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Soluble amyloid-β (Aβ) oligomers, a key driver of pathogenesis in Alzheimer disease, bind to cellular prion proteins (PrP C ) expressed on synaptosomes resulting in increased cholesterol concentrations, movement of cytoplasmic phospholipase A 2  (cPLA 2 ) to lipid rafts and activation of cPLA 2 . The formation of Aβ-PrP C -cPLA 2  complexes was controlled by the cholesterol ester cycle. Thus, Aβ activated cholesterol ester hydrolases which released cholesterol from stores of cholesterol esters; the increased cholesterol concentrations stabilised Aβ-PrP C -cPLA 2  complexes. Conversely, cholesterol esterification reduced cholesterol concentrations causing the dispersal of Aβ-PrP C -cPLA 2 . In cultured neurons, the cholesterol ester cycle regulated Aβ-induced synapse damage; inhibition of cholesterol ester hydrolases protected neurons, whereas inhibition of cholesterol esterification increased the Aβ-induced synapse damage. Here, I speculate that a failure to deactivate signalling pathways can lead to pathology. Consequently, the esterification of cholesterol is a key factor in the dispersal of Aβ-induced signalling platforms and synapse degeneration.

Breaking the Cycle, Cholesterol Cycling, and Synapse Damage in Response to Amyloid-β