Pathological concentration of zinc dramatically accelerates abnormal aggregation of full-length human Tau and thereby significantly increases Tau toxicity in neuronal cells

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• 作者：Ji-Ying Hu^a ; De-Lin Zhang^a ; Xiao-Ling Liu^a ; Xue-Shou Li^a ; Xiao-Qing Cheng^b ; Jie Chen^a ; Hai-Ning Du^b ; Yi Liang^a ; ^{liangyi@whu.edu.cn}
• 关键词：AD ; Alzheimer disease ; TEM ; transmission electron microscopy ; ThS ; thioflavin S ; PI ; propidium iodide ; DAPI ; 4&prime ; 6&prime ; -diamino-2-phenylindole dihydrochloride ; IAPP ; islet amyloid polypeptide ; TDP-43 ; TAR DNA-binding protein of 43  ; kDa ; MTT ; 3-(4 ; 5-dimethylthiazol-2-yl)-2 ; 5-diphenyltetrazolium bromide ; ITC ; isothermal titration calorimetry ; GSK-3β ; glycogen synthase kinase-3β
• 刊名：Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease
• 出版年：2017
• 出版时间：February 2017
• 年：2017
• 卷：1863
• 期：2
• 页码：414-427
• 全文大小：2632 K
• 卷排序：1863

文摘

Zn2 + enhances Tau aggregation in neuronal cells. Zn2 + enhances Tau aggregation-induced apoptosis and toxicity in neuronal cells. Substitution of two cysteine residues in Tau eliminates such enhancing effects. Our findings link Tau aggregation and toxicity regulated by zinc to the pathogenesis of Alzheimer disease.