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Volumn 5, Issue , 2014, Pages

Glucocerebrosidase depletion enhances cell-to-cell transmission of α-synuclein

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA SYNUCLEIN; GLUCOSYLCERAMIDASE; BETA GLUCOSIDASE; GBA2 PROTEIN, HUMAN;

EID: 84907360500     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/ncomms5755     Document Type: Article
Times cited : (153)

References (34)
  • 1
    • 0042974099 scopus 로고    scopus 로고
    • Alpha-synuclein pathology in Parkinson's and Alzheimer's disease brain: Incidence and topographic distribution-A pilot study
    • Jellinger, K. A. Alpha-synuclein pathology in Parkinson's and Alzheimer's disease brain: incidence and topographic distribution-a pilot study. Acta Neuropathol. 106, 191-201 (2003).
    • (2003) Acta Neuropathol. , vol.106 , pp. 191-201
    • Jellinger, K.A.1
  • 2
    • 77949848854 scopus 로고    scopus 로고
    • Prion-like transmission of protein aggregates in neurodegenerative diseases
    • Brundin, P., Melki, R. & Kopito, R. Prion-like transmission of protein aggregates in neurodegenerative diseases. Nat. Rev. Mol. Cell. Biol. 11, 301-307 (2010).
    • (2010) Nat. Rev. Mol. Cell. Biol. , vol.11 , pp. 301-307
    • Brundin, P.1    Melki, R.2    Kopito, R.3
  • 4
    • 84862680670 scopus 로고    scopus 로고
    • Alpha-synuclein cell-to-cell transfer and seeding in grafted dopaminergic neurons in vivo
    • Angot, E. et al. Alpha-synuclein cell-to-cell transfer and seeding in grafted dopaminergic neurons in vivo. PLoS ONE 7, e39465 (2012).
    • (2012) PLoS ONE , vol.7
    • Angot, E.1
  • 5
    • 84865307818 scopus 로고    scopus 로고
    • Exosomal cell-to-cell transmission of alpha synuclein oligomers
    • Danzer, K. M. et al. Exosomal cell-to-cell transmission of alpha synuclein oligomers. Mol. Neurodegener. 7, 42 (2012).
    • (2012) Mol. Neurodegener. , vol.7 , pp. 42
    • Danzer, K.M.1
  • 6
    • 84893858665 scopus 로고    scopus 로고
    • Extracellular alpha-synuclein-A novel and crucial factor in Lewy body diseases
    • Lee, H. J., Bae, E. J. & Lee, S. J. Extracellular alpha-synuclein-a novel and crucial factor in Lewy body diseases. Nat. Rev. Neurol. 10, 92-98 (2014).
    • (2014) Nat. Rev. Neurol. , vol.10 , pp. 92-98
    • Lee, H.J.1    Bae, E.J.2    Lee, S.J.3
  • 7
    • 41549114279 scopus 로고    scopus 로고
    • The role of autophagy-lysosome pathway in neurodegeneration associated with Parkinson's disease
    • Pan, T., Kondo, S., Le, W. & Jankovic, J. The role of autophagy-lysosome pathway in neurodegeneration associated with Parkinson's disease. Brain 131(Pt 8): 1969-1978 (2008).
    • (2008) Brain , vol.131 , Issue.8 PART , pp. 1969-1978
    • Pan, T.1    Kondo Le S, W.2    Jankovic, J.3
  • 8
    • 70350319531 scopus 로고    scopus 로고
    • Multicenter analysis of glucocerebrosidase mutations in Parkinson's disease
    • Sidransky, E. et al. Multicenter analysis of glucocerebrosidase mutations in Parkinson's disease. N. Engl. J. Med. 361, 1651-1661 (2009).
    • (2009) N. Engl. J. Med. , vol.361 , pp. 1651-1661
    • Sidransky, E.1
  • 9
    • 84878798127 scopus 로고    scopus 로고
    • A multicenter study of glucocerebrosidase mutations in dementia with Lewy bodies
    • Nalls, M. A. et al. A multicenter study of glucocerebrosidase mutations in dementia with Lewy bodies. JAMA Neurol. 70, 727-735 (2013).
    • (2013) JAMA Neurol. , vol.70 , pp. 727-735
    • Nalls, M.A.1
  • 10
    • 69149089854 scopus 로고    scopus 로고
    • Inclusion formation and neuronal cell death through neuronto-neuron transmission of alpha-synuclein
    • Desplats, P. et al. Inclusion formation and neuronal cell death through neuronto-neuron transmission of alpha-synuclein. Proc. Natl Acad. Sci. USA 106, 13010-13015 (2009).
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 13010-13015
    • Desplats, P.1
  • 11
    • 44749083979 scopus 로고    scopus 로고
    • Assembly-dependent endocytosis and clearance of extracellular alpha-synuclein
    • Lee, H.-J. et al. Assembly-dependent endocytosis and clearance of extracellular alpha-synuclein. Int. J. Biochem. Cell Biol. 40, 1835-1849 (2008).
    • (2008) Int. J. Biochem. Cell Biol. , vol.40 , pp. 1835-1849
    • Lee, H.-J.1
  • 12
    • 78049259996 scopus 로고    scopus 로고
    • Zooming into protein oligomerization in neurodegeneration using BiFC
    • Goncalves, S. A., Matos, J. E. & Outeiro, T. F. Zooming into protein oligomerization in neurodegeneration using BiFC. Trends Biochem. Sci. 35, 643-651 (2010).
    • (2010) Trends Biochem. Sci. , vol.35 , pp. 643-651
    • Goncalves, S.A.1    Matos, J.E.2    Outeiro, T.F.3
  • 13
    • 44849125207 scopus 로고    scopus 로고
    • Formation of toxic oligomeric alpha-synuclein species in living cells
    • Outeiro, T. F. et al. Formation of toxic oligomeric alpha-synuclein species in living cells. PLoS ONE 3, e1867 (2008).
    • (2008) PLoS ONE , vol.3
    • Outeiro, T.F.1
  • 14
    • 0036174010 scopus 로고    scopus 로고
    • Alpha-Synuclein is phosphorylated in synucleinopathy lesions
    • Fujiwara, H. et al. alpha-Synuclein is phosphorylated in synucleinopathy lesions. Nat. Cell. Biol. 4, 160-164 (2002).
    • (2002) Nat. Cell. Biol. , vol.4 , pp. 160-164
    • Fujiwara, H.1
  • 15
    • 0032568534 scopus 로고    scopus 로고
    • Alpha-Synuclein in filamentous inclusions of Lewy bodies from Parkinson's disease and dementia with lewy bodies
    • Spillantini, M. G., Crowther, R. A., Jakes, R., Hasegawa, M. & Goedert, M. alpha-Synuclein in filamentous inclusions of Lewy bodies from Parkinson's disease and dementia with lewy bodies. Proc. Natl Acad. Sci. USA 95, 6469-6473 (1998).
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 6469-6473
    • Spillantini, M.G.1    Crowther, R.A.2    Jakes, R.3    Hasegawa, M.4    Goedert, M.5
  • 16
    • 36949031267 scopus 로고    scopus 로고
    • Alpha-Synucleinopathy models and human neuropathology: Similarities and differences
    • Kahle, P. J. alpha-Synucleinopathy models and human neuropathology: similarities and differences. Acta Neuropathol. 115, 87-95 (2008).
    • (2008) Acta Neuropathol. , vol.115 , pp. 87-95
    • Kahle, P.J.1
  • 17
    • 84875898265 scopus 로고    scopus 로고
    • Neuron-released oligomeric alpha-synuclein is an endogenous agonist of TLR2 for paracrine activation of microglia
    • Kim, C. et al. Neuron-released oligomeric alpha-synuclein is an endogenous agonist of TLR2 for paracrine activation of microglia. Nat. Commun. 4, 1562 (2013).
    • (2013) Nat. Commun. , vol.4 , pp. 1562
    • Kim, C.1
  • 18
    • 77951885732 scopus 로고    scopus 로고
    • Non-classical exocytosis of alpha-synuclein is sensitive to folding states and promoted under stress conditions
    • Jang, A. et al. Non-classical exocytosis of alpha-synuclein is sensitive to folding states and promoted under stress conditions. J. Neurochem. 113, 1263-1274 (2010).
    • (2010) J. Neurochem. , vol.113 , pp. 1263-1274
    • Jang, A.1
  • 19
    • 84867036900 scopus 로고    scopus 로고
    • Glucocerebrosidase deficiency in substantia nigra of parkinson disease brains
    • Gegg, M. E. et al. Glucocerebrosidase deficiency in substantia nigra of parkinson disease brains. Ann. Neurol. 72, 455-463 (2012).
    • (2012) Ann. Neurol. , vol.72 , pp. 455-463
    • Gegg, M.E.1
  • 20
    • 66249129677 scopus 로고    scopus 로고
    • Association of glucocerebrosidase mutations with dementia with lewy bodies
    • Clark, L. N. et al. Association of glucocerebrosidase mutations with dementia with lewy bodies. Arch. Neurol. 66, 578-583 (2009).
    • (2009) Arch. Neurol. , vol.66 , pp. 578-583
    • Clark, L.N.1
  • 21
    • 84860708754 scopus 로고    scopus 로고
    • Cognitive performance of GBA mutation carriers with early-onset PD: The CORE-PD study
    • Alcalay, R. N. et al. Cognitive performance of GBA mutation carriers with early-onset PD: the CORE-PD study. Neurology 78, 1434-1440 (2012).
    • (2012) Neurology , vol.78 , pp. 1434-1440
    • Alcalay, R.N.1
  • 22
    • 84874307778 scopus 로고    scopus 로고
    • Glucocerebrosidase mutations influence the natural history of Parkinson's disease in a community-based incident cohort
    • Winder-Rhodes, S. E. et al. Glucocerebrosidase mutations influence the natural history of Parkinson's disease in a community-based incident cohort. Brain 136, 392-399 (2013).
    • (2013) Brain , vol.136 , pp. 392-399
    • Winder-Rhodes, S.E.1
  • 23
    • 77950571596 scopus 로고    scopus 로고
    • Direct transfer of alpha-synuclein from neuron to astroglia causes inflammatory responses in synucleinopathies
    • Lee, H. J. et al. Direct transfer of alpha-synuclein from neuron to astroglia causes inflammatory responses in synucleinopathies. J. Biol. Chem. 285, 9262-9272 (2010).
    • (2010) J. Biol. Chem. , vol.285 , pp. 9262-9272
    • Lee, H.J.1
  • 24
    • 84892538035 scopus 로고    scopus 로고
    • Alpha-synuclein transfers from neurons to oligodendrocytes
    • Reyes, J. F. et al. Alpha-synuclein transfers from neurons to oligodendrocytes. Glia 62, 387-398 (2014).
    • (2014) Glia , vol.62 , pp. 387-398
    • Reyes, J.F.1
  • 25
    • 26444609722 scopus 로고    scopus 로고
    • ER retention and degradation as the molecular basis underlying Gaucher disease heterogeneity
    • Ron, I. & Horowitz, M. ER retention and degradation as the molecular basis underlying Gaucher disease heterogeneity. Hum. Mol. Genet. 14, 2387-2398 (2005).
    • (2005) Hum. Mol. Genet. , vol.14 , pp. 2387-2398
    • Ron, I.1    Horowitz, M.2
  • 26
    • 79959925894 scopus 로고    scopus 로고
    • Alpha-synuclein interacts with Glucocerebrosidase providing a molecular link between Parkinson and Gaucher diseases
    • Yap, T. L. et al. Alpha-synuclein interacts with Glucocerebrosidase providing a molecular link between Parkinson and Gaucher diseases. J. Biol. Chem. 286, 28080-28088 (2011).
    • (2011) J. Biol. Chem. , vol.286 , pp. 28080-28088
    • Yap, T.L.1
  • 27
    • 79961083395 scopus 로고    scopus 로고
    • CNS expression of glucocerebrosidase corrects alpha-synuclein pathology and memory in a mouse model of gaucher-related synucleinopathy
    • Sardi, S. P. et al. CNS expression of glucocerebrosidase corrects alpha-synuclein pathology and memory in a mouse model of Gaucher-related synucleinopathy. Proc. Natl Acad. Sci. USA 108, 12101-12106 (2011).
    • (2011) Proc. Natl Acad. Sci. USA , vol.108 , pp. 12101-12106
    • Sardi, S.P.1
  • 28
    • 1442275729 scopus 로고    scopus 로고
    • Clearance of alpha-synuclein oligomeric intermediates via the lysosomal degradation pathway
    • Lee, H.-J., Khoshaghideh, F., Patel, S. & Lee, S.-J. Clearance of alpha-synuclein oligomeric intermediates via the lysosomal degradation pathway. J. Neurosci. 24, 1888-1896 (2004).
    • (2004) J. Neurosci. , vol.24 , pp. 1888-1896
    • Lee, H.-J.1    Khoshaghideh, F.2    Patel, S.3    Lee, S.-J.4
  • 29
    • 79960259164 scopus 로고    scopus 로고
    • Enzyme-linked immunosorbent assays for alpha-synuclein with species and multimeric state specificities
    • Lee, H. J. et al. Enzyme-linked immunosorbent assays for alpha-synuclein with species and multimeric state specificities. J. Neurosci. Methods 199, 249-257 (2011).
    • (2011) J. Neurosci. Methods , vol.199 , pp. 249-257
    • Lee, H.J.1
  • 30
    • 0037073747 scopus 로고    scopus 로고
    • Characterization of cytoplasmic alpha-synuclein aggregates. Fibril formation is tightly linked to the inclusion-forming process in cells
    • Lee, H.-J. & Lee, S.-J. Characterization of cytoplasmic alpha-synuclein aggregates. fibril formation is tightly linked to the inclusion-forming process in cells. J. Biol. Chem. 277, 48976-48983 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 48976-48983
    • Lee, H.-J.1    Lee, S.-J.2
  • 31
    • 0036605566 scopus 로고    scopus 로고
    • Differential neuropathological alterations in transgenic mice expressing alpha-synuclein from the platelet-derived growth factor and Thy-1 promoters
    • Rockenstein, E. et al. Differential neuropathological alterations in transgenic mice expressing alpha-synuclein from the platelet-derived growth factor and Thy-1 promoters. J. Neurosci. Res. 68, 568-578 (2002).
    • (2002) J. Neurosci. Res. , vol.68 , pp. 568-578
    • Rockenstein, E.1
  • 32
    • 7044270767 scopus 로고    scopus 로고
    • Early and progressive sensorimotor anomalies in mice overexpressing wild-type human alpha-synuclein
    • Fleming, S. M. et al. Early and progressive sensorimotor anomalies in mice overexpressing wild-type human alpha-synuclein. J. Neurosci. 24, 9434-9440 (2004).
    • (2004) J. Neurosci. , vol.24 , pp. 9434-9440
    • Fleming, S.M.1
  • 33
    • 84866679781 scopus 로고    scopus 로고
    • Antibody-aided clearance of extracellular alpha-synuclein prevents cell-to-cell aggregate transmission
    • Bae, E. J. et al. Antibody-aided clearance of extracellular alpha-synuclein prevents cell-to-cell aggregate transmission. J. Neurosci. 32, 13454-13469 (2012).
    • (2012) J. Neurosci. , vol.32 , pp. 13454-13469
    • Bae, E.J.1
  • 34
    • 79955757052 scopus 로고    scopus 로고
    • Passive immunization reduces behavioral and neuropathological deficits in an alpha-synuclein transgenic model of Lewy body disease
    • Masliah, E. et al. Passive immunization reduces behavioral and neuropathological deficits in an alpha-synuclein transgenic model of Lewy body disease. PLoS ONE 6, e19338 (2011).
    • (2011) PLoS ONE , vol.6
    • Masliah, E.1


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