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Volumn 466, Issue 1, 2015, Pages 66-71

The soluble extracellular fragment of neuroligin-1 targets Aβ oligomers to the postsynaptic region of excitatory synapses

Author keywords

A oligomer; Excitatory synapses; Hippocampal neurons; Neuroligin 1

Indexed keywords

AMYLOID BETA PROTEIN[1-40]; AMYLOID BETA PROTEIN[1-42]; N METHYL DEXTRO ASPARTIC ACID RECEPTOR 2B; NEUROLIGIN; NEUROLIGIN 1; AMYLOID BETA PROTEIN; N METHYL DEXTRO ASPARTIC ACID RECEPTOR; NERVE CELL ADHESION MOLECULE;

EID: 84941942564     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2015.08.107     Document Type: Article
Times cited : (24)

References (34)
  • 3
    • 27144511230 scopus 로고    scopus 로고
    • Games, β-Amyloid immunotherapy prevents synaptic degeneration in a mouse model of Alzheimer's disease
    • M. Buttini, E. Masliah, R. Barbour, and et al. Games, β-Amyloid immunotherapy prevents synaptic degeneration in a mouse model of Alzheimer's disease J. Neurosci. 25 2005 9096 9101
    • (2005) J. Neurosci. , vol.25 , pp. 9096-9101
    • Buttini, M.1    Masliah, E.2    Barbour, R.3
  • 5
    • 85027929889 scopus 로고    scopus 로고
    • Aβ Oligomer-induced synapse degeneration in Alzheimer's disease
    • K. Wilcox, P.N. Lacor, J. Pitt, and W.L. Klein Aβ Oligomer-induced synapse degeneration in Alzheimer's disease Cell Mol. Neurobiol. 31 2011 939 948
    • (2011) Cell Mol. Neurobiol. , vol.31 , pp. 939-948
    • Wilcox, K.1    Lacor, P.N.2    Pitt, J.3    Klein, W.L.4
  • 6
    • 33847662852 scopus 로고    scopus 로고
    • Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid β-peptide
    • C. Haass, and D.J. Selkoe Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid β-peptide Nat. Rev. Mol. Cell Biol. 8 2007 101 112
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 101-112
    • Haass, C.1    Selkoe, D.J.2
  • 7
    • 75549092259 scopus 로고    scopus 로고
    • Amyloid β from axons and dendrites reduces local spine number and plasticity
    • W. Wei, L.N. Nguyen, H.W. Kessels, and et al. Amyloid β from axons and dendrites reduces local spine number and plasticity Nat. Neurosci. 13 2010 190 196
    • (2010) Nat. Neurosci. , vol.13 , pp. 190-196
    • Wei, W.1    Nguyen, L.N.2    Kessels, H.W.3
  • 8
    • 84882670192 scopus 로고    scopus 로고
    • Postsynaptic receptors for amyloid-β oligomers as mediators of neuronal damage in Alzheimer's disease
    • M.C. Dinamarca, J. Rios, and N.C. Inestrosa Postsynaptic receptors for amyloid-β oligomers as mediators of neuronal damage in Alzheimer's disease Front. Physiol. 3 2012 1 7
    • (2012) Front. Physiol. , vol.3 , pp. 1-7
    • Dinamarca, M.C.1    Rios, J.2    Inestrosa, N.C.3
  • 9
    • 23044445669 scopus 로고    scopus 로고
    • Regulation of NMDA receptor trafficking by amyloid-β
    • E.M. Snyder, Y. Nong, C.G. Almeida, and et al. Regulation of NMDA receptor trafficking by amyloid-β Nat. Neurosci. 8 2005 1051 1058
    • (2005) Nat. Neurosci. , vol.8 , pp. 1051-1058
    • Snyder, E.M.1    Nong, Y.2    Almeida, C.G.3
  • 10
    • 34249672242 scopus 로고    scopus 로고
    • Aβ oligomers induce neuronal oxidative stress through an N-methyl-D-aspartate receptor-dependent mechanism that is blocked by the Alzheimer drug memantine
    • F.G. De Felice, P.T. Velasco, M.P. Lambert, and et al. Aβ 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. 282 2007 11590 11601
    • (2007) J. Biol. Chem. , vol.282 , pp. 11590-11601
    • De Felice, F.G.1    Velasco, P.T.2    Lambert, M.P.3
  • 11
    • 80052982307 scopus 로고    scopus 로고
    • The synaptic protein neuroligin-1 interacts with the amyloid β-peptide. Is there a role in Alzheimer's disease?
    • M.C. Dinamarca, D. Weinstein, O. Monasterio, and N.C. Inestrosa The synaptic protein neuroligin-1 interacts with the amyloid β-peptide. Is there a role in Alzheimer's disease? Biochemistry 50 2011 8127 8137
    • (2011) Biochemistry , vol.50 , pp. 8127-8137
    • Dinamarca, M.C.1    Weinstein, D.2    Monasterio, O.3    Inestrosa, N.C.4
  • 12
    • 84863445395 scopus 로고    scopus 로고
    • The role of neurexins and neuroligins in the formation, maturation, and function of vertebrate synapses
    • D.D. Krueger, L.P. Tuffy, T. Papadopoulus, and N. Brose The role of neurexins and neuroligins in the formation, maturation, and function of vertebrate synapses Curr. Opin. Neurobiol. 22 2012 412 422
    • (2012) Curr. Opin. Neurobiol. , vol.22 , pp. 412-422
    • Krueger, D.D.1    Tuffy, L.P.2    Papadopoulus, T.3    Brose, N.4
  • 13
    • 0242317361 scopus 로고    scopus 로고
    • Making connections: cholinesterase-domain proteins in the CNS
    • F.G. Scholl, and P. Scheiffele Making connections: cholinesterase-domain proteins in the CNS Trends Neurosci. 26 2003 618 624
    • (2003) Trends Neurosci , vol.26 , pp. 618-624
    • Scholl, F.G.1    Scheiffele, P.2
  • 14
    • 0029863697 scopus 로고    scopus 로고
    • Acetylcholinesterase accelerates assembly of amyloid-β-peptides into Alzheimer's fibrils: possible role of the peripheral site of the enzyme
    • N.C. Inestrosa, A. Alvarez, C.A. Pérez, and et al. Acetylcholinesterase accelerates assembly of amyloid-β-peptides into Alzheimer's fibrils: possible role of the peripheral site of the enzyme Neuron 16 1996 881 891
    • (1996) Neuron , vol.16 , pp. 881-891
    • Inestrosa, N.C.1    Alvarez, A.2    Pérez, C.A.3
  • 15
    • 38549098085 scopus 로고    scopus 로고
    • Amyloid-cholinesterase interactions. Implications for Alzheimer's disease
    • N.C. Inestrosa, M.C. Dinamarca, and A. Alvarez Amyloid-cholinesterase interactions. Implications for Alzheimer's disease FEBS J. 275 2008 625 632
    • (2008) FEBS J , vol.275 , pp. 625-632
    • Inestrosa, N.C.1    Dinamarca, M.C.2    Alvarez, A.3
  • 16
    • 0346118881 scopus 로고    scopus 로고
    • Characterization of the interaction of a recombinant soluble neuroligin-1 with neurexin-1β
    • D. Comoletti, R. Flynn, L.L. Jennings, and et al. Characterization of the interaction of a recombinant soluble neuroligin-1 with neurexin-1β J. Biol. Chem. 278 2003 50497 50505
    • (2003) J. Biol. Chem. , vol.278 , pp. 50497-50505
    • Comoletti, D.1    Flynn, R.2    Jennings, L.L.3
  • 17
    • 0019134836 scopus 로고
    • Isolation and characterization of postsynaptic densities from various brain regions: enrichment of different types of postsynaptic densities
    • R.K. Carlin, D.J. Grab, R.S. Cohen, and P.J. Siekevitz Isolation and characterization of postsynaptic densities from various brain regions: enrichment of different types of postsynaptic densities J. Cell Biol. 86 1980 831 843
    • (1980) J. Cell Biol. , vol.86 , pp. 831-843
    • Carlin, R.K.1    Grab, D.J.2    Cohen, R.S.3    Siekevitz, P.J.4
  • 18
    • 0031667493 scopus 로고    scopus 로고
    • Calcium/calmodulin-dependent protein kinase II is associated with NR2A/B subunits of NMDA receptor in postsynaptic densities
    • F. Gardoni, A. Caputi, M. Cimino, and et al. Calcium/calmodulin-dependent protein kinase II is associated with NR2A/B subunits of NMDA receptor in postsynaptic densities J. Neurochem. 71 1998 1733 1741
    • (1998) J. Neurochem. , vol.71 , pp. 1733-1741
    • Gardoni, F.1    Caputi, A.2    Cimino, M.3
  • 19
    • 33750284656 scopus 로고    scopus 로고
    • Hyperforin prevents β-amyloid neurotoxicity and spatial memory impairments by disaggregation of Alzheimer's amyloid-β-deposits
    • M.C. Dinamarca, W. Cerpa, J. Garrido, J.L. Hancke, and N.C. Inestrosa Hyperforin prevents β-amyloid neurotoxicity and spatial memory impairments by disaggregation of Alzheimer's amyloid-β-deposits Mol. Psychiatry 11 2006 1032 1048
    • (2006) Mol. Psychiatry , vol.11 , pp. 1032-1048
    • Dinamarca, M.C.1    Cerpa, W.2    Garrido, J.3    Hancke, J.L.4    Inestrosa, N.C.5
  • 20
    • 67650136764 scopus 로고    scopus 로고
    • Wnt-5a/JNK signaling promotes the clustering of PSD-95 in hippocampal neurons
    • G.G. Farías, I.E. Alfaro, W. Cerpa, and et al. Wnt-5a/JNK signaling promotes the clustering of PSD-95 in hippocampal neurons J. Biol. Chem. 284 2009 15857 15866
    • (2009) J. Biol. Chem. , vol.284 , pp. 15857-15866
    • Farías, G.G.1    Alfaro, I.E.2    Cerpa, W.3
  • 21
    • 77249117920 scopus 로고    scopus 로고
    • Wnt- 5a occludes Aβoligomer-induced depression of glutamatergic transmission in hippocampal neurons
    • W. Cerpa, G.G. Farias, J.A. Godoy, and et al. Wnt- 5a occludes Aβoligomer-induced depression of glutamatergic transmission in hippocampal neurons Mol. Neurodegener. 5 2010 3
    • (2010) Mol. Neurodegener. , vol.5 , pp. 3
    • Cerpa, W.1    Farias, G.G.2    Godoy, J.A.3
  • 22
    • 80053652289 scopus 로고    scopus 로고
    • Early neuronal dysfunction by amyloid β oligomers depends on activation of NR2B-containing NMDA receptors
    • R. Rönicke, M. Mikhaylova, S. Rönicke, and et al. Early neuronal dysfunction by amyloid β oligomers depends on activation of NR2B-containing NMDA receptors Neurobiol. Aging. 32 2011 2219-22128
    • (2011) Neurobiol. Aging. , vol.32 , pp. 2219-22128
    • Rönicke, R.1    Mikhaylova, M.2    Rönicke, S.3
  • 23
    • 54049091941 scopus 로고    scopus 로고
    • Neuroligins and neurexins link synaptic function to cognitive disease
    • T.C. Sudhof Neuroligins and neurexins link synaptic function to cognitive disease Nature 455 2008 903 911
    • (2008) Nature , vol.455 , pp. 903-911
    • Sudhof, T.C.1
  • 24
    • 41149087217 scopus 로고    scopus 로고
    • Crystal structure of the extracellular cholinesterase-like domain from neuroligin-2
    • J. Koehnke, X. Jin, E.C. Budreck, and et al. Crystal structure of the extracellular cholinesterase-like domain from neuroligin-2 Proc. Natl. Acad. Sci. U. S. A. 105 2008 1873 1878
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , pp. 1873-1878
    • Koehnke, J.1    Jin, X.2    Budreck, E.C.3
  • 25
    • 77955514673 scopus 로고    scopus 로고
    • Structure- function relationships of the a/β-hydrolase fold domain of neuroligin: a comparison with acetylcholinesterase
    • P. Leone, D. Comoletti, P. Taylor, and et al. Structure- function relationships of the a/β-hydrolase fold domain of neuroligin: a comparison with acetylcholinesterase Chem. Biol. Interact. 187 2010 49 55
    • (2010) Chem. Biol. Interact. , vol.187 , pp. 49-55
    • Leone, P.1    Comoletti, D.2    Taylor, P.3
  • 26
    • 0035807054 scopus 로고    scopus 로고
    • A structural motif of acetylcholinesterase that promotes amyloid β-peptide formation
    • G.V. De Ferrari, M.A. Canales, I. Shin, and et al. A structural motif of acetylcholinesterase that promotes amyloid β-peptide formation Biochemistry 40 2001 10447 10457
    • (2001) Biochemistry , vol.40 , pp. 10447-10457
    • De Ferrari, G.V.1    Canales, M.A.2    Shin, I.3
  • 27
    • 77953658771 scopus 로고    scopus 로고
    • Deleterious effects of Amyloid β Oligomers acting as an extracellular scaffold for mGluR5
    • M. Renner, P.N. Lacor, P.T. Velasco, and et al. Deleterious effects of Amyloid β Oligomers acting as an extracellular scaffold for mGluR5 Neuron 66 2010 739 754
    • (2010) Neuron , vol.66 , pp. 739-754
    • Renner, M.1    Lacor, P.N.2    Velasco, P.T.3
  • 28
    • 44049089139 scopus 로고    scopus 로고
    • Amyloid-β binds to the extracellular cysteine-rich domain of Frizzled and inhibits Wnt/β-catenin signaling
    • M.H. Magdesian, M.M. CarvalhoM, F.A. Mendes, and et al. Amyloid-β binds to the extracellular cysteine-rich domain of Frizzled and inhibits Wnt/β-catenin signaling J. Biol. Chem. 283 2008 9359 9368
    • (2008) J. Biol. Chem. , vol.283 , pp. 9359-9368
    • Magdesian, M.H.1    Carvalhom, M.M.2    Mendes, F.A.3
  • 29
    • 84927534618 scopus 로고    scopus 로고
    • Glutamate receptors function as scaffolds for the regulation of β-amyloid and cellular prion protein signaling complexes
    • A. Hamilton, G.W. Zamponi, and S.S. Ferguson Glutamate receptors function as scaffolds for the regulation of β-amyloid and cellular prion protein signaling complexes Mol. Brain 8 2015 18
    • (2015) Mol. Brain , vol.8 , pp. 18
    • Hamilton, A.1    Zamponi, G.W.2    Ferguson, S.S.3
  • 30
    • 84884200967 scopus 로고    scopus 로고
    • Metabotropic glutamate receptor 5 is a coreceptor for Alzheimer aβ oligomer bound to cellular prion protein
    • J.W. Um, A.C. Kaufman, M. Kostylev, and et al. Metabotropic glutamate receptor 5 is a coreceptor for Alzheimer aβ oligomer bound to cellular prion protein Neuron 79 2013 887 902
    • (2013) Neuron , vol.79 , pp. 887-902
    • Um, J.W.1    Kaufman, A.C.2    Kostylev, M.3
  • 31
    • 79956302348 scopus 로고    scopus 로고
    • Alzheimer's disease brain- derived amyloid-β-mediated inhibition of hLTP in vivo is prevented by immunotargeting cellular prion protein
    • A.E. Barry, I. KlyubinI, J.M. Mc Donald, and et al. Alzheimer's disease brain- derived amyloid-β-mediated inhibition of hLTP in vivo is prevented by immunotargeting cellular prion protein J. Neurosci. 31 2011 7259 7263
    • (2011) J. Neurosci. , vol.31 , pp. 7259-7263
    • Barry, A.E.1    Klyubini, I.2    Mc Donald, J.M.3
  • 32
    • 61349201380 scopus 로고    scopus 로고
    • Cellular prion protein mediates impairment of synaptic plasticity by amyloid-β oligomers
    • J. Laurén, D.A. Gimbel, H.B. Nygaard, and et al. Cellular prion protein mediates impairment of synaptic plasticity by amyloid-β oligomers Nature 457 2009 1128 1132
    • (2009) Nature , vol.457 , pp. 1128-1132
    • Laurén, J.1    Gimbel, D.A.2    Nygaard, H.B.3
  • 33
    • 76649093635 scopus 로고    scopus 로고
    • Synthetic amyloid-β oligomers impair long-term memory independently of cellular prion protein
    • C. Balducci, M. Beeg, M. Stravalaci, and et al. Synthetic amyloid-β oligomers impair long-term memory independently of cellular prion protein Proc. Natl. Acad. Sci. U. S. A. 107 2010 2295-22300
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , pp. 2295-22300
    • Balducci, C.1    Beeg, M.2    Stravalaci, M.3
  • 34
    • 84872200318 scopus 로고    scopus 로고
    • Neuroligin-1controls synaptic abundance of NMDA-type glutamate receptors through extracellular coupling
    • E.C. Budreck, O.B. Kwon, Jung, and et al. Neuroligin-1controls synaptic abundance of NMDA-type glutamate receptors through extracellular coupling Proc. Natl. Acad. Sci. U. S. A. 110 2013 725 730
    • (2013) Proc. Natl. Acad. Sci. U. S. A. , vol.110 , pp. 725-730
    • Budreck, E.C.1    Kwon, O.B.2    Jung3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.