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West, Ewan; Osborne, Craig; Nolan, William; Bate, Clive (2015)
Publisher: Multidisciplinary Digital Publishing Institute
Journal: Biology
Languages: English
Types: Article
Subjects: synaptophysin, amyloid-?, amyloid-β, Alzheimer?s disease, Article, QH301-705.5, Alzheimer’s disease, synapses, glycosylphosphatidylinositols, prion, Biology (General)

Classified by OpenAIRE into

mesheuropmc: nervous system diseases, animal diseases, mental disorders
Alzheimer?s disease (AD) is a progressive neurodegenerative disease characterized by the accumulation of amyloid-? (A?) and the loss of synapses. Aggregation of the cellular prion protein (PrPC) by A? oligomers induced synapse damage in cultured neurons. PrPC is attached to membranes via a glycosylphosphatidylinositol (GPI) anchor, the composition of which affects protein targeting and cell signaling. Monoacylated PrPC incorporated into neurons bound ?natural A??, sequestering A? outside lipid rafts and preventing its accumulation at synapses. The presence of monoacylated PrPC reduced the A?-induced activation of cytoplasmic phospholipase A2 (cPLA2) and A?-induced synapse damage. This protective effect was stimulus specific, as treated neurons remained sensitive to ?-synuclein, a protein associated with synapse damage in Parkinson?s disease. In synaptosomes, the aggregation of PrPC by A? oligomers triggered the formation of a signaling complex containing the cPLA2.a process, disrupted by monoacylated PrPC. We propose that monoacylated PrPC acts as a molecular sponge, binding A? oligomers at the neuronal perikarya without activating cPLA2 or triggering synapse damage.