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- W4380880314 abstract "Abstract Background Amyloid‐β (Aβ) oligomers induce the overproduction of phosphorylated tau and neurodegeneration. These cascades gradually cause cognitive impairment in Alzheimer’s disease (AD). While each pathological event in AD has been studied in detail separately, the spatial and temporal relationships between pathological events in AD remain unclear. We demonstrated that lipid rafts function as a common platform for the pathological cascades of AD. Method Cellular and synaptosomal lipid rafts were prepared from the brains of Aβ amyloid model mice (Tg2576 mice) and double transgenic mice (Tg2576 x TgTauP301L mice) and longitudinally analyzed. Result Aβ oligomers, the cellular prion protein (PrP c ), and Aβ oligomer/PrP c complexes were detected in the lipid rafts. The levels of Fyn, the phosphorylated NR2B subunit of the N‐methyl‐D‐aspartate receptor, glycogen synthase kinase 3β, total tau, phosphorylated tau, and tau oligomers increased with Aβ oligomer accumulation in both the cellular and synaptosomal lipid rafts. Increases in the levels of these molecules were first seen at 6 months of age and corresponded with the early stages of Aβ accumulation in the amyloid model mice. Conclusion Lipid rafts act as a common platform for the progression of Alzheimer’s pathology. The findings of this study suggest a novel therapeutic approach to AD, involving the modification of lipid raft components and the inhibition of their roles in the sequential pathological events of AD." @default.
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- W4380880314 date "2023-06-01" @default.
- W4380880314 modified "2023-09-27" @default.
- W4380880314 title "Lipid rafts act as a common platform for Aβ oligomer‐induced Alzheimer’s pathology" @default.
- W4380880314 doi "https://doi.org/10.1002/alz.061716" @default.
- W4380880314 hasPublicationYear "2023" @default.
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