Mechanisms of Amyloid-Beta Peptide Uptake by Neurons: The Role of Lipid Rafts and Lipid Raft-Associated ProteinsReport as inadecuate

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International Journal of Alzheimer-s DiseaseVolume 2011 2011, Article ID 548380, 11 pages

Review Article

Tanz Centre for Research in Neurodegenerative Diseases, University of Toronto, 6 Queen-s Park Crescent West, Toronto, ON, Canada M5S 3H2

Department of Laboratory Medicine and Pathobiology, University of Toronto, Toronto, ON, Canada M5S 3H2

Received 15 October 2010; Accepted 29 November 2010

Academic Editor: Anne Eckert

Copyright © 2011 Aaron Y. Lai and JoAnne McLaurin. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.


A hallmark pathological feature of Alzheimer-s disease AD is the accumulation of extracellular plaques composed of the amyloid-beta Aβ peptide. Thus, classically experiments were designed to examine Aβ toxicities within the central nervous system CNS from the extracellular space. However, a significant amount of evidence now suggests that intraneuronal accumulation of Aβ is neurotoxic and may play an important role in the disease progression of AD. One of the means by which neurons accumulate intracellular Aβ is through uptake of extracellular Aβ peptides, and this process may be a potential link between Aβ generation, synaptic dysfunction, and AD pathology. Recent studies have found that neuronal internalization of Aβ involves lipid rafts and various lipid raft-associated receptor proteins. Uptake mechanisms independent of lipid rafts have also been implicated. The aim of this paper is to summarize these findings and discuss their significance in the pathogenesis of AD.

Author: Aaron Y. Lai and JoAnne McLaurin



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