Callistephin inhibits amyloid-β protein aggregation and determined cytotoxicity against cerebrovascular smooth muscle cells as an in vitro model of cerebral amyloid angiopathy |
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Affiliation: | 1. Department of Neurology, Baodi Clinical College of Tianjin Medical University, Tianjin 301800, China;2. Department of Neurology, The First Hospital of Xi’an, Xi’an 710002, China;3. Department of Neurology, Xianyang Hospital of Yan''an University, Xianyang 712000, China;4. Department of Vascular Surgery, the First Affiliated Hospital of Dalian Medical University, Dalian 116021, China |
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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. |
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Keywords: | Amyloid-β Callistephin Cerebral amyloid angiopathy |
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