Author(s): JaroszGriffiths HH, Noble E, Rushworth JV, Hooper NM
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Abstract Several different receptor proteins have been identified that bind monomeric, oligomeric, or fibrillar forms of amyloid-β (Aβ). "Good" receptors internalize Aβ or promote its transcytosis out of the brain, whereas "bad" receptors bind oligomeric forms of Aβ that are largely responsible for the synapticloss, memory impairments, and neurotoxicity that underlie Alzheimer disease. The prion protein both removes Aβ from the brain and transduces the toxic actions of Aβ. The clustering of distinct receptors in cell surface signaling platforms likely underlies the actions of distinct oligomeric species of Aβ. These Aβ receptor-signaling platforms provide opportunities for therapeutic intervention in Alzheimer disease. © 2016 by The American Society for Biochemistry and Molecular Biology, Inc.
This article was published in J Biol Chem
and referenced in Journal of Biomolecular Research & Therapeutics