The presence of cross-β-structure as a key determinant of carbonic anhydrase amyloid fibrils cytotoxicity.
Amyloids
Cross-β-structure
Cytotoxicity
Infrared spectroscopy
carbonic anhydrase
Journal
Biochemical and biophysical research communications
ISSN: 1090-2104
Titre abrégé: Biochem Biophys Res Commun
Pays: United States
ID NLM: 0372516
Informations de publication
Date de publication:
02 04 2020
02 04 2020
Historique:
received:
28
12
2019
accepted:
20
01
2020
pubmed:
3
2
2020
medline:
21
10
2020
entrez:
3
2
2020
Statut:
ppublish
Résumé
In most cases high cytotoxicity is characteristic of aggregates formed during lag phase of amyloid formation, whereas mature fibrils represent the depot of protein molecules incapable of damaging cell membranes. However, new experimental data show that in cases of some proteins the fibrils are the most toxic type of aggregates. Meanwhile, structural characteristics of cytotoxic fibrils and mechanisms of their cell damaging action are insufficiently explored. This work is dedicated to studying amyloid aggregation of bovine carbonic anhydrase (BCA) and effect of aggregates formed at different stages of amyloid formation on viability of the cells. Here we demonstrate that oligomers formed during lag phase do not decrease cell viability, whereas protofibrils and amyloids of BCA are cytotoxic. Obtained results allow concluding that toxicity of BCA aggregates is associated with the presence of amyloid cross-β-structure, which signature is absorbance peak at low wavenumbers at FTIR spectra (1615-1630 cm
Identifiants
pubmed: 32007272
pii: S0006-291X(20)30190-X
doi: 10.1016/j.bbrc.2020.01.113
pii:
doi:
Substances chimiques
Amyloid
0
Protein Aggregates
0
Carbonic Anhydrase II
EC 4.2.1.-
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
453-458Informations de copyright
Copyright © 2020 Elsevier Inc. All rights reserved.