메뉴 건너뛰기




Volumn 12, Issue 12, 2009, Pages 1567-1576

Amyloid-Β as a positive endogenous regulator of release probability at hippocampal synapses

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID BETA PROTEIN; MEMBRANE METALLOENDOPEPTIDASE;

EID: 70549106846     PISSN: 10976256     EISSN: None     Source Type: Journal    
DOI: 10.1038/nn.2433     Document Type: Article
Times cited : (426)

References (50)
  • 1
    • 0026646604 scopus 로고
    • Amyloid β-peptide is produced by cultured cells during normal metabolism
    • Haass, C. et al. Amyloid β-peptide is produced by cultured cells during normal metabolism. Nature 359, 322-325 (1992).
    • (1992) Nature , vol.359 , pp. 322-325
    • Haass, C.1
  • 2
    • 0026646605 scopus 로고
    • Isolation and quantifcation of soluble Alzheimer's β-peptide from biological fuids
    • Seubert, P. et al. Isolation and quantifcation of soluble Alzheimer's β-peptide from biological fuids. Nature 359, 325-327 (1992).
    • (1992) Nature , vol.359 , pp. 325-327
    • Seubert, P.1
  • 3
    • 0026760261 scopus 로고
    • Production of the Alzheimer amyloid β protein by normal proteolytic processing
    • Shoji, M. et al. Production of the Alzheimer amyloid β protein by normal proteolytic processing. Science 258, 126-129 (1992).
    • (1992) Science , vol.258 , pp. 126-129
    • Shoji, M.1
  • 4
    • 0034049944 scopus 로고    scopus 로고
    • Proteolytic processing and cell biological functions of the amyloid precursor protein
    • De Strooper, B. & Annaert, W. Proteolytic processing and cell biological functions of the amyloid precursor protein. J. Cell Sci. 113, 1857-1870 (2000). (Pubitemid 30386490)
    • (2000) Journal of Cell Science , vol.113 , Issue.11 , pp. 1857-1870
    • De Strooper, B.1    Annaert, W.2
  • 5
    • 1442264828 scopus 로고    scopus 로고
    • Take fve-BACE and the gamma-secretase quartet conduct Alzheimer's amyloid β-peptide generation
    • Haass, C. Take fve-BACE and the gamma-secretase quartet conduct Alzheimer's amyloid β-peptide generation. EMBO J. 23, 483-488 (2004).
    • (2004) EMBO J , vol.23 , pp. 483-488
    • Haass, C.1
  • 6
    • 0344672942 scopus 로고    scopus 로고
    • APP processing and synaptic function
    • Kamenetz, F. et al. APP processing and synaptic function. Neuron 37, 925-937 (2003).
    • (2003) Neuron , vol.37 , pp. 925-937
    • Kamenetz, F.1
  • 7
    • 29144487182 scopus 로고    scopus 로고
    • Synaptic activity regulates interstitial fuid amyloid-β levels in vivo
    • Cirrito, J.R. et al. Synaptic activity regulates interstitial fuid amyloid-β levels in vivo. Neuron 48, 913-922 (2005).
    • (2005) Neuron , vol.48 , pp. 913-922
    • Cirrito, J.R.1
  • 8
    • 41549155927 scopus 로고    scopus 로고
    • Endocytosis is required for synaptic activity-dependent release of amyloid-β in vivo
    • Cirrito, J.R. et al. Endocytosis is required for synaptic activity-dependent release of amyloid-β in vivo. Neuron 58, 42-51 (2008).
    • (2008) Neuron , vol.58 , pp. 42-51
    • Cirrito, J.R.1
  • 9
    • 27344441173 scopus 로고    scopus 로고
    • Metabolism of amyloid-β peptide and Alzheimer's disease
    • Iwata, N., Higuchi, M. & Saido, T.C. Metabolism of amyloid-β peptide and Alzheimer's disease. Pharmacol. Ther. 108, 129-148 (2005).
    • (2005) Pharmacol. Ther , vol.108 , pp. 129-148
    • Iwata, N.1    Higuchi, M.2    Saido, T.C.3
  • 10
    • 0035950225 scopus 로고    scopus 로고
    • Clearing the brain's amyloid cobwebs
    • Selkoe, D.J. Clearing the brain's amyloid cobwebs. Neuron 32, 177-180 (2001).
    • (2001) Neuron , vol.32 , pp. 177-180
    • Selkoe, D.J.1
  • 11
    • 9144266913 scopus 로고    scopus 로고
    • Presynaptic localization of neprilysin contributes to effcient clearance of amyloid-β peptide in mouse brain
    • Iwata, N. et al. Presynaptic localization of neprilysin contributes to effcient clearance of amyloid-β peptide in mouse brain. J. Neurosci. 24, 991-998 (2004).
    • (2004) J. Neurosci , vol.24 , pp. 991-998
    • Iwata, N.1
  • 12
    • 0023335033 scopus 로고
    • Amino acid sequence of rabbit kidney neutral endopeptidase 24.11 (enkephalinase) deduced from a complementary DNA
    • Devault, A. et al. Amino acid sequence of rabbit kidney neutral endopeptidase 24.11 (enkephalinase) deduced from a complementary DNA. EMBO J. 6, 1317-1322 (1987).
    • (1987) EMBO J , vol.6 , pp. 1317-1322
    • Devault, A.1
  • 13
    • 0025987048 scopus 로고
    • Physical basis of cognitive alterations in Alzheimer's disease: Synapse loss is the major correlate of cognitive impairment
    • Terry, R.D. et al. Physical basis of cognitive alterations in Alzheimer's disease: synapse loss is the major correlate of cognitive impairment. Ann. Neurol. 30, 572-580 (1991).
    • (1991) Ann. Neurol , vol.30 , pp. 572-580
    • Terry, R.D.1
  • 14
    • 0025269152 scopus 로고
    • Synapse loss in frontal cortex biopsies in Alzheimer's disease: Correlation with cognitive severity
    • DeKosky, S.T. & Scheff, S.W. Synapse loss in frontal cortex biopsies in Alzheimer's disease: correlation with cognitive severity. Ann. Neurol. 27, 457-464 (1990).
    • (1990) Ann. Neurol , vol.27 , pp. 457-464
    • Dekosky, S.T.1    Scheff, S.W.2
  • 15
    • 33845411954 scopus 로고    scopus 로고
    • AMPAR removal underlies Aβ-induced synaptic depression and dendritic spine loss
    • Hsieh, H. et al. AMPAR removal underlies Aβ-induced synaptic depression and dendritic spine loss. Neuron 52, 831-843 (2006).
    • (2006) Neuron , vol.52 , pp. 831-843
    • Hsieh, H.1
  • 16
    • 33645520634 scopus 로고    scopus 로고
    • Early-onset behavioral and synaptic defcits in a mouse model of Alzheimer's disease
    • Jacobsen, J.S. et al. Early-onset behavioral and synaptic defcits in a mouse model of Alzheimer's disease. Proc. Natl. Acad. Sci. USA 103, 5161-5166 (2006).
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 5161-5166
    • Jacobsen, J.S.1
  • 17
    • 33947314641 scopus 로고    scopus 로고
    • Natural oligomers of the Alzheimer amyloid-β protein induce reversible synapse loss by modulating an NMDA-type glutamate receptor-dependent signaling pathway
    • Shankar, G.M. et al. Natural oligomers of the Alzheimer amyloid-β protein induce reversible synapse loss by modulating an NMDA-type glutamate receptor-dependent signaling pathway. J. Neurosci. 27, 2866-2875 (2007).
    • (2007) J. Neurosci , vol.27 , pp. 2866-2875
    • Shankar, G.M.1
  • 18
    • 49149124343 scopus 로고    scopus 로고
    • Amyloid-β protein dimers isolated directly from Alzheimer's brains impair synaptic plasticity and memory
    • Shankar, G.M. et al. Amyloid-β protein dimers isolated directly from Alzheimer's brains impair synaptic plasticity and memory. Nat. Med. 14, 837-842 (2008).
    • (2008) Nat. Med , vol.14 , pp. 837-842
    • Shankar, G.M.1
  • 19
    • 33645038471 scopus 로고    scopus 로고
    • A specifc amyloid-β protein assembly in the brain impairs memory
    • Lesné, S. et al. A specifc amyloid-β protein assembly in the brain impairs memory. Nature 440, 352-357 (2006).
    • (2006) Nature , vol.440 , pp. 352-357
    • Lesné, S.1
  • 20
    • 0033570337 scopus 로고    scopus 로고
    • Protofbrillar intermediates of amyloid β-protein induce acute electrophysiological changes and progressive neurotoxicity in cortical neurons
    • Hartley, D.M. et al. Protofbrillar intermediates of amyloid β-protein induce acute electrophysiological changes and progressive neurotoxicity in cortical neurons. J. Neurosci. 19, 8876-8884 (1999).
    • (1999) J. Neurosci , vol.19 , pp. 8876-8884
    • Hartley, D.M.1
  • 21
    • 3543060658 scopus 로고    scopus 로고
    • Amyloid β-protein induced electrophysiological changes are dependent on aggregation state: N-methyl-d-aspartate (NMDA) versus non-NMDA receptor/channel activation
    • Ye, C., Walsh, D.M., Selkoe, D.J. & Hartley, D.M. Amyloid β-protein induced electrophysiological changes are dependent on aggregation state: N-methyl-d-aspartate (NMDA) versus non-NMDA receptor/channel activation. Neurosci. Lett. 366, 320-325 (2004).
    • (2004) Neurosci. Lett , vol.366 , pp. 320-325
    • Ye, C.1    Walsh, D.M.2    Selkoe, D.J.3    Hartley, D.M.4
  • 22
    • 38549141544 scopus 로고    scopus 로고
    • Amyloid {β} oligomers (A{β}1-42 globulomer) suppress spontaneous synaptic activity by inhibition of P/Q-type calcium currents
    • Nimmrich, V. et al. Amyloid {β} oligomers (A{β}1-42 globulomer) suppress spontaneous synaptic activity by inhibition of P/Q-type calcium currents. J. Neurosci. 28, 788-797 (2008).
    • (2008) J. Neurosci , vol.28 , pp. 788-797
    • Nimmrich, V.1
  • 23
    • 0033621739 scopus 로고    scopus 로고
    • Identifcation of the major Aβ1-42-degrading catabolic pathway in brain parenchyma: Suppression leads to biochemical and pathological deposition
    • Iwata, N. et al. Identifcation of the major Aβ1-42-degrading catabolic pathway in brain parenchyma: suppression leads to biochemical and pathological deposition. Nat. Med. 6, 143-150 (2000).
    • (2000) Nat. Med , vol.6 , pp. 143-150
    • Iwata, N.1
  • 24
    • 0035947207 scopus 로고    scopus 로고
    • Metabolic regulation of brain Aβ by neprilysin
    • Iwata, N. et al. Metabolic regulation of brain Aβ by neprilysin. Science 292, 1550-1552 (2001).
    • (2001) Science , vol.292 , pp. 1550-1552
    • Iwata, N.1
  • 25
    • 0035877747 scopus 로고    scopus 로고
    • Neprilysin degrades both amyloid β peptides 1-40 and 1-42 most rapidly and effciently among thiorphan-and phosphoramidon-sensitive endopeptidases
    • Shirotani, K. et al. Neprilysin degrades both amyloid β peptides 1-40 and 1-42 most rapidly and effciently among thiorphan-and phosphoramidon-sensitive endopeptidases. J. Biol. Chem. 276, 21895-21901 (2001).
    • (2001) J. Biol. Chem , vol.276 , pp. 21895-21901
    • Shirotani, K.1
  • 26
    • 0027487057 scopus 로고
    • The kinetics of synaptic vesicle recycling measured at single presynaptic boutons
    • Ryan, T.A. et al. The kinetics of synaptic vesicle recycling measured at single presynaptic boutons. Neuron 11, 713-724 (1993).
    • (1993) Neuron , vol.11 , pp. 713-724
    • Ryan, T.A.1
  • 27
    • 0030895332 scopus 로고    scopus 로고
    • Heterogeneous release properties of visualized individual hippocampal synapses
    • Murthy, V.N., Sejnowski, T.J. & Stevens, C.F. Heterogeneous release properties of visualized individual hippocampal synapses. Neuron 18, 599-612 (1997).
    • (1997) Neuron , vol.18 , pp. 599-612
    • Murthy, V.N.1    Sejnowski, T.J.2    Stevens, C.F.3
  • 28
    • 9644303173 scopus 로고    scopus 로고
    • Enhancement of synaptic plasticity through chronically reduced Ca2+ fux during uncorrelated activity
    • Slutsky, I., Sadeghpour, S., Li, B. & Liu, G. Enhancement of synaptic plasticity through chronically reduced Ca2+ fux during uncorrelated activity. Neuron 44, 835-849 (2004).
    • (2004) Neuron , vol.44 , pp. 835-849
    • Slutsky, I.1    Sadeghpour, S.2    Li, B.3    Liu, G.4
  • 29
    • 0034955245 scopus 로고    scopus 로고
    • Visualization of changes in presynaptic function during long-term synaptic plasticity
    • Zakharenko, S.S., Zablow, L. & Siegelbaum, S.A. Visualization of changes in presynaptic function during long-term synaptic plasticity. Nat. Neurosci. 4, 711-717 (2001).
    • (2001) Nat. Neurosci , vol.4 , pp. 711-717
    • Zakharenko, S.S.1    Zablow, L.2    Siegelbaum, S.A.3
  • 30
    • 0028988801 scopus 로고
    • β-Amyloid precursor protein-defcient mice show reactive gliosis and decreased locomotor activity
    • Zheng, H. et al. β-Amyloid precursor protein-defcient mice show reactive gliosis and decreased locomotor activity. Cell 81, 525-531 (1995).
    • (1995) Cell , vol.81 , pp. 525-531
    • Zheng, H.1
  • 31
    • 0029670738 scopus 로고    scopus 로고
    • Paired-pulse facilitation and depression at unitary synapses in rat hippocampus: Quantal fuctuation affects subsequent release
    • Debanne, D., Guerineau, N.C., Gahwiler, B.H. & Thompson, S.M. Paired-pulse facilitation and depression at unitary synapses in rat hippocampus: quantal fuctuation affects subsequent release. J. Physiol. (Lond.) 491, 163-176 (1996).
    • (1996) J. Physiol. (Lond.) , vol.491 , pp. 163-176
    • Debanne, D.1    Guerineau, N.C.2    Gahwiler, B.H.3    Thompson, S.M.4
  • 32
    • 0030919664 scopus 로고    scopus 로고
    • Heterogeneity of release probability, facilitation, and depletion at central synapses
    • Dobrunz, L.E. & Stevens, C.F. Heterogeneity of release probability, facilitation, and depletion at central synapses. Neuron 18, 995-1008 (1997).
    • (1997) Neuron , vol.18 , pp. 995-1008
    • Dobrunz, L.E.1    Stevens, C.F.2
  • 33
    • 0037174618 scopus 로고    scopus 로고
    • Alzheimer's disease is a synaptic failure
    • Selkoe, D.J. Alzheimer's disease is a synaptic failure. Science 298, 789-791 (2002).
    • (2002) Science , vol.298 , pp. 789-791
    • Selkoe, D.J.1
  • 34
    • 0036201201 scopus 로고    scopus 로고
    • Short-term synaptic plasticity
    • Zucker, R.S. & Regehr, W.G. Short-term synaptic plasticity. Annu. Rev. Physiol. 64, 355-405 (2002).
    • (2002) Annu. Rev. Physiol , vol.64 , pp. 355-405
    • Zucker, R.S.1    Regehr, W.G.2
  • 35
    • 7244229524 scopus 로고    scopus 로고
    • Synaptic computation
    • Abbott, L.F. & Regehr, W.G. Synaptic computation. Nature 431, 796-803 (2004).
    • (2004) Nature , vol.431 , pp. 796-803
    • Abbott, L.F.1    Regehr, W.G.2
  • 36
    • 34447625042 scopus 로고    scopus 로고
    • The sequence of events that underlie quantal transmission at central glutamatergic synapses
    • Lisman, J.E., Raghavachari, S. & Tsien, R.W. The sequence of events that underlie quantal transmission at central glutamatergic synapses. Nat. Rev. Neurosci. 8, 597-609 (2007).
    • (2007) Nat. Rev. Neurosci , vol.8 , pp. 597-609
    • Lisman, J.E.1    Raghavachari, S.2    Tsien, R.W.3
  • 37
    • 0031059920 scopus 로고    scopus 로고
    • Bursts as a unit of neural information: Making unreliable synapses reliable
    • Lisman, J.E. Bursts as a unit of neural information: making unreliable synapses reliable. Trends Neurosci. 20, 38-43 (1997).
    • (1997) Trends Neurosci , vol.20 , pp. 38-43
    • Lisman, J.E.1
  • 38
    • 0014259321 scopus 로고
    • The role of calcium in neuromuscular facilitation
    • Katz, B. & Miledi, R. The role of calcium in neuromuscular facilitation. J. Physiol. (Lond.) 195, 481-492 (1968).
    • (1968) J. Physiol. (Lond.) , vol.195 , pp. 481-492
    • Katz, B.1    Miledi, R.2
  • 39
    • 19444365446 scopus 로고    scopus 로고
    • Allosteric modulation of the presynaptic Ca2+ sensor for vesicle fusion
    • Lou, X., Scheuss, V. & Schneggenburger, R. Allosteric modulation of the presynaptic Ca2+ sensor for vesicle fusion. Nature 435, 497-501 (2005).
    • (2005) Nature , vol.435 , pp. 497-501
    • Lou, X.1    Scheuss, V.2    Schneggenburger, R.3
  • 40
    • 0033017690 scopus 로고    scopus 로고
    • Age-related cognitive defcits, impaired long-term potentiation and reduction in synaptic marker density in mice lacking the β-amyloid precursor protein
    • Dawson, G.R. et al. Age-related cognitive defcits, impaired long-term potentiation and reduction in synaptic marker density in mice lacking the β-amyloid precursor protein. Neuroscience 90, 1-13 (1999).
    • (1999) Neuroscience , vol.90 , pp. 1-13
    • Dawson, G.R.1
  • 41
    • 0033012737 scopus 로고    scopus 로고
    • Mechanisms contributing to the defcits in hippocampal synaptic plasticity in mice lacking amyloid precursor protein
    • Seabrook, G.R. et al. Mechanisms contributing to the defcits in hippocampal synaptic plasticity in mice lacking amyloid precursor protein. Neuropharmacology 38, 349-359 (1999).
    • (1999) Neuropharmacology , vol.38 , pp. 349-359
    • Seabrook, G.R.1
  • 42
    • 0346055155 scopus 로고    scopus 로고
    • BACE1 defciency rescues memory defcits and cholinergic dysfunction in a mouse model of Alzheimer's disease
    • Ohno, M. et al. BACE1 defciency rescues memory defcits and cholinergic dysfunction in a mouse model of Alzheimer's disease. Neuron 41, 27-33 (2004).
    • (2004) Neuron , vol.41 , pp. 27-33
    • Ohno, M.1
  • 43
    • 11144354609 scopus 로고    scopus 로고
    • Loss of presenilin function causes impairments of memory and synaptic plasticity followed by age-dependent neurodegeneration
    • Saura, C.A. et al. Loss of presenilin function causes impairments of memory and synaptic plasticity followed by age-dependent neurodegeneration. Neuron 42, 23-36 (2004).
    • (2004) Neuron , vol.42 , pp. 23-36
    • Saura, C.A.1
  • 44
    • 58149385218 scopus 로고    scopus 로고
    • Picomolar amyloid-β positively modulates synaptic plasticity and memory in hippocampus
    • Puzzo, D. et al. Picomolar amyloid-β positively modulates synaptic plasticity and memory in hippocampus. J. Neurosci. 28, 14537-14545 (2008).
    • (2008) J. Neurosci , vol.28 , pp. 14537-14545
    • Puzzo, D.1
  • 45
    • 34548264782 scopus 로고    scopus 로고
    • Aberrant excitatory neuronal activity and compensatory remodeling of inhibitory hippocampal circuits in mouse models of Alzheimer's disease
    • Palop, J.J. et al. Aberrant excitatory neuronal activity and compensatory remodeling of inhibitory hippocampal circuits in mouse models of Alzheimer's disease. Neuron 55, 697-711 (2007).
    • (2007) Neuron , vol.55 , pp. 697-711
    • Palop, J.J.1
  • 46
    • 50649114611 scopus 로고    scopus 로고
    • Amyloid-β dynamics correlate with neurological status in the injured human brain
    • Brody, D.L. et al. Amyloid-β dynamics correlate with neurological status in the injured human brain. Science 321, 1221-1224 (2008).
    • (2008) Science , vol.321 , pp. 1221-1224
    • Brody, D.L.1
  • 47
    • 13044287361 scopus 로고    scopus 로고
    • Plaque-independent disruption of neural circuits in Alzheimer's disease mouse models
    • Hsia, A.Y. et al. Plaque-independent disruption of neural circuits in Alzheimer's disease mouse models. Proc. Natl. Acad. Sci. USA 96, 3228-3233 (1999).
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 3228-3233
    • Hsia, A.Y.1
  • 48
    • 0025217385 scopus 로고
    • Quantitative assessment of cortical synaptic density in Alzheimer's disease
    • Scheff, S.W., DeKosky, S.T. & Price, D.A. Quantitative assessment of cortical synaptic density in Alzheimer's disease. Neurobiol. Aging 11, 29-37 (1990).
    • (1990) Neurobiol. Aging , vol.11 , pp. 29-37
    • Scheff, S.W.1    Dekosky, S.T.2    Price, D.A.3
  • 49
    • 23944444806 scopus 로고    scopus 로고
    • Molecular, structural, and functional characterization of Alzheimer's disease: Evidence for a relationship between default activity, amyloid, and memory
    • Buckner, R.L. et al. Molecular, structural, and functional characterization of Alzheimer's disease: evidence for a relationship between default activity, amyloid, and memory. J. Neurosci. 25, 7709-7717 (2005).
    • (2005) J. Neurosci , vol.25 , pp. 7709-7717
    • Buckner, R.L.1
  • 50
    • 0034075589 scopus 로고    scopus 로고
    • Axonal membrane proteins are transported in distinct carriers: A two-color video microscopy study in cultured hippocampal neurons
    • Kaether, C., Skehel, P. & Dotti, C.G. Axonal membrane proteins are transported in distinct carriers: a two-color video microscopy study in cultured hippocampal neurons. Mol. Biol. Cell 11, 1213-1224 (2000).
    • (2000) Mol. Biol. Cell , vol.11 , pp. 1213-1224
    • Kaether, C.1    Skehel, P.2    Dotti, C.G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.