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    Membrane-bound beta-amyloid oligomers are recruited into lipid rafts by a fyn-dependent mechanism

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    Publication date
    2008
    Author
    Williamson, Ritchie
    Usardi, A.
    Hanger, D.P.
    Anderton, B.H.
    Keyword
    Amyloid beta-Peptides; Metabolism
    Animals
    Cerebral Cortex; Cytology
    Hippocampus
    Ligands
    Membrane Microdomains
    Mice
    Peptide Fragments
    Proto-Oncogene Proteins c-fyn; Physiology
    Rats
    REF 2014
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    Abstract
    Recently published research indicates that soluble oligomers of beta-amyloid (Abeta) may be the key neurotoxic species associated with the progression of Alzheimer's disease (AD) and that the process of Abeta aggregation may drive this event. Furthermore, soluble oligomers of Abeta and tau accumulate in the lipid rafts of brains from AD patients through an as yet unknown mechanism. Using cell culture models we report a novel action of Abeta on neuronal plasma membranes where exogenously applied Abeta in the form of ADDLs can be trafficked on the neuronal membrane and accumulate in lipid rafts. ADDL-induced dynamic alterations in lipid raft protein composition were found to facilitate this movement. We show clear associations between Abeta accumulation and redistribution on the neuronal membrane and alterations in the protein composition of lipid rafts. In addition, our data from fyn(-/-) transgenic mice show that accumulation of Abeta on the neuronal surface was not sufficient to cause cell death but that fyn is required for both the redistribution of Abeta and subsequent cell death. These results identify fyn-dependent Abeta redistribution and accumulation in lipid rafts as being key to ADDL-induced cell death and defines a mechanism by which oligomers of Abeta and tau accumulate in lipid rafts.
    URI
    http://hdl.handle.net/10454/6237
    Citation
    Williamson, R., Usardi, A., Hanger, D. P., Anderton, B. H. (2008) Membrane-bound beta-amyloid oligomers are recruited into lipid rafts by a fyn-dependent mechanism. FASEB Journal, 22 (5), 1552-9.
    Link to publisher’s version
    http://dx.doi.org/10.1096/fj.07-9766com
    Type
    Article
    Collections
    Life Sciences Publications

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