메뉴 건너뛰기




Volumn 30, Issue 36, 2010, Pages 11938-11950

Aβ oligomers cause localized Ca2+ elevation, missorting of endogenous Tau into dendrites, Tau phosphorylation, and destruction of microtubules and spines

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID BETA PROTEIN; CALCIUM; CYCLIN DEPENDENT KINASE 5; EPITOPE; GLUTAMIC ACID; HYDROGEN PEROXIDE; MITOGEN ACTIVATED PROTEIN KINASE; PACLITAXEL; PHOSPHOTRANSFERASE; STRESS ACTIVATED PROTEIN KINASE; TAU PROTEIN; ADENOSINE TRIPHOSPHATE; LACTATE DEHYDROGENASE; NEUROFILAMENT PROTEIN; PEPTIDE FRAGMENT; PROTEIN KINASE;

EID: 77956587739     PISSN: 02706474     EISSN: 15292401     Source Type: Journal    
DOI: 10.1523/JNEUROSCI.2357-10.2010     Document Type: Article
Times cited : (561)

References (64)
  • 1
    • 33845394649 scopus 로고    scopus 로고
    • In search of the molecular basis of memory loss in Alzheimer disease
    • Ashe KH (2006) In search of the molecular basis of memory loss in Alzheimer disease. Alzheimer Dis Assoc Disord 20:200-201.
    • (2006) Alzheimer Dis Assoc Disord , vol.20 , pp. 200-201
    • Ashe, K.H.1
  • 2
    • 34548036227 scopus 로고    scopus 로고
    • Tau-mediated neurodegeneration in Alzheimer's disease and related disorders
    • DOI 10.1038/nrn2194, PII NRN2194
    • Ballatore C, Lee VM, Trojanowski JQ (2007) Tau-mediated neurodegeneration in Alzheimer's disease and related disorders. Nat Rev Neurosci 8:663-672. (Pubitemid 47283144)
    • (2007) Nature Reviews Neuroscience , vol.8 , Issue.9 , pp. 663-672
    • Ballatore, C.1    Lee, V.M.-Y.2    Trojanowski, J.Q.3
  • 4
    • 0026693232 scopus 로고
    • A high-affinity protein stain for Western blots, tissue prints, and electrophoretic gels
    • Bickar D, Reid PD (1992) A high-affinity protein stain for Western blots, tissue prints, and electrophoretic gels. Anal Biochem 203:109-115.
    • (1992) Anal Biochem , vol.203 , pp. 109-115
    • Bickar, D.1    Reid, P.D.2
  • 7
    • 0026134421 scopus 로고
    • Demonstration of amyloid deposits and neurofibrillary changes in whole brain sections
    • Braak H, Braak E (1991) Demonstration of amyloid deposits and neurofibrillary changes in whole brain sections. Brain Pathol 1:213-216.
    • (1991) Brain Pathol , vol.1 , pp. 213-216
    • Braak, H.1    Braak, E.2
  • 8
    • 34248576759 scopus 로고    scopus 로고
    • Physiology and pathophysiology of purinergic neurotransmission
    • Burnstock G (2007) Physiology and pathophysiology of purinergic neurotransmission. Physiol Rev 87:659-797.
    • (2007) Physiol Rev , vol.87 , pp. 659-797
    • Burnstock, G.1
  • 9
    • 0028986916 scopus 로고
    • Beta-amyloid fibrils induce tau phosphorylation and loss of microtubule binding
    • Busciglio J, Lorenzo A, Yeh J, Yankner BA (1995) beta-amyloid fibrils induce tau phosphorylation and loss of microtubule binding. Neuron 14:879-888.
    • (1995) Neuron , vol.14 , pp. 879-888
    • Busciglio, J.1    Lorenzo, A.2    Yeh, J.3    Yankner, B.A.4
  • 11
    • 65249107203 scopus 로고    scopus 로고
    • Microtubule assembly, organization and dynamics in axons and dendrites
    • Conde C, Cáceres A (2009) Microtubule assembly, organization and dynamics in axons and dendrites. Nat Rev Neurosci 10:319-332.
    • (2009) Nat Rev Neurosci , vol.10 , pp. 319-332
    • Conde, C.1    Cáceres, A.2
  • 12
    • 0030998758 scopus 로고    scopus 로고
    • Oxidative stress induces dephosphorylation of tau in rat brain primary neuronal cultures
    • Davis DR, Anderton BH, Brion JP, Reynolds CH, Hanger DP (1997) Oxidative stress induces dephosphorylation of tau in rat brain primary neuronal cultures. J Neurochem 68:1590-1597.
    • (1997) J Neurochem , vol.68 , pp. 1590-1597
    • Davis, D.R.1    Anderton, B.H.2    Brion, J.P.3    Reynolds, C.H.4    Hanger, D.P.5
  • 13
    • 34249672242 scopus 로고    scopus 로고
    • Abeta oligomers induce neuronal oxidative stress through an N-methyl-D-aspartate receptor-dependent mechanism that is blocked by the Alzheimer drug memantine
    • De Felice FG, Velasco PT, Lambert MP, Viola K, Fernandez SJ, Ferreira ST, Klein WL (2007) Abeta 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 282:11590-11601.
    • (2007) J Biol Chem , vol.282 , pp. 11590-11601
    • De Felice, F.G.1    Velasco, P.T.2    Lambert, M.P.3    Viola, K.4    Fernandez, S.J.5    Ferreira, S.T.6    Klein, W.L.7
  • 15
    • 12844282223 scopus 로고    scopus 로고
    • Proteasome-mediated effects on amyloid precursor protein processing at the gamma-secretase site
    • DOI 10.1042/BJ20041145
    • Flood F, Murphy S, Cowburn RF, Lannfelt L, Walker B, Johnston JA (2005) Proteasome-mediated effects on amyloid precursor protein processing at the gamma-secretase site. Biochem J 385:545-550. (Pubitemid 40165088)
    • (2005) Biochemical Journal , vol.385 , Issue.2 , pp. 545-550
    • Flood, F.1    Murphy, S.2    Cowburn, R.F.3    Lannfelt, L.4    Walkers, B.5    Johnston, J.A.6
  • 16
    • 57649148788 scopus 로고    scopus 로고
    • Structural classification of toxic amyloid oligomers
    • Glabe CG (2008) Structural classification of toxic amyloid oligomers. J Biol Chem 283:29639-29643.
    • (2008) J Biol Chem , vol.283 , pp. 29639-29643
    • Glabe, C.G.1
  • 17
    • 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
  • 18
    • 33847662852 scopus 로고    scopus 로고
    • Soluble protein oligomers in neurodegeneration: Lessons from the Alzheimer's amyloid beta-peptide
    • Haass C, Selkoe DJ (2007) Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid beta-peptide. Nat Rev Mol Cell Biol 8:101-112.
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 101-112
    • Haass, C.1    Selkoe, D.J.2
  • 19
    • 45149092373 scopus 로고    scopus 로고
    • Calmodulin binding and Cdk5 phosphorylation of p35 regulate its effect on microtubules
    • He L, Hou Z, Qi RZ (2008) Calmodulin binding and Cdk5 phosphorylation of p35 regulate its effect on microtubules. J Biol Chem 283:13252-13260.
    • (2008) J Biol Chem , vol.283 , pp. 13252-13260
    • He, L.1    Hou, Z.2    Qi, R.Z.3
  • 20
    • 30544452263 scopus 로고    scopus 로고
    • The axonal transport of mitochondria
    • Hollenbeck PJ, Saxton WM (2005) The axonal transport of mitochondria. J Cell Sci 118:5411-5419.
    • (2005) J Cell Sci , vol.118 , pp. 5411-5419
    • Hollenbeck, P.J.1    Saxton, W.M.2
  • 21
    • 33747401659 scopus 로고    scopus 로고
    • Tau phosphorylation and proteolysis: Insights and perspectives
    • Johnson GV (2006) Tau phosphorylation and proteolysis: insights and perspectives. J Alzheimers Dis 9:243-250.
    • (2006) J Alzheimers Dis , vol.9 , pp. 243-250
    • Johnson, G.V.1
  • 22
    • 0033133456 scopus 로고    scopus 로고
    • Beta-Amyloid precursor protein is detectable on monocytes and is increased in Alzheimer's disease
    • DOI 10.1016/S0197-4580(99)00051-2, PII S0197458099000512
    • Jung SS, Gauthier S, Cashman NR (1999) Beta-amyloid precursor protein is detectable on monocytes and is increased in Alzheimer's disease. Neurobiol Aging 20:249-257. (Pubitemid 29525410)
    • (1999) Neurobiology of Aging , vol.20 , Issue.3 , pp. 249-257
    • Jung, S.S.1    Gauthier, S.2    Cashman, N.R.3
  • 25
    • 33751218015 scopus 로고    scopus 로고
    • Tau-dependent microtubule disassembly initiated by prefibrillar beta-amyloid
    • King ME, Kan HM, Baas PW, Erisir A, Glabe CG, Bloom GS (2006) Tau-dependent microtubule disassembly initiated by prefibrillar beta-amyloid. J Cell Biol 175:541-546.
    • (2006) J Cell Biol , vol.175 , pp. 541-546
    • King, M.E.1    Kan, H.M.2    Baas, P.W.3    Erisir, A.4    Glabe, C.G.5    Bloom, G.S.6
  • 26
    • 13644267037 scopus 로고    scopus 로고
    • Mammalian SAD kinases are required for neuronal polarization
    • DOI 10.1126/science.1107403
    • Kishi M, Pan YA, Crump JG, Sanes JR (2005) Mammalian SAD kinases are required for neuronal polarization. Science 307:929-932. (Pubitemid 40229230)
    • (2005) Science , vol.307 , Issue.5711 , pp. 929-932
    • Kishi, M.1    Pan, Y.A.2    Crump, J.G.3    Sanes, J.R.4
  • 27
    • 33144484368 scopus 로고    scopus 로고
    • Synaptic targeting by Abeta oligomers (ADDLS) as a basis for memory loss in early Alzheimer's disease
    • Klein WL (2006) Synaptic targeting by Abeta oligomers (ADDLS) as a basis for memory loss in early Alzheimer's disease. Alzheimers Dement 2:43-55.
    • (2006) Alzheimers Dement , vol.2 , pp. 43-55
    • Klein, W.L.1
  • 28
    • 2542455537 scopus 로고    scopus 로고
    • Small assemblies of unmodified amyloid beta-protein are the proximate neurotoxin in Alzheimer's disease
    • Klein WL, Stine WB Jr, Teplow DB (2004) Small assemblies of unmodified amyloid beta-protein are the proximate neurotoxin in Alzheimer's disease. Neurobiol Aging 25:569-580.
    • (2004) Neurobiol Aging , vol.25 , pp. 569-580
    • Klein, W.L.1    Stine Jr., W.B.2    Teplow, D.B.3
  • 29
    • 67349200776 scopus 로고    scopus 로고
    • Tubulin tyrosination navigates the kinesin-1 motor domain to axons
    • Konishi Y, Setou M (2009) Tubulin tyrosination navigates the kinesin-1 motor domain to axons. Nat Neurosci 12:559-567.
    • (2009) Nat Neurosci , vol.12 , pp. 559-567
    • Konishi, Y.1    Setou, M.2
  • 30
    • 34548620157 scopus 로고    scopus 로고
    • Swimming against the tide: Mobility of the microtubule-associated protein tau in neurons
    • Konzack S, Thies E, Marx A, Mandelkow EM, Mandelkow E (2007) Swimming against the tide: mobility of the microtubule-associated protein tau in neurons. J Neurosci 27:9916-9927.
    • (2007) J Neurosci , vol.27 , pp. 9916-9927
    • Konzack, S.1    Thies, E.2    Marx, A.3    Mandelkow, E.M.4    Mandelkow, E.5
  • 31
    • 0027361281 scopus 로고
    • Microtubule-associated protein tau. Abnormal phosphorylation of a non-paired helical filament pool in Alzheimer disease
    • Köpke E, Tung YC, Shaikh S, Alonso AC, Iqbal K, Grundke-Iqbal I (1993) Microtubule-associated protein tau. Abnormal phosphorylation of a non-paired helical filament pool in Alzheimer disease. J Biol Chem 268:24374-24384.
    • (1993) J Biol Chem , vol.268 , pp. 24374-24384
    • Köpke, E.1    Tung, Y.C.2    Shaikh, S.3    Alonso, A.C.4    Iqbal, K.5    Grundke-Iqbal, I.6
  • 34
    • 54549102288 scopus 로고    scopus 로고
    • Beyond polymer polarity: How the cytoskeleton builds a polarized cell
    • Li R, Gundersen GG (2008) Beyond polymer polarity: how the cytoskeleton builds a polarized cell. Nat Rev Mol Cell Biol 9:860-873.
    • (2008) Nat Rev Mol Cell Biol , vol.9 , pp. 860-873
    • Li, R.1    Gundersen, G.G.2
  • 35
    • 12844250694 scopus 로고    scopus 로고
    • Induction of hyperphosphorylated tau in primary rat cortical neuron cultures mediated by oxidative stress and glycogen synthase kinase-3
    • Lovell MA, Xiong S, Xie C, Davies P, Markesbery WR (2004) Induction of hyperphosphorylated tau in primary rat cortical neuron cultures mediated by oxidative stress and glycogen synthase kinase-3. J Alzheimers Dis 6:659-671. (Pubitemid 40164172)
    • (2004) Journal of Alzheimer's Disease , vol.6 , Issue.6 , pp. 659-671
    • Lovell, M.A.1    Xiong, S.2    Xie, C.3    Davies, P.4    Markesbery, W.R.5
  • 36
    • 0025273543 scopus 로고
    • Antigenic changes similar to those seen in neurofibrillary tangles are elicited by glutamate and Ca2+ influx in cultured hippocampal neurons
    • Mattson MP (1990) Antigenic changes similar to those seen in neurofibrillary tangles are elicited by glutamate and Ca2+ influx in cultured hippocampal neurons. Neuron 4:105-117.
    • (1990) Neuron , vol.4 , pp. 105-117
    • Mattson, M.P.1
  • 37
    • 0026650367 scopus 로고
    • Effects of microtubule stabilization and destabilization on tau immunoreactivity in cultured hippocampal neurons
    • Mattson MP (1992) Effects of microtubule stabilization and destabilization on tau immunoreactivity in cultured hippocampal neurons. Brain Res 582:107-118.
    • (1992) Brain Res , vol.582 , pp. 107-118
    • Mattson, M.P.1
  • 38
    • 34249092704 scopus 로고    scopus 로고
    • Calcium and neurodegeneration
    • Mattson MP (2007) Calcium and neurodegeneration. Aging Cell 6:337-350.
    • (2007) Aging Cell , vol.6 , pp. 337-350
    • Mattson, M.P.1
  • 40
    • 70349295278 scopus 로고    scopus 로고
    • Structure-neurotoxicity relationships of amyloid beta-protein oligomers
    • Ono K, Condron MM, Teplow DB (2009) Structure-neurotoxicity relationships of amyloid beta-protein oligomers. Proc Natl Acad Sci U S A 106:14745-14750.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 14745-14750
    • Ono, K.1    Condron, M.M.2    Teplow, D.B.3
  • 41
    • 20044370830 scopus 로고    scopus 로고
    • The generation of a 17 kDa neurotoxic fragment: An alternative mechanism by which tau mediates beta-amyloid-induced neurodegeneration
    • Park SY, Ferreira A (2005) The generation of a 17 kDa neurotoxic fragment: an alternative mechanism by which tau mediates beta-amyloid-induced neurodegeneration. J Neurosci 25:5365-5375.
    • (2005) J Neurosci , vol.25 , pp. 5365-5375
    • Park, S.Y.1    Ferreira, A.2
  • 42
    • 0028170719 scopus 로고
    • Soluble amyloid beta-protein in the cerebrospinal fluid from patients with Alzheimer's disease, vascular dementia and controls
    • DOI 10.1016/0022-510X(94)90140-6
    • Pirttilä T, Kim KS, Mehta PD, Frey H, Wisniewski HM (1994) Soluble amyloid beta-protein in the cerebrospinal fluid from patients with Alzheimer's disease, vascular dementia and controls. J Neurol Sci 127:90-95. (Pubitemid 24372529)
    • (1994) Journal of the Neurological Sciences , vol.127 , Issue.1 , pp. 90-95
    • Pirttila, T.1    Kim, K.S.2    Mehta, P.D.3    Frey, H.4    Wisniewski, H.M.5
  • 45
  • 47
    • 5644239087 scopus 로고    scopus 로고
    • Alzheimer disease: Mechanistic understanding predicts novel therapies
    • Selkoe DJ (2004) Alzheimer disease: mechanistic understanding predicts novel therapies. Ann Intern Med 140:627-638.
    • (2004) Ann Intern Med , vol.140 , pp. 627-638
    • Selkoe, D.J.1
  • 48
    • 72849142054 scopus 로고    scopus 로고
    • Alzheimer's disease: Synaptic dysfunction and Abeta
    • Shankar GM, Walsh DM (2009) Alzheimer's disease: synaptic dysfunction and Abeta. Mol Neurodegener 4:48.
    • (2009) Mol Neurodegener , vol.4 , pp. 48
    • Shankar, G.M.1    Walsh, D.M.2
  • 49
    • 33947314641 scopus 로고    scopus 로고
    • Natural oligomers of the Alzheimer amyloid-beta protein induce reversible synapse loss by modulating an NMDA-type glutamate receptor-dependent signaling pathway
    • Shankar GM, Bloodgood BL, Townsend M, Walsh DM, Selkoe DJ, Sabatini BL (2007) Natural oligomers of the Alzheimer amyloid-beta protein induce reversible synapse loss by modulating an NMDA-type glutamate receptor-dependent signaling pathway. J Neurosci 27:2866-2875.
    • (2007) J Neurosci , vol.27 , pp. 2866-2875
    • Shankar, G.M.1    Bloodgood, B.L.2    Townsend, M.3    Walsh, D.M.4    Selkoe, D.J.5    Sabatini, B.L.6
  • 50
    • 56349119351 scopus 로고    scopus 로고
    • Linking Abeta and tau in late-onset Alzheimer's disease: A dual pathway hypothesis
    • Small SA, Duff K (2008) Linking Abeta and tau in late-onset Alzheimer's disease: a dual pathway hypothesis. Neuron 60:534-542.
    • (2008) Neuron , vol.60 , pp. 534-542
    • Small, S.A.1    Duff, K.2
  • 52
    • 0037128935 scopus 로고    scopus 로고
    • Tau blocks traffic of organelles, neurofilaments, and APP vesicles in neurons and enhances oxidative stress
    • DOI 10.1083/jcb.200108057
    • Stamer K, Vogel R, Thies E, Mandelkow E, Mandelkow EM (2002) Tau blocks traffic of organelles, neurofilaments, and APP vesicles in neurons and enhances oxidative stress. J Cell Biol 156:1051-1063. (Pubitemid 34839854)
    • (2002) Journal of Cell Biology , vol.156 , Issue.6 , pp. 1051-1063
    • Stamer, K.1    Vogel, R.2    Thies, E.3    Mandelkow, E.4    Mandelkow, E.-M.5
  • 53
    • 72249109630 scopus 로고    scopus 로고
    • Chronic oxidative stress causes increased tau phosphorylation in M17 neuroblastoma cells
    • Su B, Wang X, Lee HG, Tabaton M, Perry G, Smith MA, Zhu X (2010) Chronic oxidative stress causes increased tau phosphorylation in M17 neuroblastoma cells. Neurosci Lett 468:267-271.
    • (2010) Neurosci Lett , vol.468 , pp. 267-271
    • Su, B.1    Wang, X.2    Lee, H.G.3    Tabaton, M.4    Perry, G.5    Smith, M.A.6    Zhu, X.7
  • 54
    • 33947307791 scopus 로고    scopus 로고
    • Missorting of tau in neurons causes degeneration of synapses that can be rescued by the kinase MARK2/Par-1
    • Thies E, Mandelkow EM (2007) Missorting of tau in neurons causes degeneration of synapses that can be rescued by the kinase MARK2/Par-1. J Neurosci 27:2896-2907.
    • (2007) J Neurosci , vol.27 , pp. 2896-2907
    • Thies, E.1    Mandelkow, E.M.2
  • 55
    • 49649116434 scopus 로고    scopus 로고
    • Glycogen synthase kinase (GSK) 3beta directly phosphorylates Serine 212 in the regulatory loop and inhibits microtubule affinity-regulating kinase (MARK) 2
    • Timm T, Balusamy K, Li X, Biernat J, Mandelkow E, Mandelkow EM (2008) Glycogen synthase kinase (GSK) 3beta directly phosphorylates Serine 212 in the regulatory loop and inhibits microtubule affinity-regulating kinase (MARK) 2. J Biol Chem 283:18873-18882.
    • (2008) J Biol Chem , vol.283 , pp. 18873-18882
    • Timm, T.1    Balusamy, K.2    Li, X.3    Biernat, J.4    Mandelkow, E.5    Mandelkow, E.M.6
  • 56
    • 34247396622 scopus 로고    scopus 로고
    • A calcium- and calmodulin-dependent kinase Ialpha/microtubule affinity regulating kinase 2 signaling cascade mediates calcium-dependent neurite outgrowth
    • Uboha NV, Flajolet M, Nairn AC, Picciotto MR (2007) A calcium- and calmodulin-dependent kinase Ialpha/microtubule affinity regulating kinase 2 signaling cascade mediates calcium-dependent neurite outgrowth. J Neurosci 27:4413-4423.
    • (2007) J Neurosci , vol.27 , pp. 4413-4423
    • Uboha, N.V.1    Flajolet, M.2    Nairn, A.C.3    Picciotto, M.R.4
  • 58
    • 58149091896 scopus 로고    scopus 로고
    • The mechanism of Ca2+-dependent regulation of kinesin-mediated mitochondrial motility
    • Wang X, Schwarz TL (2009) The mechanism of Ca2+-dependent regulation of kinesin-mediated mitochondrial motility. Cell 136:163-174.
    • (2009) Cell , vol.136 , pp. 163-174
    • Wang, X.1    Schwarz, T.L.2
  • 59
  • 60
    • 18944407388 scopus 로고    scopus 로고
    • Nucleation-dependent polymerization is an essential component of amyloid-mediated neuronal cell death
    • DOI 10.1523/JNEUROSCI.2381-04.2005
    • Wogulis M, Wright S, Cunningham D, Chilcote T, Powell K, Rydel RE (2005) Nucleation-dependent polymerization is an essential component of amyloid-mediated neuronal cell death. J Neurosci 25:1071-1080. (Pubitemid 41741352)
    • (2005) Journal of Neuroscience , vol.25 , Issue.5 , pp. 1071-1080
    • Wogulis, M.1    Wright, S.2    Cunningham, D.3    Chilcote, T.4    Powell, K.5    Rydel, R.E.6
  • 62
    • 77249162118 scopus 로고    scopus 로고
    • Axon degeneration: Mechanisms and implications of a distinct program from cell death
    • Yan T, Feng Y, Zhai Q (2010) Axon degeneration: Mechanisms and implications of a distinct program from cell death. Neurochem Int 56:529-534.
    • (2010) Neurochem Int , vol.56 , pp. 529-534
    • Yan, T.1    Feng, Y.2    Zhai, Q.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.