TY - JOUR
T1 - Biophysical Characteristics of Human Neuroblastoma Cell in Oligomeric β-Amyloid (1-40) Cytotoxicity
AU - Gao, Qi
AU - Fang, Yuqiang
AU - ZHANG, Shiqing
AU - LI, Hung Wing
AU - YUNG, Kin Lam
AU - Lai, King Wai Chiu
N1 - Funding Information:
Manuscript received June 8, 2017; revised September 24, 2017, December 22, 2017, and January 22, 2018; accepted January 24, 2018. Date of publication February 1, 2018; date of current version March 20, 2018. This work was supported in part by the Research Grant Council of the Hong Kong Special Administrative Region Government under Grant CityU139313, Grant CityU11205815, and Grant CityU11205514, and in part by HKBU under Grant RC-IRMS/14-15/05. (Corresponding author: King Wai Chiu Lai.) Q. Gao and K. W. C. Lai are with the Department of Mechanical and Biomedical Engineering, City University of Hong Kong, Hong Kong (e-mail: [email protected]).
PY - 2018/1
Y1 - 2018/1
N2 - Beta amyloid (Aβ) peptide, which is a common neuropathological hallmark deposit in the brain of patients with Alzheimer's disease, typically comprises 39-43 amino acid residues. Aβ peptides exist as isoforms of Aβ1-40 and Aβ1-42 with various lengths. In this research, atomic force microscopy (AFM) was applied to investigate Aβ 1-40 aggregations in Hank's Balanced Salt Solution. Toxic effect of Aβ1-40 oligomer was investigated in live SH-SY5Y neuroblastoma cells by characterizing cell morphology and cell mechanics using high-resolution AFM scanning. Aβ 1-40 oligomer-induced cytoskeleton reorganization was also observed under confocal microscopy, and it can account for reduction in Young's modulus of cells. Meanwhile, phosphorylation of tau increased after Aβ 1-40 oligomer treatment, possibly resulting inmicrotubule disassembly. This paper demonstrates the linkage between cellular mechanical changes and neurodegeneration mediated by Aβ 1-40. The method used implies promising applications of real-time monitoring of cellular mechanical properties given the toxic effects of Aβ 1-40 on living neuronal cells.
AB - Beta amyloid (Aβ) peptide, which is a common neuropathological hallmark deposit in the brain of patients with Alzheimer's disease, typically comprises 39-43 amino acid residues. Aβ peptides exist as isoforms of Aβ1-40 and Aβ1-42 with various lengths. In this research, atomic force microscopy (AFM) was applied to investigate Aβ 1-40 aggregations in Hank's Balanced Salt Solution. Toxic effect of Aβ1-40 oligomer was investigated in live SH-SY5Y neuroblastoma cells by characterizing cell morphology and cell mechanics using high-resolution AFM scanning. Aβ 1-40 oligomer-induced cytoskeleton reorganization was also observed under confocal microscopy, and it can account for reduction in Young's modulus of cells. Meanwhile, phosphorylation of tau increased after Aβ 1-40 oligomer treatment, possibly resulting inmicrotubule disassembly. This paper demonstrates the linkage between cellular mechanical changes and neurodegeneration mediated by Aβ 1-40. The method used implies promising applications of real-time monitoring of cellular mechanical properties given the toxic effects of Aβ 1-40 on living neuronal cells.
KW - atomic force microscopy
KW - Beta amyloid
KW - cellular mechanics
UR - http://www.scopus.com/inward/record.url?scp=85041400926&partnerID=8YFLogxK
U2 - 10.1109/TNB.2018.2800723
DO - 10.1109/TNB.2018.2800723
M3 - Journal article
C2 - 29570077
AN - SCOPUS:85041400926
SN - 1536-1241
VL - 17
SP - 70
EP - 77
JO - IEEE Transactions on Nanobioscience
JF - IEEE Transactions on Nanobioscience
IS - 1
ER -
