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Volumn 72, Issue 1, 2011, Pages 57-71

Exogenous α-Synuclein Fibrils Induce Lewy Body Pathology Leading to Synaptic Dysfunction and Neuron Death

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA SYNUCLEIN; MUTANT PROTEIN; RECOMBINANT PROTEIN;

EID: 80053613574     PISSN: 08966273     EISSN: 10974199     Source Type: Journal    
DOI: 10.1016/j.neuron.2011.08.033     Document Type: Article
Times cited : (1171)

References (46)
  • 2
    • 72149125838 scopus 로고    scopus 로고
    • The transcellular spread of cytosolic amyloids, prions, and prionoids
    • Aguzzi A., Rajendran L. The transcellular spread of cytosolic amyloids, prions, and prionoids. Neuron 2009, 64:783-790.
    • (2009) Neuron , vol.64 , pp. 783-790
    • Aguzzi, A.1    Rajendran, L.2
  • 4
    • 0031934154 scopus 로고    scopus 로고
    • Adsorptive endocytosis mediates the passage of HIV-1 across the blood-brain barrier: evidence for a post-internalization coreceptor
    • Banks W.A., Akerstrom V., Kastin A.J. Adsorptive endocytosis mediates the passage of HIV-1 across the blood-brain barrier: evidence for a post-internalization coreceptor. J. Cell Sci. 1998, 111:533-540.
    • (1998) J. Cell Sci. , vol.111 , pp. 533-540
    • Banks, W.A.1    Akerstrom, V.2    Kastin, A.J.3
  • 5
    • 0025863618 scopus 로고
    • Neuropathological stageing of Alzheimer-related changes
    • Braak H., Braak E. Neuropathological stageing of Alzheimer-related changes. Acta Neuropathol. 1991, 82:239-259.
    • (1991) Acta Neuropathol. , vol.82 , pp. 239-259
    • Braak, H.1    Braak, E.2
  • 8
    • 1842269785 scopus 로고
    • Transcytotic pathway for blood-borne protein through the blood-brain barrier
    • Broadwell R.D., Balin B.J., Salcman M. Transcytotic pathway for blood-borne protein through the blood-brain barrier. Proc. Natl. Acad. Sci. USA 1988, 85:632-636.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 632-636
    • Broadwell, R.D.1    Balin, B.J.2    Salcman, M.3
  • 11
    • 33751118534 scopus 로고    scopus 로고
    • Age-associated increases of alpha-synuclein in monkeys and humans are associated with nigrostriatal dopamine depletion: Is this the target for Parkinson's disease?
    • Chu Y., Kordower J.H. Age-associated increases of alpha-synuclein in monkeys and humans are associated with nigrostriatal dopamine depletion: Is this the target for Parkinson's disease?. Neurobiol. Dis. 2007, 25:134-149.
    • (2007) Neurobiol. Dis. , vol.25 , pp. 134-149
    • Chu, Y.1    Kordower, J.H.2
  • 13
    • 0034681163 scopus 로고    scopus 로고
    • Acceleration of oligomerization, not fibrillization, is a shared property of both alpha-synuclein mutations linked to early-onset Parkinson's disease: implications for pathogenesis and therapy
    • Conway K.A., Lee S.J., Rochet J.C., Ding T.T., Williamson R.E., Lansbury P.T. Acceleration of oligomerization, not fibrillization, is a shared property of both alpha-synuclein mutations linked to early-onset Parkinson's disease: implications for pathogenesis and therapy. Proc. Natl. Acad. Sci. USA 2000, 97:571-576.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 571-576
    • Conway, K.A.1    Lee, S.J.2    Rochet, J.C.3    Ding, T.T.4    Williamson, R.E.5    Lansbury, P.T.6
  • 17
    • 67649273927 scopus 로고    scopus 로고
    • Propagation of tau misfolding from the outside to the inside of a cell
    • Frost B., Jacks R.L., Diamond M.I. Propagation of tau misfolding from the outside to the inside of a cell. J. Biol. Chem. 2009, 284:12845-12852.
    • (2009) J. Biol. Chem. , vol.284 , pp. 12845-12852
    • Frost, B.1    Jacks, R.L.2    Diamond, M.I.3
  • 19
    • 0034651575 scopus 로고    scopus 로고
    • A panel of epitope-specific antibodies detects protein domains distributed throughout human alpha-synuclein in Lewy bodies of Parkinson's disease
    • Giasson B.I., Jakes R., Goedert M., Duda J.E., Leight S., Trojanowski J.Q., Lee V.M.-Y. A panel of epitope-specific antibodies detects protein domains distributed throughout human alpha-synuclein in Lewy bodies of Parkinson's disease. J. Neurosci. Res. 2000, 59:528-533.
    • (2000) J. Neurosci. Res. , vol.59 , pp. 528-533
    • Giasson, B.I.1    Jakes, R.2    Goedert, M.3    Duda, J.E.4    Leight, S.5    Trojanowski, J.Q.6    Lee, V.M.-Y.7
  • 20
    • 0035951869 scopus 로고    scopus 로고
    • A hydrophobic stretch of 12 amino acid residues in the middle of alpha-synuclein is essential for filament assembly
    • Giasson B.I., Murray I.V., Trojanowski J.Q., Lee V.M.-Y. A hydrophobic stretch of 12 amino acid residues in the middle of alpha-synuclein is essential for filament assembly. J. Biol. Chem. 2001, 276:2380-2386.
    • (2001) J. Biol. Chem. , vol.276 , pp. 2380-2386
    • Giasson, B.I.1    Murray, I.V.2    Trojanowski, J.Q.3    Lee, V.M.-Y.4
  • 21
    • 0015822048 scopus 로고
    • Detection of plasma membrane carbohydrates with lectin peroxidase conjugates
    • Gonatas N.K., Avrameas S. Detection of plasma membrane carbohydrates with lectin peroxidase conjugates. J. Cell Biol. 1973, 59:436-443.
    • (1973) J. Cell Biol. , vol.59 , pp. 436-443
    • Gonatas, N.K.1    Avrameas, S.2
  • 23
    • 79955441814 scopus 로고    scopus 로고
    • Seeding of normal Tau by pathological Tau conformers drives pathogenesis of Alzheimer-like tangles
    • Guo J.L., Lee V.M.-Y. Seeding of normal Tau by pathological Tau conformers drives pathogenesis of Alzheimer-like tangles. J. Biol. Chem. 2011, 286:15317-15331.
    • (2011) J. Biol. Chem. , vol.286 , pp. 15317-15331
    • Guo, J.L.1    Lee, V.M.-Y.2
  • 24
    • 0029257497 scopus 로고
    • The core Alzheimer's peptide NAC forms amyloid fibrils which seed and are seeded by beta-amyloid: is NAC a common trigger or target in neurodegenerative disease?
    • Han H., Weinreb P.H., Lansbury P.T. The core Alzheimer's peptide NAC forms amyloid fibrils which seed and are seeded by beta-amyloid: is NAC a common trigger or target in neurodegenerative disease?. Chem. Biol. 1995, 2:163-169.
    • (1995) Chem. Biol. , vol.2 , pp. 163-169
    • Han, H.1    Weinreb, P.H.2    Lansbury, P.T.3
  • 26
    • 0037469147 scopus 로고    scopus 로고
    • The N-terminal repeat domain of alpha-synuclein inhibits beta-sheet and amyloid fibril formation
    • Kessler J.C., Rochet J.C., Lansbury P.T. The N-terminal repeat domain of alpha-synuclein inhibits beta-sheet and amyloid fibril formation. Biochemistry 2003, 42:672-678.
    • (2003) Biochemistry , vol.42 , pp. 672-678
    • Kessler, J.C.1    Rochet, J.C.2    Lansbury, P.T.3
  • 27
    • 43249114934 scopus 로고    scopus 로고
    • Lewy body-like pathology in long-term embryonic nigral transplants in Parkinson's disease
    • Kordower J.H., Chu Y., Hauser R.A., Freeman T.B., Olanow C.W. Lewy body-like pathology in long-term embryonic nigral transplants in Parkinson's disease. Nat. Med. 2008, 14:504-506.
    • (2008) Nat. Med. , vol.14 , pp. 504-506
    • Kordower, J.H.1    Chu, Y.2    Hauser, R.A.3    Freeman, T.B.4    Olanow, C.W.5
  • 28
    • 61449216234 scopus 로고    scopus 로고
    • Transplanted dopaminergic neurons develop PD pathologic changes: a second case report
    • Kordower J.H., Chu Y., Hauser R.A., Olanow C.W., Freeman T.B. Transplanted dopaminergic neurons develop PD pathologic changes: a second case report. Mov. Disord. 2008, 23:2303-2306.
    • (2008) Mov. Disord. , vol.23 , pp. 2303-2306
    • Kordower, J.H.1    Chu, Y.2    Hauser, R.A.3    Olanow, C.W.4    Freeman, T.B.5
  • 32
    • 0034193399 scopus 로고    scopus 로고
    • Synucleins are developmentally expressed, and alpha-synuclein regulates the size of the presynaptic vesicular pool in primary hippocampal neurons
    • Murphy D.D., Rueter S.M., Trojanowski J.Q., Lee V.M.-Y. Synucleins are developmentally expressed, and alpha-synuclein regulates the size of the presynaptic vesicular pool in primary hippocampal neurons. J. Neurosci. 2000, 20:3214-3220.
    • (2000) J. Neurosci. , vol.20 , pp. 3214-3220
    • Murphy, D.D.1    Rueter, S.M.2    Trojanowski, J.Q.3    Lee, V.M.-Y.4
  • 34
    • 73549085595 scopus 로고    scopus 로고
    • Increased expression of alpha-synuclein reduces neurotransmitter release by inhibiting synaptic vesicle reclustering after endocytosis
    • Nemani V.M., Lu W., Berge V., Nakamura K., Onoa B., Lee M.K., Chaudhry F.A., Nicoll R.A., Edwards R.H. Increased expression of alpha-synuclein reduces neurotransmitter release by inhibiting synaptic vesicle reclustering after endocytosis. Neuron 2010, 65:66-79.
    • (2010) Neuron , vol.65 , pp. 66-79
    • Nemani, V.M.1    Lu, W.2    Berge, V.3    Nakamura, K.4    Onoa, B.5    Lee, M.K.6    Chaudhry, F.A.7    Nicoll, R.A.8    Edwards, R.H.9
  • 35
    • 0038307156 scopus 로고    scopus 로고
    • Ubiquitination of alpha-synuclein is not required for formation of pathological inclusions in alpha-synucleinopathies
    • Sampathu D.M., Giasson B.I., Pawlyk A.C., Trojanowski J.Q., Lee V.M.-Y. Ubiquitination of alpha-synuclein is not required for formation of pathological inclusions in alpha-synucleinopathies. Am. J. Pathol. 2003, 163:91-100.
    • (2003) Am. J. Pathol. , vol.163 , pp. 91-100
    • Sampathu, D.M.1    Giasson, B.I.2    Pawlyk, A.C.3    Trojanowski, J.Q.4    Lee, V.M.-Y.5
  • 36
    • 0034712918 scopus 로고    scopus 로고
    • Fiber diffraction of synthetic alpha-synuclein filaments shows amyloid-like cross-beta conformation
    • Serpell L.C., Berriman J., Jakes R., Goedert M., Crowther R.A. Fiber diffraction of synthetic alpha-synuclein filaments shows amyloid-like cross-beta conformation. Proc. Natl. Acad. Sci. USA 2000, 97:4897-4902.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 4897-4902
    • Serpell, L.C.1    Berriman, J.2    Jakes, R.3    Goedert, M.4    Crowther, R.A.5
  • 39
    • 0032584686 scopus 로고    scopus 로고
    • Filamentous alpha-synuclein inclusions link multiple system atrophy with Parkinson's disease and dementia with Lewy bodies
    • Spillantini M.G., Crowther R.A., Jakes R., Cairns N.J., Lantos P.L., Goedert M. Filamentous alpha-synuclein inclusions link multiple system atrophy with Parkinson's disease and dementia with Lewy bodies. Neurosci. Lett. 1998, 251:205-208.
    • (1998) Neurosci. Lett. , vol.251 , pp. 205-208
    • Spillantini, M.G.1    Crowther, R.A.2    Jakes, R.3    Cairns, N.J.4    Lantos, P.L.5    Goedert, M.6
  • 42
    • 0035815664 scopus 로고    scopus 로고
    • Evidence for a partially folded intermediate in alpha-synuclein fibril formation
    • Uversky V.N., Li J., Fink A.L. Evidence for a partially folded intermediate in alpha-synuclein fibril formation. J. Biol. Chem. 2001, 276:10737-10744.
    • (2001) J. Biol. Chem. , vol.276 , pp. 10737-10744
    • Uversky, V.N.1    Li, J.2    Fink, A.L.3
  • 43
    • 43249108653 scopus 로고    scopus 로고
    • Specificity and regulation of casein kinase-mediated phosphorylation of alpha-synuclein
    • Waxman E.A., Giasson B.I. Specificity and regulation of casein kinase-mediated phosphorylation of alpha-synuclein. J Neuropathol. Exp. Neurol 2008, 67:402-416.
    • (2008) J Neuropathol. Exp. Neurol , vol.67 , pp. 402-416
    • Waxman, E.A.1    Giasson, B.I.2
  • 44
    • 68649095418 scopus 로고    scopus 로고
    • Molecular mechanisms of alpha-synuclein neurodegeneration
    • Waxman E.A., Giasson B.I. Molecular mechanisms of alpha-synuclein neurodegeneration. Biochim. Biophys. Acta 2009, 1792:616-624.
    • (2009) Biochim. Biophys. Acta , vol.1792 , pp. 616-624
    • Waxman, E.A.1    Giasson, B.I.2
  • 46
    • 0033538541 scopus 로고    scopus 로고
    • Alpha-synuclein fibrillogenesis is nucleation-dependent. Implications for the pathogenesis of Parkinson's disease
    • Wood S.J., Wypych J., Steavenson S., Louis J.C., Citron M., Biere A.L. alpha-synuclein fibrillogenesis is nucleation-dependent. Implications for the pathogenesis of Parkinson's disease. J. Biol. Chem. 1999, 274:19509-19512.
    • (1999) J. Biol. Chem. , vol.274 , pp. 19509-19512
    • Wood, S.J.1    Wypych, J.2    Steavenson, S.3    Louis, J.C.4    Citron, M.5    Biere, A.L.6


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