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Endogenously generated amyloid-β increases stiffness in human neuroblastoma cells.
European Biophysics Journal : EBJ 2017 July
Amyloid-β (Aβ) is widely recognized as toxic to neuronal cells. Its deposition on plasma and intracellular membranes and aggregation into amyloid plaques can disturb the composition and physiological function of neurons. Whether a physical property of cells, such as stiffness, is altered by endogenously overexpressed Aβ has not yet been investigated. In this study, we used human neuroblastoma cells stably overexpressing amyloid precursor protein (APP) and its Swedish mutant form (APPswe) to measure the changes in cell stiffness. Our results showed that the stiffness of cells overexpressing APP or APPswe was higher than that of control SH-SY5Y cells. Either reducing levels of Aβ with the γ secretase inhibitor DAPT or blocking the membrane calcium channel formed by Aβ with tromethamine decreased cell stiffness to a level close to the control SH-SY5Y cells. Our results suggested that Aβ, not APP, contributed to increased cell stiffness and that closure of calcium channels formed by Aβ can alleviate the effects of Aβ on membrane stiffness.
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