The polyphenol EGCG directly targets intracellular amyloid-β aggregates and promotes their lysosomal degradation.
Alzheimer's disease
EGCG derivatives
amyloid-β
cathepsin
epigallocatechin gallate
lysosome
Journal
Journal of neurochemistry
ISSN: 1471-4159
Titre abrégé: J Neurochem
Pays: England
ID NLM: 2985190R
Informations de publication
Date de publication:
07 2023
07 2023
Historique:
revised:
02
04
2023
received:
01
03
2023
accepted:
25
04
2023
medline:
19
7
2023
pubmed:
11
5
2023
entrez:
11
5
2023
Statut:
ppublish
Résumé
The accumulation of amyloidogenic protein aggregates in neurons is a pathogenic hallmark of a large number of neurodegenerative diseases including Alzheimer's disease (AD). Small molecules targeting such structures and promoting their degradation may have therapeutic potential for the treatment of AD. Here, we searched for natural chemical compounds that decrease the abundance of stable, proteotoxic β-sheet-rich amyloid-β (Aβ) aggregates in cells. We found that the polyphenol (-)-epigallocatechin gallate (EGCG) functions as a potent chemical aggregate degrader in SH-EP cells. We further demonstrate that a novel, fluorescently labeled EGCG derivative (EGC-dihydroxybenzoate (DHB)-Rhodamine) also shows cellular activity. It directly targets intracellular Aβ42 aggregates and competes with EGCG for Aβ42 aggregate binding in vitro. Mechanistic investigations indicated a lysosomal accumulation of Aβ42 aggregates in SH-EP cells and showed that lysosomal cathepsin activity is critical for efficient EGCG-mediated aggregate clearance. In fact, EGCG treatment leads to an increased abundance of active cathepsin B isoforms and increased enzymatic activity in our SH-EP cell model. Our findings suggest that intracellular Aβ42 aggregates are cleared through the endo-lysosomal system. We show that EGCG directly targets intracellular Aβ42 aggregates and facilitates their lysosomal degradation. Small molecules, which bind to protein aggregates and increase their lysosomal degradation could have therapeutic potential for the treatment of amyloid diseases.
Substances chimiques
epigallocatechin gallate
BQM438CTEL
Amyloid beta-Peptides
0
Catechin
8R1V1STN48
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
294-317Informations de copyright
© 2023 The Authors. Journal of Neurochemistry published by John Wiley & Sons Ltd on behalf of International Society for Neurochemistry.
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