The amyloid precursor protein: a converging point in Alzheimer's disease.
Alzheimer’s disease
Amyloid precursor protein
C-terminal fragment β (CTFβ)
C31 peptide
Posiphen
Journal
Molecular neurobiology
ISSN: 1559-1182
Titre abrégé: Mol Neurobiol
Pays: United States
ID NLM: 8900963
Informations de publication
Date de publication:
Jul 2022
Jul 2022
Historique:
received:
25
04
2021
accepted:
30
04
2022
pubmed:
18
5
2022
medline:
9
6
2022
entrez:
17
5
2022
Statut:
ppublish
Résumé
The decades of evidence that showcase the role of amyloid precursor protein (APP), and its fragment amyloidβ (Aβ), in Alzheimer's disease (AD) pathogenesis are irrefutable. However, the absolute focus on the single APP metabolite Aβ as the cause for AD has resulted in APP and its other fragments that possess toxic propensity, to be overlooked as targets for treatment. The complexity of its processing and its association with systematic metabolism suggests that, if misregulated, APP has the potential to provoke an array of metabolic dysfunctions. This review discusses APP and several of its cleaved products with a particular focus on their toxicity and ability to disrupt healthy cellular function, in relation to AD development. We subsequently argue that the reduction of APP, which would result in a concurrent decrease in Aβ as well as all other toxic APP metabolites, would alleviate the toxic environment associated with AD and slow disease progression. A discussion of those drug-like compounds already identified to possess this capacity is also included.
Identifiants
pubmed: 35579846
doi: 10.1007/s12035-022-02863-x
pii: 10.1007/s12035-022-02863-x
doi:
Substances chimiques
Amyloid beta-Peptides
0
Amyloid beta-Protein Precursor
0
Amyloid Precursor Protein Secretases
EC 3.4.-
Types de publication
Journal Article
Review
Langues
eng
Sous-ensembles de citation
IM
Pagination
4501-4516Subventions
Organisme : National Research Foundation
ID : 141924
Organisme : National Research Foundation
ID : 142719
Informations de copyright
© 2022. The Author(s), under exclusive licence to Springer Science+Business Media, LLC, part of Springer Nature.
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