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Callistephin inhibits amyloid-β protein aggregation and determined cytotoxicity against cerebrovascular smooth muscle cells as an in vitro model of cerebral amyloid angiopathy
- Source :
- Arabian Journal of Chemistry, Vol 15, Iss 2, Pp 103605- (2022)
- Publication Year :
- 2022
- Publisher :
- Elsevier, 2022.
-
Abstract
- It has been indicated that amyloid β (Aβ) plaques can be accumulated within the basement membranes of cerebrovascular smooth muscle cells (CVSMCs) and stimulate the induction of cerebral amyloid angiopathy (CAA). However, the exact mechanism(s) of which small molecules including callistephin mitigate the formation of Aβ aggregation and associated CAA is not well-understood. Therefore, in the present study, Aβ1–42 samples in the aggregation buffer were co-incubated for 36 h without or with of callistephin and the protein aggregation features along with the associated cytotoxicity against CVSMCs as the core components of cerebral arterial wall were explored by different biochemical and cellular methods. Fluorescence (ThT, Nile red) and CD techniques indicated the inhibition of Aβ1–42 fibrillization in the presence of callistephin. Cellular assays revealed that cytotoxicity of Aβ1–42 samples aged in the aggregation buffer with callistephin was much less against CVSMCs than Aβ1–42 amyloid alone through regulation of membrane leakage and downregulation of TNF-α and IL-6 at protein level. In conclusion, these data may provide useful information about the possible mechanisms by which callistephin can show its protective effect against CAA.
- Subjects :
- Amyloid-β
Callistephin
Cerebral amyloid angiopathy
Chemistry
QD1-999
Subjects
Details
- Language :
- English
- ISSN :
- 18785352 and 81130201
- Volume :
- 15
- Issue :
- 2
- Database :
- Directory of Open Access Journals
- Journal :
- Arabian Journal of Chemistry
- Publication Type :
- Academic Journal
- Accession number :
- edsdoj.fe7a8f17932b472d81130201ab25b1c4
- Document Type :
- article
- Full Text :
- https://doi.org/10.1016/j.arabjc.2021.103605