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• W2050409712 abstract "Two recent reports showed that amyloid precursor protein (APP) may contribute to postsynaptic mechanisms via the regulation of the surface trafficking of excitatory N-methyl-d-aspartate (NMDA) receptors. Here we have investigated the interactions and surface trafficking of NR1-1a/NR2A and NR1-1a/NR2B NMDA receptor subtypes with three APP mutations linked to familial Alzheimer's disease, APP695Indiana, APP695London and APP695Swedish. Flag-tagged mutated APP695s were generated and shown to be expressed at equivalent levels to wild-type APP695 in mammalian cells. Each APP mutant co-precipitated with NR1-1a/NR2A and NR1-1a/NR2B receptors following co-expression in mammalian cells. Further, as found for wild-type APP695, each enhanced NMDA receptor surface expression with no concomitant increase in total NR1-1a, NR2A or NR2B subunit expression. Thus these three familial APP mutations behave as wild-type APP695 with respect to their association with assembled NMDA receptors and their APP695-enhanced receptor cell surface trafficking." @default.
• W2050409712 created "2016-06-24" @default.
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• W2050409712 date "2012-05-01" @default.
• W2050409712 modified "2023-10-06" @default.
• W2050409712 title "NMDA receptor/amyloid precursor protein interactions: A comparison between wild-type and amyloid precursor protein mutations associated with familial Alzheimer's disease" @default.
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• W2050409712 doi "https://doi.org/10.1016/j.neulet.2012.03.029" @default.
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