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https://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 In Vitro Techniques |
DOI: | 10.1006/exnr.2000.7527 |
Published version: | http://dx.doi.org/10.1006/exnr.2000.7527 |
Appears in Collections: | Aurora harvest Pathology publications |
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