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European Biophysics Journal

, Volume 46, Issue 5, pp 415–424 | Cite as

Endogenously generated amyloid-β increases stiffness in human neuroblastoma cells

  • Zhuoyang Lu
  • Hua Li
  • Chen Hou
  • Yunhua Peng
  • Jiangang LongEmail author
  • Jiankang LiuEmail author
Original Article

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.

Keywords

Alzheimer’s disease Amyloid-β Human neuroblastoma cells Stiffness Atomic force microscopy 

Notes

Acknowledgements

The study was supported by the Major State Basic Research Development Program (2015CB856302, 2015CB553602), the Fundamental Research Funds for the Central Universities (08143101) and the opening foundation of the State Key Laboratory of Space Medicine Fundamentals and Application, Chinese Astronaut Research and Training Center (NO. SMFA15K01).

Compliance with ethical standards

Conflict of interest

The authors declare that they have no conflicts of interest.

Supplementary material

249_2016_1185_MOESM1_ESM.doc (18.7 mb)
Supplementary material 1 (DOC 19119 kb)

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Copyright information

© European Biophysical Societies' Association 2016

Authors and Affiliations

  1. 1.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, FISTXi’an Jiaotong UniversityXi’anChina

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