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- W2744012760 abstract "Amyloidogenic processing of APP by β- and γ-secretases leads to the generation of amyloid-β peptide (Aβ), and the accumulation of Aβ in senile plaques is a hallmark of Alzheimer's disease (AD). Understanding the mechanisms of APP processing is therefore paramount. Increasing evidence suggests that APP intracellular domain (AICD) interacting proteins influence APP processing. In this study, we characterized the overexpression of AICD interactor GULP1 in a Drosophila AD model expressing human BACE and APP695. Transgenic GULP1 significantly lowered the levels of both Aβ1-40 and Aβ1-42 without decreasing the BACE and APP695 levels. Overexpression of GULP1 also reduced APP/BACE-mediated retinal degeneration, rescued motor dysfunction and extended longevity of the flies. Our results indicate that GULP1 regulate APP processing and reduce neurotoxicity in a Drosophila AD model." @default.
- W2744012760 created "2017-08-17" @default.
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- W2744012760 date "2017-08-08" @default.
- W2744012760 modified "2023-10-14" @default.
- W2744012760 title "GULP1/CED-6 ameliorates amyloid-β toxicity in a Drosophila model of Alzheimer’s disease" @default.
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- W2744012760 doi "https://doi.org/10.18632/oncotarget.20062" @default.
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