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Amyloid β aggregation induces human brain microvascular endothelial cell death with abnormal actin organization.

Authors:
Yushiro Take Yusaku Chikai Keiya Shimamori Masahiro Kuragano Hiroki Kurita Kiyotaka Tokuraku

Biochem Biophys Rep 2022 Mar 15;29:101189. Epub 2021 Dec 15.

Graduate School of Engineering, Muroran Institute of Technology, Hokkaido, 050-8585, Japan.

Cerebral amyloid angiopathy (CAA) is a disease in which amyloid β (Aβ) is deposited on the walls of blood vessels in the brain, making those walls brittle and causing cerebral hemorrhage. However, the mechanism underlying its onset is not well understood. The aggregation and accumulation of Aβ cause the occlusion and fragility of blood vessels due to endothelial cell damage, breakdown of the blood-brain barrier, and replacement with elements constituting the blood vessel wall. In this study, we observed the effect of Aβ on human primary brain microvascular endothelial cells (hBMECs) in real-time using quantum dot nanoprobes to elucidate the mechanism of vascular weakening by Aβ. It was observed that Aβ began to aggregate around hBMECs after the start of incubation and that the cells were covered with aggregates. Aβ aggregates firmly anchored the cells on the plate surface, and eventually suppressed cell motility and caused cell death. Furthermore, Aβ aggregation induced the organization of abnormal actin, resulting in a significant increase in intracellular actin dots over 10 μm. These results suggest that the mechanism by which Aβ forms a fragile vessel wall is as follows: Aβ aggregation around vascular endothelial cells anchors them to the substrate, induces abnormal actin organization, and leads to cell death.

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http://dx.doi.org/10.1016/j.bbrep.2021.101189DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC8685982PMC
March 2022

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