HIF-1α downregulates the APP protein after oxygen and glucose deprivation in the APPswe/PSEN1 mouse model of Alzheimer's disease

The mTORC1 and AMPK signalling pathways are considered key nodes regulating anabolism and catabolism, and they are altered in certain processes of neurodegeneration such as hypoxia associated with ischemic stroke or Alzheimer's disease. The lack of oxygen and/or glucose (oxygen and glucose depr...

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Bibliographic Details
Authors: Villa González, Mario, García Juan, Marta, Ordóñez Gutiérrez, Lara, Pérez Álvarez, María José, Wandosell Jurado, Francisco
Format: article
Publication Date:2025
Country:España
Institution:Universidad Autónoma de Madrid
Repository:Biblos-e Archivo. Repositorio Institucional de la UAM
Language:English
OAI Identifier:oai:dnet:biblosearchi::336fd51b8518990dd75d33d27a89535e
Online Access:https://hdl.handle.net/10486/764841
https://dx.doi.org/10.1016/j.neuint.2024.105923
Access Level:Open access
Keyword:mTORC1
AMPK
autophagy
APP
Amyloid-β
hypoxia
Alzheimer's disease
OGD
Neurodegeneration and neurons
Biología y Biomedicina / Biología
Description
Summary:The mTORC1 and AMPK signalling pathways are considered key nodes regulating anabolism and catabolism, and they are altered in certain processes of neurodegeneration such as hypoxia associated with ischemic stroke or Alzheimer's disease. The lack of oxygen and/or glucose (oxygen and glucose deprivation-OGD) may affect the equilibrium of the mTORC1/AMPK pathways, perhaps aggravating neurodegeneration. The alteration of these pathways mediated by OGD may be reflected in other alterations, such as the activation of autophagy that could in turn modify the secretion/accumulation of amyloid-β, one of the two histopathological markers of Alzheimer's disease. Accordingly, we set out to analyze whether OGD enhances autophagy and its implication in neuronal amyloidosis. The data obtained reveal that OGD significantly dampens not only neuronal amyloid-β production but also, the total APP protein levels, without affecting BACE-1 levels. We show that this mechanism is independent of cellular proteolysis (autophagy or proteasome) and that it can be partially recovered by inhibiting HIF-1α activity