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Endocytic pathways mediating oligomeric Aβ42 neurotoxicity

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Title: Endocytic pathways mediating oligomeric Aβ42 neurotoxicity
Author(s): Yu, Chunjiang; Health, Evelyn; Laxton, Kevin; LaDu, Mary Jo
Subject(s): amyloid-beta-protein down-syndrome
Abstract: Background One pathological hallmark of Alzheimer’s disease (AD) is amyloid plaques, composed primarily of amyloid-β peptide (Aβ). Over-production or diminished clearance of the 42 amino acid form of Aβ (Aβ42) in the brain leads to accumulation of soluble Aβ and plaque formation. Soluble oligomeric Aβ (oAβ) has recently emerged to be as a likely proximal cause of AD. Results Here we demonstrate that endocytosis is critical in mediating oAβ42-induced neurotoxicity and intraneuronal accumulation of Aβ. Inhibition of clathrin function either with a pharmacological inhibitor, knock-down of clathrin heavy chain expression, or expression of the dominant-negative mutant of clathrin-assembly protein AP180 did not block oAβ42-induced neurotoxicity or intraneuronal accumulation of Aβ. However, inhibition of dynamin and RhoA by expression of dominant negative mutants, reduced neurotoxicity and intraneuronal Aβaccumulation. Pharmacologic inhibition of the dynamin-mediated endocytic pathway by genistein also reduced neurotoxicity. Conclusions These data suggest that dynamin-mediated and RhoA-regulated endocytosis are integral steps for oligomeric Aβ42-induced neurotoxicity and intraneuronal Aβ accumulation.
Issue Date: 2010-05-17
Publisher: BioMed Central
Citation Info: Yu, C. J., Nwabuisi-Heath, E., Laxton, K., & Ladu, M. J. 2010. Endocytic pathways mediating oligomeric A beta 42 neurotoxicity. Molecular Neurodegeneration, 5. DOI: 10.1186/1750-1326-5-19
Type: Article
Description: The original version is available through BioMed Central at DOI: 10.1186/1750-1326-5-19. © 2010 Yu et al; licensee BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
ISSN: 1750-1326
Sponsor: This work was supported by grants from the Alzheimer’s Association NIRG-06-26957 (CY); and ZEN-08-899000 and NIH/NIA PO1AG021184 (MJL).
Date Available in INDIGO: 2011-05-25

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