메뉴 건너뛰기




Volumn 491, Issue 1, 2011, Pages 48-52

Cerebrospinal fluid from patients with multiple system atrophy promotes in vitro α-synuclein fibril formation

Author keywords

Synuclein fibrils; Cerebrospinal fluid; Lewy body diseases; Multiple system atrophy; Parkinson's disease; Thioflavin S

Indexed keywords

ALPHA SYNUCLEIN; DIRECT YELLOW 7; THIOFLAVINE; UNCLASSIFIED DRUG;

EID: 79951513184     PISSN: 03043940     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.neulet.2011.01.005     Document Type: Article
Times cited : (12)

References (39)
  • 4
    • 0037551741 scopus 로고    scopus 로고
    • Protofibrils, pores, fibrils, and neurodegeneration: separating the responsible protein aggregates from the innocent bystanders
    • Caughey B., Lansbury P.T. Protofibrils, pores, fibrils, and neurodegeneration: separating the responsible protein aggregates from the innocent bystanders. Annu. Rev. Neurosci. 2003, 26:267-298.
    • (2003) Annu. Rev. Neurosci. , vol.26 , pp. 267-298
    • Caughey, B.1    Lansbury, P.T.2
  • 6
    • 0033669319 scopus 로고    scopus 로고
    • In situ and in vitro study of colocalization and segregation of α-synuclein, ubiquitin, and lipids in Lewy bodies
    • Gai W.P., Yuan H.X., Li X.Q., Power J.T., Blumbergs P.C., Jensen P.H. In situ and in vitro study of colocalization and segregation of α-synuclein, ubiquitin, and lipids in Lewy bodies. Exp. Neurol. 2000, 166:324-333.
    • (2000) Exp. Neurol. , vol.166 , pp. 324-333
    • Gai, W.P.1    Yuan, H.X.2    Li, X.Q.3    Power, J.T.4    Blumbergs, P.C.5    Jensen, P.H.6
  • 10
    • 0033771793 scopus 로고    scopus 로고
    • Is there a cause-and-effect relationship between α-synuclein fibrillization and Parkinson's disease?
    • Goldberg M.S., Lansbury P.T. Is there a cause-and-effect relationship between α-synuclein fibrillization and Parkinson's disease?. Nat. Cell Biol. 2000, 2:E115-119.
    • (2000) Nat. Cell Biol. , vol.2
    • Goldberg, M.S.1    Lansbury, P.T.2
  • 11
    • 0031965346 scopus 로고    scopus 로고
    • Increased cerebrospinal fluid levels of neurofilament protein in progressive supranuclear palsy and multiple-system atrophy compared with Parkinson's disease
    • Holmberg B., Rosengren L., Karlsson J.E., Johnels B. Increased cerebrospinal fluid levels of neurofilament protein in progressive supranuclear palsy and multiple-system atrophy compared with Parkinson's disease. Mov. Disord. 1998, 13:70-77.
    • (1998) Mov. Disord. , vol.13 , pp. 70-77
    • Holmberg, B.1    Rosengren, L.2    Karlsson, J.E.3    Johnels, B.4
  • 12
    • 0037295255 scopus 로고    scopus 로고
    • Cerebrospinal fluid Aβ42 is reduced in multiple system atrophy but normal in Parkinson's disease and progressive supranuclear palsy
    • Holmberg B., Johnels B., Blennow K., Rosengren L. Cerebrospinal fluid Aβ42 is reduced in multiple system atrophy but normal in Parkinson's disease and progressive supranuclear palsy. Mov. Disord. 2003, 18:186-190.
    • (2003) Mov. Disord. , vol.18 , pp. 186-190
    • Holmberg, B.1    Johnels, B.2    Blennow, K.3    Rosengren, L.4
  • 13
    • 0026629509 scopus 로고
    • What features improve the accuracy of clinical diagnosis in Parkinson's disease: a clinicopathologic study
    • Hughes A.J., Ben-Shlomo Y., Daniel S.E., Lees A.J. What features improve the accuracy of clinical diagnosis in Parkinson's disease: a clinicopathologic study. Neurology 1992, 42:1142-1146.
    • (1992) Neurology , vol.42 , pp. 1142-1146
    • Hughes, A.J.1    Ben-Shlomo, Y.2    Daniel, S.E.3    Lees, A.J.4
  • 14
    • 0028985267 scopus 로고
    • The precursor protein of non-Aβ component of Alzheimer's disease amyloid is a presynaptic protein of the central nervous system
    • Iwai A., Masliah E., Yoshimoto M., Ge N., Flanagan L., de Silva H.A., Kittel A., Saitoh T. The precursor protein of non-Aβ component of Alzheimer's disease amyloid is a presynaptic protein of the central nervous system. Neuron 1995, 14:467-475.
    • (1995) Neuron , vol.14 , pp. 467-475
    • Iwai, A.1    Masliah, E.2    Yoshimoto, M.3    Ge, N.4    Flanagan, L.5    de Silva, H.A.6    Kittel, A.7    Saitoh, T.8
  • 15
    • 0028277520 scopus 로고
    • Identification of two distinct synucleins from human brain
    • Jakes R., Spillantini M.G., Goedert M. Identification of two distinct synucleins from human brain. FEBS Lett. 1994, 345:27-32.
    • (1994) FEBS Lett. , vol.345 , pp. 27-32
    • Jakes, R.1    Spillantini, M.G.2    Goedert, M.3
  • 16
    • 84941411014 scopus 로고
    • Rapid manual immunoturbidimetric and immunonephelometric assays of prealbumin, albumin, IgG, IgA and IgM in cerebrospinal fluid
    • Kleine T.O., Merten B. Rapid manual immunoturbidimetric and immunonephelometric assays of prealbumin, albumin, IgG, IgA and IgM in cerebrospinal fluid. J. Clin. Chem. Clin. Biochem. 1980, 18:245-254.
    • (1980) J. Clin. Chem. Clin. Biochem. , vol.18 , pp. 245-254
    • Kleine, T.O.1    Merten, B.2
  • 17
    • 21344456506 scopus 로고    scopus 로고
    • Intravesicular localization and exocytosis of α-synuclein and its aggregates
    • Lee H.J., Patel S., Lee S.J. Intravesicular localization and exocytosis of α-synuclein and its aggregates. J. Neurosci. 2005, 25:6016-6024.
    • (2005) J. Neurosci. , vol.25 , pp. 6016-6024
    • Lee, H.J.1    Patel, S.2    Lee, S.J.3
  • 21
    • 0034489853 scopus 로고    scopus 로고
    • Parkinson's disease
    • Alpha-synuclein
    • Lücking C.B., Brice A., Alpha-synuclein Parkinson's disease. Cell. Mol. Life Sci. 2000, 57:1894-1908.
    • (2000) Cell. Mol. Life Sci. , vol.57 , pp. 1894-1908
    • Lücking, C.B.1    Brice, A.2
  • 22
    • 0034491419 scopus 로고    scopus 로고
    • Protein determination in cerebrospinal fluid by protein dye-binding assay
    • Marshall T., Williams K.M. Protein determination in cerebrospinal fluid by protein dye-binding assay. Br. J. Biomed. Sci. 2000, 57:281-286.
    • (2000) Br. J. Biomed. Sci. , vol.57 , pp. 281-286
    • Marshall, T.1    Williams, K.M.2
  • 26
    • 33846455859 scopus 로고    scopus 로고
    • Cerebrospinal fluid of Alzheimer's disease and dementia with Lewy bodies patients enhances α-synuclein fibril formation in vitro
    • Ono K., Noguchi-Shinohara M., Yoshita M., Naiki H., Yamada M. Cerebrospinal fluid of Alzheimer's disease and dementia with Lewy bodies patients enhances α-synuclein fibril formation in vitro. Exp. Neurol. 2007, 203:579-583.
    • (2007) Exp. Neurol. , vol.203 , pp. 579-583
    • Ono, K.1    Noguchi-Shinohara, M.2    Yoshita, M.3    Naiki, H.4    Yamada, M.5
  • 27
    • 59649087536 scopus 로고    scopus 로고
    • α-Synuclein assembly as a therapeutic target of Parkinson's disease and related disorders
    • Ono K., Hirohata M., Yamada M. α-Synuclein assembly as a therapeutic target of Parkinson's disease and related disorders. Curr. Pharm. Des. 2008, 14:3247-3266.
    • (2008) Curr. Pharm. Des. , vol.14 , pp. 3247-3266
    • Ono, K.1    Hirohata, M.2    Yamada, M.3
  • 28
    • 77954927651 scopus 로고    scopus 로고
    • Effects of the english (H6R) and tottori (D7N) familial Alzheimer disease mutations on amyloid β-protein assembly and toxicity
    • Ono K., Condron M.M., Teplow D.B. Effects of the english (H6R) and tottori (D7N) familial Alzheimer disease mutations on amyloid β-protein assembly and toxicity. J. Biol. Chem. 2010, 285:23186-23197.
    • (2010) J. Biol. Chem. , vol.285 , pp. 23186-23197
    • Ono, K.1    Condron, M.M.2    Teplow, D.B.3
  • 29
    • 65249162241 scopus 로고    scopus 로고
    • Detection of elevated levels of soluble α-synuclein oligomers in post-mortem brain extracts from patients with dementia with Lewy bodies
    • Paleologou K.E., Kragh C.L., Mann D.M., Salem S.A., Al-Shami R., Allsop D., Hassan A.H., Jensen P.H., El-Agnaf O.M. Detection of elevated levels of soluble α-synuclein oligomers in post-mortem brain extracts from patients with dementia with Lewy bodies. Brain 2009, 132:1093-1101.
    • (2009) Brain , vol.132 , pp. 1093-1101
    • Paleologou, K.E.1    Kragh, C.L.2    Mann, D.M.3    Salem, S.A.4    Al-Shami, R.5    Allsop, D.6    Hassan, A.H.7    Jensen, P.H.8    El-Agnaf, O.M.9
  • 30
    • 57449091884 scopus 로고    scopus 로고
    • Molecular structural basis for polymorphism in Alzheimer's β-amyloid fibrils
    • Paravastu A.K., Leapman R.D., Yau W.M., Tycko R. Molecular structural basis for polymorphism in Alzheimer's β-amyloid fibrils. Proc. Natl. Acad. Sci. U.S.A. 2008, 105:18349-18354.
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 18349-18354
    • Paravastu, A.K.1    Leapman, R.D.2    Yau, W.M.3    Tycko, R.4
  • 32
    • 30744433878 scopus 로고    scopus 로고
    • Experimental constraints on quaternary structure in Alzheimer's β-amyloid fibrils
    • Petkova A.T., Yau W.M., Tycko R. Experimental constraints on quaternary structure in Alzheimer's β-amyloid fibrils. Biochemistry 2006, 45:498-512.
    • (2006) Biochemistry , vol.45 , pp. 498-512
    • Petkova, A.T.1    Yau, W.M.2    Tycko, R.3
  • 33
    • 0036970672 scopus 로고    scopus 로고
    • Deferoxamine attenuates iron-induced oxidative stress and prevents mitochondrial aggregation and α-synuclein translocation in SK-N-SH cells in culture
    • Sangchot P., Sharma S., Chetsawang B., Porter J., Govitrapong P., Ebadi M. Deferoxamine attenuates iron-induced oxidative stress and prevents mitochondrial aggregation and α-synuclein translocation in SK-N-SH cells in culture. Dev. Neurosci. 2002, 24:143-153.
    • (2002) Dev. Neurosci. , vol.24 , pp. 143-153
    • Sangchot, P.1    Sharma, S.2    Chetsawang, B.3    Porter, J.4    Govitrapong, P.5    Ebadi, M.6
  • 35
    • 0035941201 scopus 로고    scopus 로고
    • Metal-triggered structural transformations, aggregation, and fibrillation of human α-synuclein. A possible molecular NK between Parkinson's disease and heavy metal exposure
    • Uversky V.N., Li J., Fink A.L. Metal-triggered structural transformations, aggregation, and fibrillation of human α-synuclein. A possible molecular NK between Parkinson's disease and heavy metal exposure. J. Biol. Chem. 2001, 276:44284-44296.
    • (2001) J. Biol. Chem. , vol.276 , pp. 44284-44296
    • Uversky, V.N.1    Li, J.2    Fink, A.L.3
  • 36
    • 0027930620 scopus 로고
    • Clinical features and natural history of multiple system atrophy. An analysis of 100 cases
    • Wenning G.K., Ben Shlomo Y., Magalhães M., Daniel S.E., Quinn N.P. Clinical features and natural history of multiple system atrophy. An analysis of 100 cases. Brain 1994, 117:835-845.
    • (1994) Brain , vol.117 , pp. 835-845
    • Wenning, G.K.1    Ben Shlomo, Y.2    Magalhães, M.3    Daniel, S.E.4    Quinn, N.P.5
  • 37
    • 0033538541 scopus 로고    scopus 로고
    • α-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. α-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
  • 38
    • 65549150887 scopus 로고    scopus 로고
    • Conversion of wild-type α-synuclein into mutant-type fibrils and its propagation in the presence of A30P mutant
    • Yonetani M., Nonaka T., Masuda M., Inukai Y., Oikawa T., Hisanaga S., Hasegawa M. Conversion of wild-type α-synuclein into mutant-type fibrils and its propagation in the presence of A30P mutant. J. Biol. Chem. 2009, 284:7940-7950.
    • (2009) J. Biol. Chem. , vol.284 , pp. 7940-7950
    • Yonetani, M.1    Nonaka, T.2    Masuda, M.3    Inukai, Y.4    Oikawa, T.5    Hisanaga, S.6    Hasegawa, M.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.