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|dc.identifier.citation||Experimental Neurology, 2000; 166(2):324-333||en|
|dc.description.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.||en|
|dc.description.statementofresponsibility||W.P. Gai, H.X. Yuan, X.Q. Li, J.T.H. Power, P.C. Blumbergs, P.H. Jensen||en|
|dc.publisher||Academic Press Inc Elsevier Science||en|
|dc.subject||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||en|
|dc.title||In situ and in vitro study of colocalization and segregation of a-Synuclein, ubiquitin, and lipids in Lewy bodies||en|
|Appears in Collections:||Pathology publications|
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