메뉴 건너뛰기




Volumn 30, Issue 4, 2010, Pages 1512-1522

Expression of β-amyloid induced age-dependent presynaptic and axonal changes in Drosophila

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID BETA PROTEIN[1-42];

EID: 75349092711     PISSN: 02706474     EISSN: 15292401     Source Type: Journal    
DOI: 10.1523/JNEUROSCI.3699-09.2010     Document Type: Article
Times cited : (120)

References (72)
  • 1
    • 0033232718 scopus 로고    scopus 로고
    • Targeted expression of truncated glued disrupts giant fiber synapse formation in Drosophila
    • Allen MJ, Shan X, Caruccio P, Froggett SJ, Moffat KG, Murphey RK (1999) Targeted expression of truncated glued disrupts giant fiber synapse formation in Drosophila. J Neurosci 19:9374-9384.
    • (1999) J Neurosci , vol.19 , pp. 9374-9384
    • Allen, M.J.1    Shan, X.2    Caruccio, P.3    Froggett, S.J.4    Moffat, K.G.5    Murphey, R.K.6
  • 2
    • 29444455075 scopus 로고    scopus 로고
    • Drosophila as a model for human neurodegenerative disease
    • Bilen J, Bonini NM (2005) Drosophila as a model for human neurodegenerative disease. Annu Rev Genet 39:153-171.
    • (2005) Annu Rev Genet , vol.39 , pp. 153-171
    • Bilen, J.1    Bonini, N.M.2
  • 10
    • 33644986233 scopus 로고    scopus 로고
    • The nicotinic acetylcholine receptor Dalpha7 is required for an escape behavior in Drosophila
    • Fayyazuddin A, Zaheer MA, Hiesinger PR, Bellen HJ (2006) The nicotinic acetylcholine receptor Dalpha7 is required for an escape behavior in Drosophila. PLoS Biol 4:e63.
    • (2006) PLoS Biol , vol.4
    • Fayyazuddin, A.1    Zaheer, M.A.2    Hiesinger, P.R.3    Bellen, H.J.4
  • 11
    • 3242809725 scopus 로고    scopus 로고
    • A model for studying Alzheimer's Abeta42-induced toxicity in Drosophila melanogaster
    • Finelli A, Kelkar A, Song HJ, Yang H, Konsolaki M (2004) A model for studying Alzheimer's Abeta42-induced toxicity in Drosophila melanogaster. Mol Cell Neurosci 26:365-375.
    • (2004) Mol Cell Neurosci , vol.26 , pp. 365-375
    • Finelli, A.1    Kelkar, A.2    Song, H.J.3    Yang, H.4    Konsolaki, M.5
  • 13
    • 0021256895 scopus 로고
    • Alzheimer's disease: Initial report of the purification and characterization of a novel cerebrovascular amyloid protein
    • Glenner GG, Wong CW (1984) Alzheimer's disease: initial report of the purification and characterization of a novel cerebrovascular amyloid protein. Biochem Biophys Res Commun 120:885-890.
    • (1984) Biochem Biophys Res Commun , vol.120 , pp. 885-890
    • Glenner, G.G.1    Wong, C.W.2
  • 14
    • 45749151056 scopus 로고    scopus 로고
    • Animal models of Alzheimer's disease and frontotemporal dementia
    • Götz J, Ittner LM (2008) Animal models of Alzheimer's disease and frontotemporal dementia. Nat Rev Neurosci 9:532-544.
    • (2008) Nat Rev Neurosci , vol.9 , pp. 532-544
    • Götz, J.1    Ittner, L.M.2
  • 15
    • 25144501662 scopus 로고    scopus 로고
    • Intraneuronal Abeta accumulation and origin of plaques in Alzheimer's disease
    • Gouras GK, Almeida CG, Takahashi RH (2005) Intraneuronal Abeta accumulation and origin of plaques in Alzheimer's disease. Neurobiol Aging 26:1235-1244.
    • (2005) Neurobiol Aging , vol.26 , pp. 1235-1244
    • Gouras, G.K.1    Almeida, C.G.2    Takahashi, R.H.3
  • 18
    • 0037135111 scopus 로고    scopus 로고
    • The amyloid hypothesis of Alzheimer's disease: Progress and problems on the road to therapeutics
    • Hardy J, Selkoe DJ (2002) The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics. Science 297:353-356.
    • (2002) Science , vol.297 , pp. 353-356
    • Hardy, J.1    Selkoe, D.J.2
  • 22
    • 33645652013 scopus 로고    scopus 로고
    • Rolling blackout is required for synaptic vesicle exocytosis
    • Huang FD, Woodruff E, Mohrmann R, Broadie K (2006) Rolling blackout is required for synaptic vesicle exocytosis. J Neurosci 26:2369-2379.
    • (2006) J Neurosci , vol.26 , pp. 2369-2379
    • Huang, F.D.1    Woodruff, E.2    Mohrmann, R.3    Broadie, K.4
  • 23
    • 49649123892 scopus 로고    scopus 로고
    • Overexpression of neprilysin reduces alzheimer amyloid-beta42 (Abeta42)-induced neuron loss and intraneuronal Abeta42 deposits but causes a reduction in cAMP-responsive element-binding protein-mediated transcription, age-dependent axon pathology, and premature death in Drosophila
    • Iijima-Ando K, Hearn SA, Granger L, Shenton C, Gatt A, Chiang HC, Hakker I, Zhong Y, Iijima K (2008) Overexpression of neprilysin reduces alzheimer amyloid-beta42 (Abeta42)-induced neuron loss and intraneuronal Abeta42 deposits but causes a reduction in cAMP-responsive element-binding protein-mediated transcription, age-dependent axon pathology, and premature death in Drosophila. J Biol Chem 283:19066-19076.
    • (2008) J Biol Chem , vol.283 , pp. 19066-19076
    • Iijima-Ando, K.1    Hearn, S.A.2    Granger, L.3    Shenton, C.4    Gatt, A.5    Chiang, H.C.6    Hakker, I.7    Zhong, Y.8    Iijima, K.9
  • 24
    • 0019134485 scopus 로고
    • Organization of identified axons innervating the dorsal longitudinal flight muscle of Drosophila melanogaster
    • Ikeda K, Koenig JH, Tsuruhara T (1980) Organization of identified axons innervating the dorsal longitudinal flight muscle of Drosophila melanogaster. J Neurocytol 9:799-823.
    • (1980) J Neurocytol , vol.9 , pp. 799-823
    • Ikeda, K.1    Koenig, J.H.2    Tsuruhara, T.3
  • 26
    • 0037004511 scopus 로고    scopus 로고
    • Long-term potentiation is increased in the CA1 area of the hippocampus of APP(swe/ind) CRND8 mice
    • Jolas T, Zhang XS, Zhang Q, Wong G, Del Vecchio R, Gold L, Priestley T (2002) Long-term potentiation is increased in the CA1 area of the hippocampus of APP(swe/ind) CRND8 mice. Neurobiol Dis 11:394-409.
    • (2002) Neurobiol Dis , vol.11 , pp. 394-409
    • Jolas, T.1    Zhang, X.S.2    Zhang, Q.3    Wong, G.4    Del Vecchio, R.5    Gold, L.6    Priestley, T.7
  • 28
    • 0019134484 scopus 로고
    • Anatomy of the giant fibre pathway in Drosophila. I. Three thoracic components of the pathway
    • King DG, Wyman RJ (1980) Anatomy of the giant fibre pathway in Drosophila. I. Three thoracic components of the pathway. J Neurocytol 9:753-770.
    • (1980) J Neurocytol , vol.9 , pp. 753-770
    • King, D.G.1    Wyman, R.J.2
  • 29
    • 0037130472 scopus 로고    scopus 로고
    • 2+ at the Drosophila synapse
    • 2+ at the Drosophila synapse. Neuron 35:333-343.
    • (2002) Neuron , vol.35 , pp. 333-343
    • Kuromi, H.1    Kidokoro, Y.2
  • 30
    • 34250819839 scopus 로고    scopus 로고
    • Intracellular amyloid-beta in Alzheimer's disease
    • LaFerla FM, Green KN, Oddo S (2007) Intracellular amyloid-beta in Alzheimer's disease. Nat Rev Neurosci 8:499-509.
    • (2007) Nat Rev Neurosci , vol.8 , pp. 499-509
    • LaFerla, F.M.1    Green, K.N.2    Oddo, S.3
  • 31
    • 0033523480 scopus 로고    scopus 로고
    • Alterations in synaptic transmission and long-term potentiation in hippocampal slices from young and aged PDAPP mice
    • Larson J, Lynch G, Games D, Seubert P (1999) Alterations in synaptic transmission and long-term potentiation in hippocampal slices from young and aged PDAPP mice. Brain Res 840:23-35.
    • (1999) Brain Res , vol.840 , pp. 23-35
    • Larson, J.1    Lynch, G.2    Games, D.3    Seubert, P.4
  • 32
    • 33750347347 scopus 로고    scopus 로고
    • Mitochondrial dysfunction and oxidative stress in neurodegenerative diseases
    • Lin MT, Beal MF (2006) Mitochondrial dysfunction and oxidative stress in neurodegenerative diseases. Nature 443:787-795.
    • (2006) Nature , vol.443 , pp. 787-795
    • Lin, M.T.1    Beal, M.F.2
  • 33
    • 0024381253 scopus 로고
    • ATP-dependent directional movement of rat synaptic vesicles injected into the presynaptic terminal of squid giant synapse
    • Llinás R, Sugimori M, Lin JW, Leopold PL, Brady ST (1989) ATP-dependent directional movement of rat synaptic vesicles injected into the presynaptic terminal of squid giant synapse. Proc Natl Acad Sci U S A 86:5656-5660.
    • (1989) Proc Natl Acad Sci U S A , vol.86 , pp. 5656-5660
    • Llinás, R.1    Sugimori, M.2    Lin, J.W.3    Leopold, P.L.4    Brady, S.T.5
  • 36
    • 33646152108 scopus 로고    scopus 로고
    • Mitochondria are a direct site of A beta accumulation in Alzheimer's disease neurons: Implications for free radical generation and oxidative damage in disease progression
    • Manczak M, Anekonda TS, Henson E, Park BS, Quinn J, Reddy PH (2006) Mitochondria are a direct site of A beta accumulation in Alzheimer's disease neurons: implications for free radical generation and oxidative damage in disease progression. Hum Mol Genet 15:1437-1449.
    • (2006) Hum Mol Genet , vol.15 , pp. 1437-1449
    • Manczak, M.1    Anekonda, T.S.2    Henson, E.3    Park, B.S.4    Quinn, J.5    Reddy, P.H.6
  • 37
    • 33749242234 scopus 로고    scopus 로고
    • Drosophila in the study of neurodegenerative disease
    • Marsh JL, Thompson LM (2006) Drosophila in the study of neurodegenerative disease. Neuron 52:169-178.
    • (2006) Neuron , vol.52 , pp. 169-178
    • Marsh, J.L.1    Thompson, L.M.2
  • 41
    • 0036288788 scopus 로고    scopus 로고
    • Murakami K, Irie K, Morimoto A, Ohigashi H, Shindo M, Nagao M, Shimizu T, Shirasawa T (2002) Synthesis, aggregation, neurotoxicity, and secondary structure of various A beta 1-42 mutants of familial Alzheimer's disease at positions 21-23. Biochem Biophys Res Commun 294:5-10.
    • Murakami K, Irie K, Morimoto A, Ohigashi H, Shindo M, Nagao M, Shimizu T, Shirasawa T (2002) Synthesis, aggregation, neurotoxicity, and secondary structure of various A beta 1-42 mutants of familial Alzheimer's disease at positions 21-23. Biochem Biophys Res Commun 294:5-10.
  • 43
    • 48249103491 scopus 로고    scopus 로고
    • Neurodegenerative lysosomal disorders: A continuum from development to late age
    • Nixon RA, Yang DS, Lee JH (2008) Neurodegenerative lysosomal disorders: a continuum from development to late age. Autophagy 4:590-599.
    • (2008) Autophagy , vol.4 , pp. 590-599
    • Nixon, R.A.1    Yang, D.S.2    Lee, J.H.3
  • 45
    • 0027447286 scopus 로고
    • Neurodegeneration induced by beta-amyloid peptides in vitro: The role of peptide assembly state
    • Pike CJ, Burdick D, Walencewicz AJ, Glabe CG, Cotman CW (1993) Neurodegeneration induced by beta-amyloid peptides in vitro: the role of peptide assembly state. J Neurosci 13:1676-1687.
    • (1993) J Neurosci , vol.13 , pp. 1676-1687
    • Pike, C.J.1    Burdick, D.2    Walencewicz, A.J.3    Glabe, C.G.4    Cotman, C.W.5
  • 46
    • 33646759268 scopus 로고    scopus 로고
    • Kinesin-1 and Dynein are the primary motors for fast transport of mitochondria in Drosophila motor axons
    • Pilling AD, Horiuchi D, Lively CM, Saxton WM (2006) Kinesin-1 and Dynein are the primary motors for fast transport of mitochondria in Drosophila motor axons. Mol Biol Cell 17:2057-2068.
    • (2006) Mol Biol Cell , vol.17 , pp. 2057-2068
    • Pilling, A.D.1    Horiuchi, D.2    Lively, C.M.3    Saxton, W.M.4
  • 47
    • 39149122810 scopus 로고    scopus 로고
    • Amyloid beta, mitochondrial dysfunction and synaptic damage: Implications for cognitive decline in aging and Alzheimer's disease
    • Reddy PH, Beal MF (2008) Amyloid beta, mitochondrial dysfunction and synaptic damage: implications for cognitive decline in aging and Alzheimer's disease. Trends Mol Med 14:45-53.
    • (2008) Trends Mol Med , vol.14 , pp. 45-53
    • Reddy, P.H.1    Beal, M.F.2
  • 48
    • 84880185901 scopus 로고    scopus 로고
    • Alzheimer's disease-related alterations in synaptic density: Neocortex and hippocampus
    • Scheff SW, Price DA (2006) Alzheimer's disease-related alterations in synaptic density: neocortex and hippocampus. J Alzheimers Dis 9 [Suppl 3]:101-115.
    • (2006) J Alzheimers Dis , vol.9 , Issue.SUPPL. 3 , pp. 101-115
    • Scheff, S.W.1    Price, D.A.2
  • 49
    • 0022362882 scopus 로고
    • Fast axonal transport of foreign synaptic vesicles in squid axoplasm
    • Schroer TA, Brady ST, Kelly RB (1985) Fast axonal transport of foreign synaptic vesicles in squid axoplasm. J Cell Biol 101:568-572.
    • (1985) J Cell Biol , vol.101 , pp. 568-572
    • Schroer, T.A.1    Brady, S.T.2    Kelly, R.B.3
  • 50
    • 0035066332 scopus 로고    scopus 로고
    • Alzheimer's disease: Genes, proteins, and therapy
    • Selkoe DJ (2001) Alzheimer's disease: genes, proteins, and therapy. Physiol Rev 81:741-766.
    • (2001) Physiol Rev , vol.81 , pp. 741-766
    • Selkoe, D.J.1
  • 51
    • 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
  • 52
    • 44549087765 scopus 로고    scopus 로고
    • Soluble oligomers of the amyloid beta-protein impair synaptic plasticity and behavior
    • Selkoe DJ (2008) Soluble oligomers of the amyloid beta-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
  • 54
    • 33846282302 scopus 로고    scopus 로고
    • Shen J, Kelleher RJ 3rd (2007) The presenilin hypothesis of Alzheimer's disease: evidence for a loss-of-function pathogenic mechanism. Proc Natl Acad Sci U S A 104:403-409.
    • Shen J, Kelleher RJ 3rd (2007) The presenilin hypothesis of Alzheimer's disease: evidence for a loss-of-function pathogenic mechanism. Proc Natl Acad Sci U S A 104:403-409.
  • 55
    • 37249067994 scopus 로고    scopus 로고
    • The cell-selective neurotoxicity of the Alzheimer's Aβ peptide is determined by surface phosphatidylserine and cytosolic ATP levels. Membrane binding is required for Aβ toxicity
    • Simakova O, Arispe NJ (2007) The cell-selective neurotoxicity of the Alzheimer's Aβ peptide is determined by surface phosphatidylserine and cytosolic ATP levels. Membrane binding is required for Aβ toxicity. J Neurosci 27:13719-13729.
    • (2007) J Neurosci , vol.27 , pp. 13719-13729
    • Simakova, O.1    Arispe, N.J.2
  • 56
    • 0035433962 scopus 로고    scopus 로고
    • Alzheimer's disease and Abeta toxicity: From top to bottom
    • Small DH, Mok SS, Bornstein JC (2001) Alzheimer's disease and Abeta toxicity: from top to bottom. Nat Rev Neurosci 2:595-598.
    • (2001) Nat Rev Neurosci , vol.2 , pp. 595-598
    • Small, D.H.1    Mok, S.S.2    Bornstein, J.C.3
  • 59
    • 0030872413 scopus 로고    scopus 로고
    • Loss of the presynaptic vesicle protein synaptophysin in hippocampus correlates with cognitive decline in Alzheimer disease
    • Sze CI, Troncoso JC, Kawas C, Mouton P, Price DL, Martin LJ (1997) Loss of the presynaptic vesicle protein synaptophysin in hippocampus correlates with cognitive decline in Alzheimer disease. J Neuropathol Exp Neurol 56:933-944.
    • (1997) J Neuropathol Exp Neurol , vol.56 , pp. 933-944
    • Sze, C.I.1    Troncoso, J.C.2    Kawas, C.3    Mouton, P.4    Price, D.L.5    Martin, L.J.6
  • 60
    • 1842732209 scopus 로고    scopus 로고
    • Oligomerization of Alzheimer's β-amyloid within processes and synapses of cultured neurons and brain
    • Takahashi RH, Almeida CG, Kearney PF, Yu F, Lin MT, Milner TA, Gouras GK (2004) Oligomerization of Alzheimer's β-amyloid within processes and synapses of cultured neurons and brain. J Neurosci 24:3592-3599.
    • (2004) J Neurosci , vol.24 , pp. 3592-3599
    • Takahashi, R.H.1    Almeida, C.G.2    Kearney, P.F.3    Yu, F.4    Lin, M.T.5    Milner, T.A.6    Gouras, G.K.7
  • 61
    • 13944276825 scopus 로고    scopus 로고
    • Twenty years of the Alzheimer's disease amyloid hypothesis: A genetic perspective
    • Tanzi RE, Bertram L (2005) Twenty years of the Alzheimer's disease amyloid hypothesis: a genetic perspective. Cell 120:545-555.
    • (2005) Cell , vol.120 , pp. 545-555
    • Tanzi, R.E.1    Bertram, L.2
  • 63
    • 0025987048 scopus 로고
    • Physical basis of cognitive alterations in Alzheimer's disease: Synapse loss is the major correlate of cognitive impairment
    • Terry RD, Masliah E, Salmon DP, Butters N, DeTeresa R, Hill R, Hansen LA, Katzman R (1991) Physical basis of cognitive alterations in Alzheimer's disease: synapse loss is the major correlate of cognitive impairment. Ann Neurol 30:572-580.
    • (1991) Ann Neurol , vol.30 , pp. 572-580
    • Terry, R.D.1    Masliah, E.2    Salmon, D.P.3    Butters, N.4    DeTeresa, R.5    Hill, R.6    Hansen, L.A.7    Katzman, R.8
  • 64
    • 23044506102 scopus 로고    scopus 로고
    • Synaptic mitochondria are critical for mobilization of reserve pool vesicles at Drosophila neuromuscular junctions
    • Verstreken P, Ly CV, Venken KJ, Koh TW, Zhou Y, Bellen HJ (2005) Synaptic mitochondria are critical for mobilization of reserve pool vesicles at Drosophila neuromuscular junctions. Neuron 47:365-378.
    • (2005) Neuron , vol.47 , pp. 365-378
    • Verstreken, P.1    Ly, C.V.2    Venken, K.J.3    Koh, T.W.4    Zhou, Y.5    Bellen, H.J.6
  • 65
    • 0037041426 scopus 로고    scopus 로고
    • Naturally secreted oligomers of amyloid beta protein potently inhibit hippocampal long-term potentiation in vivo
    • Walsh DM, Klyubin I, Fadeeva JV, Cullen WK, Anwyl R, Wolfe MS, Rowan MJ, Selkoe DJ (2002) Naturally secreted oligomers of amyloid beta 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
  • 66
    • 33646384419 scopus 로고    scopus 로고
    • Immunology and immunotherapy of Alzheimer's disease
    • Weiner HL, Frenkel D (2006) Immunology and immunotherapy of Alzheimer's disease. Nat Rev Immunol 6:404-416.
    • (2006) Nat Rev Immunol , vol.6 , pp. 404-416
    • Weiner, H.L.1    Frenkel, D.2
  • 68
    • 7244236841 scopus 로고    scopus 로고
    • A modified beta-amyloid hypothesis: Intraneuronal accumulation of the beta-amyloid peptide - the first step of a fatal cascade
    • Wirths O, Multhaup G, Bayer TA (2004) A modified beta-amyloid hypothesis: intraneuronal accumulation of the beta-amyloid peptide - the first step of a fatal cascade. J Neurochem 91:513-520.
    • (2004) J Neurochem , vol.91 , pp. 513-520
    • Wirths, O.1    Multhaup, G.2    Bayer, T.A.3
  • 69
  • 70
    • 20444441575 scopus 로고    scopus 로고
    • Mitochondrial dysfunction and Alzheimer's disease: Role of amyloid-beta peptide alcohol dehydrogenase (ABAD)
    • Yan SD, Stern DM (2005) Mitochondrial dysfunction and Alzheimer's disease: role of amyloid-beta peptide alcohol dehydrogenase (ABAD). Int J Exp Pathol 86:161-171.
    • (2005) Int J Exp Pathol , vol.86 , pp. 161-171
    • Yan, S.D.1    Stern, D.M.2
  • 71
    • 0024990330 scopus 로고
    • Neurotrophic and neurotoxic effects of amyloid beta protein: Reversal by tachykinin neuropeptides
    • Yankner BA, Duffy LK, Kirschner DA (1990) Neurotrophic and neurotoxic effects of amyloid beta protein: reversal by tachykinin neuropeptides. Science 250:279-282.
    • (1990) Science , vol.250 , pp. 279-282
    • Yankner, B.A.1    Duffy, L.K.2    Kirschner, D.A.3
  • 72
    • 20844443826 scopus 로고    scopus 로고
    • Synaptic fatigue is more pronounced in the APP/PS1 transgenic mouse model of Alzheimer's disease
    • Zhang H, Gong B, Liu S, Fá M, Ninan I, Staniszewski A, Arancio O (2005) Synaptic fatigue is more pronounced in the APP/PS1 transgenic mouse model of Alzheimer's disease. Curr Alzheimer Res 2:137-140.
    • (2005) Curr Alzheimer Res , vol.2 , pp. 137-140
    • Zhang, H.1    Gong, B.2    Liu, S.3    Fá, M.4    Ninan, I.5    Staniszewski, A.6    Arancio, O.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.