title: Endogenously generated amyloid-β increases stiffness in human neuroblastoma cells.
abstract: 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.
authors.affiliation: The Key Laboratory of Biomedical Information Engineering of the Ministry of Education, Center for Mitochondrial Biology and Medicine, School of Life Science and Technology and Frontier Institute of Life Science, FIST, Xi'an Jiaotong University, 710049, Xi'an, China.
authors.forename: Zhuoyang
authors.initials: Z
authors.lastname: Lu
authors.affiliation: The Key Laboratory of Biomedical Information Engineering of the Ministry of Education, Center for Mitochondrial Biology and Medicine, School of Life Science and Technology and Frontier Institute of Life Science, FIST, Xi'an Jiaotong University, 710049, Xi'an, China.
authors.forename: Hua
authors.initials: H
authors.lastname: Li
authors.affiliation: The Key Laboratory of Biomedical Information Engineering of the Ministry of Education, Center for Mitochondrial Biology and Medicine, School of Life Science and Technology and Frontier Institute of Life Science, FIST, Xi'an Jiaotong University, 710049, Xi'an, China.
authors.forename: Chen
authors.initials: C
authors.lastname: Hou
authors.affiliation: The Key Laboratory of Biomedical Information Engineering of the Ministry of Education, Center for Mitochondrial Biology and Medicine, School of Life Science and Technology and Frontier Institute of Life Science, FIST, Xi'an Jiaotong University, 710049, Xi'an, China.
authors.forename: Yunhua
authors.initials: Y
authors.lastname: Peng
authors.affiliation: The Key Laboratory of Biomedical Information Engineering of the Ministry of Education, Center for Mitochondrial Biology and Medicine, School of Life Science and Technology and Frontier Institute of Life Science, FIST, Xi'an Jiaotong University, 710049, Xi'an, China. jglong@mail.xjtu.edu.cn.
authors.forename: Jiangang
authors.initials: J
authors.lastname: Long
authors.affiliation: The Key Laboratory of Biomedical Information Engineering of the Ministry of Education, Center for Mitochondrial Biology and Medicine, School of Life Science and Technology and Frontier Institute of Life Science, FIST, Xi'an Jiaotong University, 710049, Xi'an, China. j.liu@mail.xjtu.edu.cn.
authors.forename: Jiankang
authors.initials: J
authors.lastname: Liu
mesh_terms: D016229:Amyloid beta-Peptides / Q000378:metabolism*; D001696:Biomechanical Phenomena; D045744:Cell Line, Tumor; D006801:Humans; D055595:Mechanical Phenomena; D009447:Neuroblastoma / Q000473:pathology*; D010446:Peptide Fragments / Q000378:metabolism*
chemical_list: D016229:Amyloid beta-Peptides; D010446:Peptide Fragments; C078592:amyloid beta-protein (1-40)
keywords: Alzheimer’s disease; Amyloid-β; Atomic force microscopy; Human neuroblastoma cells; Stiffness