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• W4247279487 abstract "While it is generally understood that processing of APP leads to the production of Aβ of the plaques characteristic of Alzheimer's Disease, questions remain about the regulation of the specific cleavages of APP. We have found that ApoE receptors, a genetic risk factor for AD, have many similarities to APP: they undergo similar patterns of proteolytic processing and share common cytoplasmic adaptor proteins and an extracellular ligand. Recent studies have shown that ApoE receptors, including LRP1 and ApoEr2, interact with NMDA receptors and affect long term potentiation. We examined whether NMDA receptors interact with APP and whether these interactions affect APP processing and Aβ production. We used co–IP's and immunostaining to determine if APP and NMDA receptors interact. We analyzed APP processing by western blot analysis of APP proteolytic fragments. We measured all surface APP by biotinylation and live cell surface staining. We co–transfected COS7 cells with truncated APP constructs and full–length NMDA R1, and found the co–immunoprecipitation requires the APP extracellular domain, including amino acids 200–400 of APP770 (which contains the Kunitz protease inhibitor domain). In other experiments, we found that the PDZ1 domain of PSD95, a postsynaptic scaffolding protein that binds NMDA R2 subunits, interacted with the C–terminus of APP, between amino acids 729 and 751. This interaction between APP and PSD95 was confirmed in primary neurons, and was modulated by NMDA receptor activation (i.e., the addition of NMDA receptor agonist or antagonist). Full–length PSD95 increased production of secreted APP and APP C–terminal fragments in transfected cells. PSD–95 also increased levels of cell surface APP. These data suggest that APP can form a multiprotein complex with NMDA receptor subunits and PSD95. Through these experiments, we hope to determine how molecules that bind to the extracellular domains of APP alter its cleavage and affect Aβ levels. Such information will further our understanding of the genesis of AD and potentially provide insight into the development of therapeutic agents." @default.
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• W4247279487 date "2006-07-01" @default.
• W4247279487 modified "2023-09-27" @default.
• W4247279487 title "P4-063: Modulation of APP processing by NMDA receptors" @default.
• W4247279487 doi "https://doi.org/10.1016/j.jalz.2006.05.1801" @default.
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