Please use this identifier to cite or link to this item: http://hdl.handle.net/2440/5624
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Type: Journal article
Title: In situ and in vitro study of colocalization and segregation of a-Synuclein, ubiquitin, and lipids in Lewy bodies
Author: Gai, W.
Yaun, H.
Li, Q.
Power, J.
Blumbergs, P.
Jensen, P.
Citation: Experimental Neurology, 2000; 166(2):324-333
Publisher: Academic Press Inc Elsevier Science
Issue Date: 2000
ISSN: 0014-4886
1090-2430
Statement of
Responsibility: 
W.P. Gai, H.X. Yuan, X.Q. Li, J.T.H. Power, P.C. Blumbergs, P.H. Jensen
Abstract: alpha-Synuclein and ubiquitin are two Lewy body protein components that may play antagonistic roles in the pathogenesis of Lewy bodies. We examined the relationship between alpha-synuclein, ubiquitin, and lipids in Lewy bodies of fixed brain sections or isolated from cortical tissues of dementia with Lewy bodies. Lewy bodies exhibited a range of labeling patterns for alpha-synuclein and ubiquitin, from a homogeneous pattern in which alpha-synuclein and ubiquitin were evenly distributed and overlapped across the inclusion body to a concentric pattern in which alpha-synuclein and ubiquitin were partially segregated, with alpha-synuclein labeling concentrated in the peripheral domain and ubiquitin in the central domain of the Lewy body. Lipids represented a significant component in both homogeneous and concentric Lewy bodies. These results suggest that Lewy bodies are heterogeneous in their subregional composition. The segregation of alpha-synuclein to Lewy body peripheral domain is consistent with the hypothesis that alpha-synuclein is continually deposited onto Lewy bodies.
Keywords: Brain; Neurons; Lewy Bodies; Humans; Lewy Body Disease; Parkinson Disease; Lipids; Nerve Tissue Proteins; Ubiquitins; Microscopy, Immunoelectron; Brain Chemistry; Aged; Aged, 80 and over; Middle Aged; Female; Male; Synucleins; alpha-Synuclein
RMID: 0001000924
DOI: 10.1006/exnr.2000.7527
Appears in Collections:Pathology publications

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