Amyloid protein-induced sequestration of the eukaryotic ribosome: effect of stoichiometry and polyphenolic inhibitors.
FEBS Lett
; 596(9): 1190-1202, 2022 05.
Article
em En
| MEDLINE
| ID: mdl-35114013
ABSTRACT
Alzheimer's disease (AD) is characterized by the appearance of neurofibrillary tangles comprising of the Tau protein and aggregation of amyloid-ß peptides (Aß 1-40 and Aß 1-42). A concomitant loss of the ribosomal population is also observed in AD-affected neurons. Our studies demonstrate that, similarly to Tau protein aggregation, in vitro aggregation of Aß peptides in the vicinity of the yeast 80S ribosome can induce co-aggregation of ribosomal components. The RNA-stimulated aggregation of Aß peptides and the Tau-K18 variant is dependent on the RNAprotein stoichiometric ratio. A similar effect of stoichiometry is also observed on the ribosome-protein co-aggregation process. Polyphenolic inhibitors of amyloid aggregation, such as rosmarinic acid and myricetin, inhibit RNA-stimulated Aß and Tau-K18 aggregation and can mitigate the co-aggregation of ribosomal components.
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Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Saccharomyces cerevisiae
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Peptídeos beta-Amiloides
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Proteínas tau
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Proteínas Amiloidogênicas
Limite:
Humans
Idioma:
En
Ano de publicação:
2022
Tipo de documento:
Article