Endoplasmic reticulum stress mediates JNK-dependent IRS-1 serine phosphorylation and results in Tau hyperphosphorylation in amyloid β oligomer-treated PC12 cells and primary neurons
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- 作者：Xiao Zhang ; Shi Tang ; Qinghua Zhang ; Wen Shao ; Xiaojuan Han ; Yongxiang Wang ; Yifeng Du ; neurology2014j@163.com" class="auth_mail" title="E-mail the corresponding author ; duyifeng@sdu.edu.cn" class="auth_mail" title="E-mail the corresponding author
- 关键词：Aβ1&ndash ; 42 oligomers ; Amyloid β1&ndash ; 42 oligomers ; AD ; Alzheimer's disease ; Akt ; Phosphorylated protein kinase B ; DMEM ; Dulbecco's modified Eagle's medium ; DMSO ; Dimethyl sulfoxide ; ERS ; Endoplasmic reticulum stress ; HIFP ; 1 ; 1 ; 1 ; 3 ; 3 ; 3-hexa-fluoro-2-propanol ; IRS-1 ; Insulin receptor substance-1 ; JNK ; c-Jun. N-terminal kinase ; PBA ; 4-Phenyl butyric acid ; PBS ; Phosphate-buffered saline ; TG ; Thapsigargin ; BiP ; Binding immunoglobulin protein ; CHOP ; C/EBP homologous protein ; ATF4 ; Activating
- 刊名：Gene
- 出版年：2016
- 出版时间：10 August 2016
- 年：2016
- 卷：587
- 期：2
- 页码：183-193
- 全文大小：1948 K
文摘
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Aβ1–42 induced ERS and impaired insulin signaling.
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ERS inhibition alleviated the IRS-1 serine phosphorylation.
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JNK inhibition attenuated the IRS-1 serine phosphorylation.
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ERS might contribute to insulin signaling impairment via JNK activation.
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ERS/JNK/IRS-1 pathway might contribute to Aβ1–42-induced Tau hyperphosphorylation.