AA amyloid fibrils from diseased tissue are structurally different from in vitro formed SAA fibrils.
Journal
Nature communications
ISSN: 2041-1723
Titre abrégé: Nat Commun
Pays: England
ID NLM: 101528555
Informations de publication
Date de publication:
12 02 2021
12 02 2021
Historique:
received:
04
09
2020
accepted:
07
01
2021
entrez:
13
2
2021
pubmed:
14
2
2021
medline:
3
3
2021
Statut:
epublish
Résumé
Systemic AA amyloidosis is a world-wide occurring protein misfolding disease of humans and animals. It arises from the formation of amyloid fibrils from serum amyloid A (SAA) protein. Using cryo electron microscopy we here show that amyloid fibrils which were purified from AA amyloidotic mice are structurally different from fibrils formed from recombinant SAA protein in vitro. Ex vivo amyloid fibrils consist of fibril proteins that contain more residues within their ordered parts and possess a higher β-sheet content than in vitro fibril proteins. They are also more resistant to proteolysis than their in vitro formed counterparts. These data suggest that pathogenic amyloid fibrils may originate from proteolytic selection, allowing specific fibril morphologies to proliferate and to cause damage to the surrounding tissue.
Identifiants
pubmed: 33579941
doi: 10.1038/s41467-021-21129-z
pii: 10.1038/s41467-021-21129-z
pmc: PMC7881110
doi:
Substances chimiques
Amyloid
0
Recombinant Proteins
0
Serum Amyloid A Protein
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
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