solution. Inorg Chem 20:1466-1469.
    • (1981) Inorg Chem , vol.20 , pp. 1466-1469
    • Al-Shatti, N.1    Lappin, A.G.2    Sykes, A.G.3
  • 55
    • 0030474926 scopus 로고    scopus 로고
    • Alzheimer's precursor protein and the use of bathocuproine for determining reduction of copper(II)
    • Sayre LM (1996) Alzheimer's precursor protein and the use of bathocuproine for determining reduction of copper(II). Science 274:1933-1934.
    • (1996) Science , vol.274 , pp. 1933-1934
    • Sayre, L.M.1
  • 56
    • 79953211568 scopus 로고    scopus 로고
    • Unification of the copper(I) binding affinities of the metallochaperones Atx1, Atox1, and related proteins: Detection probes and affinity standards
    • Xiao Z, et al. (2011) Unification of the copper(I) binding affinities of the metallochaperones Atx1, Atox1, and related proteins: Detection probes and affinity standards. J Biol Chem 286:11047-11055.
    • (2011) J Biol Chem , vol.286 , pp. 11047-11055
    • Xiao, Z.1


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