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|Title:||In situ and in vitro study of colocalization and segregation of a-Synuclein, ubiquitin, and lipids in Lewy bodies|
|Citation:||Experimental Neurology, 2000; 166(2):324-333|
|Publisher:||Academic Press Inc Elsevier Science|
|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.|
Lewy Body Disease
Nerve Tissue Proteins
Aged, 80 and over
In Vitro Techniques
|Appears in Collections:||Aurora harvest|
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