메뉴 건너뛰기




Volumn 89, Issue 7, 2011, Pages 1031-1042

Intraneuronal amyloid β oligomers cause cell death via endoplasmic reticulum stress, endosomal/lysosomal leakage, and mitochondrial dysfunction in vivo

Author keywords

Alzheimer's disease; APP E693 mutation; Transgenic mouse

Indexed keywords

AMYLOID BETA PROTEIN; CATHEPSIN D; CYTOCHROME C; GLUCOSE REGULATED PROTEIN 78; OLIGOMER; UBIQUITIN PROTEIN LIGASE E3;

EID: 79955601720     PISSN: 03604012     EISSN: 10974547     Source Type: Journal    
DOI: 10.1002/jnr.22640     Document Type: Article
Times cited : (224)

References (53)
  • 1
    • 33646461282 scopus 로고    scopus 로고
    • β-amyloid accumulation impairs multivesicular body sorting by inhibiting the ubiquitin-proteasome system
    • Almeida CG, Takahashi RH, Gouras GK. 2006. β-amyloid accumulation impairs multivesicular body sorting by inhibiting the ubiquitin-proteasome system. J Neurosci 26: 4277-4288.
    • (2006) J Neurosci , vol.26 , pp. 4277-4288
    • Almeida, C.G.1    Takahashi, R.H.2    Gouras, G.K.3
  • 2
    • 0037437192 scopus 로고    scopus 로고
    • Mitochondrial targeting and a novel transmembrane arrest of Alzheimer's amyloid precursor protein impairs mitochondrial function in neuronal cells
    • Anandatheerthavarada HK, Biswas G, Robin MA, Avadhani NG. 2003. Mitochondrial targeting and a novel transmembrane arrest of Alzheimer's amyloid precursor protein impairs mitochondrial function in neuronal cells. J Cell Biol 161: 41-54.
    • (2003) J Cell Biol , vol.161 , pp. 41-54
    • Anandatheerthavarada, H.K.1    Biswas, G.2    Robin, M.A.3    Avadhani, N.G.4
  • 5
    • 0035120525 scopus 로고    scopus 로고
    • Evidence that neurones accumulating amyloid can undergo lysis to form amyloid plaques in Alzheimer's disease
    • D'Andrea MR, Nagele RG, Wang HY, Peterson PA, Lee DH. 2001. Evidence that neurones accumulating amyloid can undergo lysis to form amyloid plaques in Alzheimer's disease. Histopathology 38: 120-134.
    • (2001) Histopathology , vol.38 , pp. 120-134
    • D'Andrea, M.R.1    Nagele, R.G.2    Wang, H.Y.3    Peterson, P.A.4    Lee, D.H.5
  • 6
    • 0035110055 scopus 로고    scopus 로고
    • Lysosomal membrane damage in soluble Aβ-mediated cell death in Alzheimer's disease
    • Ditaranto K, Tekirian TL, Yang AJ. 2001. Lysosomal membrane damage in soluble Aβ-mediated cell death in Alzheimer's disease. Neurobiol Dis 8: 19-31.
    • (2001) Neurobiol Dis , vol.8 , pp. 19-31
    • Ditaranto, K.1    Tekirian, T.L.2    Yang, A.J.3
  • 8
    • 77951976610 scopus 로고    scopus 로고
    • Cell-produced α-synuclein oligomers are targeted to, and impair, the 26S proteasome
    • Emmanouilidou E, Stefanis L, Vekrellis K. 2010. Cell-produced α-synuclein oligomers are targeted to, and impair, the 26S proteasome. Neurobiol Aging 31: 953-968.
    • (2010) Neurobiol Aging , vol.31 , pp. 953-968
    • Emmanouilidou, E.1    Stefanis, L.2    Vekrellis, K.3
  • 10
    • 0035736259 scopus 로고    scopus 로고
    • Organelle-specific initiation of cell death pathways
    • Ferri KF, Kroemer G. 2001. Organelle-specific initiation of cell death pathways. Nat Cell Biol 3: E255-E263.
    • (2001) Nat Cell Biol , vol.3
    • Ferri, K.F.1    Kroemer, G.2
  • 13
  • 17
    • 0142200947 scopus 로고    scopus 로고
    • Role of protein aggregation in mitochondrial dysfunction and neurodegeneration in Alzheimer's and Parkinson's diseases
    • Hashimoto M, Rockenstein E, Crews L, Masliah E. 2003. Role of protein aggregation in mitochondrial dysfunction and neurodegeneration in Alzheimer's and Parkinson's diseases. Neuromolecular Med 4: 21-36.
    • (2003) Neuromolecular Med , vol.4 , pp. 21-36
    • Hashimoto, M.1    Rockenstein, E.2    Crews, L.3    Masliah, E.4
  • 21
    • 73949089674 scopus 로고    scopus 로고
    • Amyloid seeds formed by cellular uptake, concentration, and aggregation of the amyloid-β peptide
    • Hu X, Crick SL, Bu G, Frieden C, Pappu RV, Lee JM. 2009. Amyloid seeds formed by cellular uptake, concentration, and aggregation of the amyloid-β peptide. Proc Natl Acad Sci U S A 106: 20324-20329.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 20324-20329
    • Hu, X.1    Crick, S.L.2    Bu, G.3    Frieden, C.4    Pappu, R.V.5    Lee, J.M.6
  • 22
    • 0037077284 scopus 로고    scopus 로고
    • Apolipoprotein E4 potentiates amyloid β peptide-induced lysosomal leakage and apoptosis in neuronal cells
    • Ji ZS, Miranda RD, Newhouse YM, Weisgraber KH, Huang Y, Mahley RW. 2002. Apolipoprotein E4 potentiates amyloid β peptide-induced lysosomal leakage and apoptosis in neuronal cells. J Biol Chem 277: 21821-21828.
    • (2002) J Biol Chem , vol.277 , pp. 21821-21828
    • Ji, Z.S.1    Miranda, R.D.2    Newhouse, Y.M.3    Weisgraber, K.H.4    Huang, Y.5    Mahley, R.W.6
  • 26
    • 0035297712 scopus 로고    scopus 로고
    • Targeting small Aβ oligomers: the solution to an Alzheimer's disease conundrum?
    • Klein WL, Krafft GA, Finch CE. 2001. Targeting small Aβ oligomers: the solution to an Alzheimer's disease conundrum? Trends Neurosci 24: 219-224.
    • (2001) Trends Neurosci , vol.24 , pp. 219-224
    • Klein, W.L.1    Krafft, G.A.2    Finch, C.E.3
  • 27
    • 34250819839 scopus 로고    scopus 로고
    • Intracellular amyloid-β in Alzheimer's disease
    • LaFerla FM, Green KN, Oddo S. 2007. Intracellular amyloid-β 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
  • 29
    • 58449101589 scopus 로고    scopus 로고
    • Aβ42-induced neurodegeneration via an age-dependent autophagic-lysosomal injury in Drosophila
    • Ling D, Song HJ, Garza D, Neufeld TP, Salvaterra PM. 2009. Aβ42-induced neurodegeneration via an age-dependent autophagic-lysosomal injury in Drosophila. PLoS One 4: e4201.
    • (2009) PLoS One , vol.4
    • Ling, D.1    Song, H.J.2    Garza, D.3    Neufeld, T.P.4    Salvaterra, P.M.5
  • 30
    • 33646152108 scopus 로고    scopus 로고
    • Mitochondria are a direct site of Aβ 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 Aβ 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
  • 31
    • 34250198647 scopus 로고    scopus 로고
    • Inverse correlation between amyloid precursor protein and synaptic plasticity in transgenic mice
    • Matsuyama S, Teraoka R, Mori H, Tomiyama T. 2007. Inverse correlation between amyloid precursor protein and synaptic plasticity in transgenic mice. Neuroreport 18: 1083-1087.
    • (2007) Neuroreport , vol.18 , pp. 1083-1087
    • Matsuyama, S.1    Teraoka, R.2    Mori, H.3    Tomiyama, T.4
  • 33
    • 0034610743 scopus 로고    scopus 로고
    • Caspase-12 mediates endoplasmic-reticulum-specific apoptosis and cytotoxicity by amyloid-β
    • Nakagawa T, Zhu H, Morishima N, Li E, Xu J, Yankner BA, Yuan J. 2000. Caspase-12 mediates endoplasmic-reticulum-specific apoptosis and cytotoxicity by amyloid-β. Nature 403: 98-103.
    • (2000) Nature , vol.403 , pp. 98-103
    • Nakagawa, T.1    Zhu, H.2    Morishima, N.3    Li, E.4    Xu, J.5    Yankner, B.A.6    Yuan, J.7
  • 34
    • 62549147038 scopus 로고    scopus 로고
    • The E693Δ mutation in amyloid precursor protein increases intracellular accumulation of amyloid β oligomers and causes endoplasmic reticulum stress-induced apoptosis in cultured cells
    • Nishitsuji K, Tomiyama T, Ishibashi K, Ito K, Teraoka R, Lambert MP, Klein WL, Mori H. 2009. The E693Δ mutation in amyloid precursor protein increases intracellular accumulation of amyloid β oligomers and causes endoplasmic reticulum stress-induced apoptosis in cultured cells. Am J Pathol 174: 957-969.
    • (2009) Am J Pathol , vol.174 , pp. 957-969
    • Nishitsuji, K.1    Tomiyama, T.2    Ishibashi, K.3    Ito, K.4    Teraoka, R.5    Lambert, M.P.6    Klein, W.L.7    Mori, H.8
  • 35
    • 67349132288 scopus 로고    scopus 로고
    • Intracellular Aβ and C99 aggregates induce mitochondria-dependent cell death in human neuroglioma H4 cells through recruitment of the 20S proteasome subunits
    • Park HJ, Kim SS, Kang S, Rhim H. 2009. Intracellular Aβ and C99 aggregates induce mitochondria-dependent cell death in human neuroglioma H4 cells through recruitment of the 20S proteasome subunits. Brain Res 1273: 1-8.
    • (2009) Brain Res , vol.1273 , pp. 1-8
    • Park, H.J.1    Kim, S.S.2    Kang, S.3    Rhim, H.4
  • 38
    • 67649803186 scopus 로고    scopus 로고
    • Amyloid β, mitochondrial structural and functional dynamics in Alzheimer's disease
    • Reddy PH. 2009. Amyloid β, mitochondrial structural and functional dynamics in Alzheimer's disease. Exp Neurol 218: 286-292.
    • (2009) Exp Neurol , vol.218 , pp. 286-292
    • Reddy, P.H.1
  • 39
    • 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
  • 40
    • 31944449691 scopus 로고    scopus 로고
    • Evidence that Perutz's double-β-stranded subunit structure for β-amyloids also applies to their channel-forming structures in membranes
    • Singer SJ, Dewji NN. 2006. Evidence that Perutz's double-β-stranded subunit structure for β-amyloids also applies to their channel-forming structures in membranes. Proc Natl Acad Sci U S A 103: 1546-1550.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 1546-1550
    • Singer, S.J.1    Dewji, N.N.2
  • 41
    • 29644434199 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress and mitochondrial cell death pathways mediate A53T mutant α-synuclein-induced toxicity
    • Smith WW, Jiang H, Pei Z, Tanaka Y, Morita H, Sawa A, Dawson VL, Dawson TM, Ross CA. 2005. Endoplasmic reticulum stress and mitochondrial cell death pathways mediate A53T mutant α-synuclein-induced toxicity. Hum Mol Genet 14: 3801-3811.
    • (2005) Hum Mol Genet , vol.14 , pp. 3801-3811
    • Smith, W.W.1    Jiang, H.2    Pei, Z.3    Tanaka, Y.4    Morita, H.5    Sawa, A.6    Dawson, V.L.7    Dawson, T.M.8    Ross, C.A.9
  • 43
    • 4344594413 scopus 로고    scopus 로고
    • Syntaxin 5 interacts with presenilin holoproteins, but not with their N- or C-terminal fragments, and affects β-amyloid peptide production
    • Suga K, Tomiyama T, Mori H, Akagawa K. 2004. Syntaxin 5 interacts with presenilin holoproteins, but not with their N- or C-terminal fragments, and affects β-amyloid peptide production. Biochem J 381: 619-628.
    • (2004) Biochem J , vol.381 , pp. 619-628
    • Suga, K.1    Tomiyama, T.2    Mori, H.3    Akagawa, K.4
  • 45
    • 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
  • 48
    • 7244236841 scopus 로고    scopus 로고
    • A modified β-amyloid hypothesis: intraneuronal accumulation of the β-amyloid peptide-the first step of a fatal cascade
    • Wirths O, Multhaup G, Bayer TA. 2004. A modified β-amyloid hypothesis: intraneuronal accumulation of the β-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
  • 49
    • 0032526652 scopus 로고    scopus 로고
    • Loss of endosomal/lysosomal membrane impermeability is an early event in amyloid Aβ1-42 pathogenesis
    • Yang AJ, Chandswangbhuvana D, Margol L, Glabe CG. 1998. Loss of endosomal/lysosomal membrane impermeability is an early event in amyloid Aβ1-42 pathogenesis. J Neurosci Res 52: 691-698.
    • (1998) J Neurosci Res , vol.52 , pp. 691-698
    • Yang, A.J.1    Chandswangbhuvana, D.2    Margol, L.3    Glabe, C.G.4
  • 50
    • 70949097901 scopus 로고    scopus 로고
    • Cell-derived soluble oligomers of human amyloid-β peptides disturb cellular homeostasis and induce apoptosis in primary hippocampal neurons
    • Yang TT, Hsu CT, Kuo YM. 2009. Cell-derived soluble oligomers of human amyloid-β peptides disturb cellular homeostasis and induce apoptosis in primary hippocampal neurons. J Neural Transm 116: 1561-1569.
    • (2009) J Neural Transm , vol.116 , pp. 1561-1569
    • Yang, T.T.1    Hsu, C.T.2    Kuo, Y.M.3
  • 51
    • 70149093436 scopus 로고    scopus 로고
    • Mitochondrial bioenergetic deficit precedes Alzheimer's pathology in female mouse model of Alzheimer's disease
    • Yao J, Irwin RW, Zhao L, Nilsen J, Hamilton RT, Brinton RD. 2009. Mitochondrial bioenergetic deficit precedes Alzheimer's pathology in female mouse model of Alzheimer's disease. Proc Natl Acad Sci U S A 106: 14670-14675.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 14670-14675
    • Yao, J.1    Irwin, R.W.2    Zhao, L.3    Nilsen, J.4    Hamilton, R.T.5    Brinton, R.D.6
  • 52
    • 33846548110 scopus 로고    scopus 로고
    • ER stress and diseases
    • Yoshida H. 2007. ER stress and diseases. FEBS J 274: 630-658.
    • (2007) FEBS J , vol.274 , pp. 630-658
    • Yoshida, H.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.