Toxic effects of endoplasmic reticulum stress transducer BBF2H7-derived small peptide fragments on neuronal cells.
Alzheimer’s disease
BBF2H7
Endoplasmic reticulum stress
Journal
Brain research
ISSN: 1872-6240
Titre abrégé: Brain Res
Pays: Netherlands
ID NLM: 0045503
Informations de publication
Date de publication:
15 12 2020
15 12 2020
Historique:
received:
08
06
2020
revised:
10
09
2020
accepted:
26
09
2020
pubmed:
4
10
2020
medline:
28
10
2021
entrez:
3
10
2020
Statut:
ppublish
Résumé
Aggregation, fibril formation, and deposition of amyloid β (Aβ) protein are believed to be the central pathogeneses of Alzheimer's disease (AD). Numerous studies have shown that fibril formation is promoted by preformed seeds at the beginning of the aggregation process. Therefore, aggregated molecules that promote fibrillization of Aβ protein as seeds could affect the pathology. We recently found that approximately 40 amino acid hydrophobic peptides, BBF2H7-derived small peptide (BSP) fragments, are generated via intramembranous cleavage under endoplasmic reticulum (ER) stress conditions. Interestingly, similar to Aβ protein, the fragments exhibit a high aggregation propensity and form fibril structures. It has been noted that ER stress is involved in the pathogenesis of AD. In this study, we examined the effect of BSP fragments on aggregation and cytotoxicity of Aβ
Identifiants
pubmed: 33010207
pii: S0006-8993(20)30497-2
doi: 10.1016/j.brainres.2020.147139
pii:
doi:
Substances chimiques
Amyloid
0
Amyloid beta-Peptides
0
Basic-Leucine Zipper Transcription Factors
0
CREB3L2 protein, human
0
Peptide Fragments
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
147139Informations de copyright
Copyright © 2020 The Author(s). Published by Elsevier B.V. All rights reserved.