瘦素敏感的JAK2激活在PC12细胞中调控Tau磷酸化。

Q1 Medicine Neurosignals Pub Date : 2016-01-01 Epub Date: 2016-09-08 DOI:10.1159/000442615

Meixia Guo, Dongliang Li, Huijun Shen, Baijie Jin, Yankai Ren, Manli Li, Ying Xing

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引用次数: 9

摘要

背景/目的:阿尔茨海默病(AD)的两个主要特征是:细胞内神经原纤维缠结中β-淀粉样蛋白(Aβ)肽的沉积和积累以及过度磷酸化的tau。一系列证据表明，瘦素减少了Aβ的产生和tau的磷酸化。在此，我们研究了瘦素激活的信号通路，以广泛了解其机制。方法:采用Western blotting检测p-tau蛋白和BAX蛋白丰度，MTT法检测细胞活力。结果:瘦素降低tau磷酸化，其作用依赖于JAK2的激活。结论:数据提示JAK2参与ad相关通路。

本文章由计算机程序翻译，如有差异，请以英文原文为准。

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Leptin-Sensitive JAK2 Activation in the Regulation of Tau Phosphorylation in PC12 Cells.

Background/aims: Alzheimer's disease (AD) is characterized by two major hallmarks: the deposition and accumulation of β-amyloid (Aβ) peptide and hyperphosphorylated tau in intracellular neurofibrillary tangles. Sets of evidence show that leptin reduces Aβ production and tau phosphorylation. Herein, we investigated the signaling pathways activated by leptin, to extensively understand its mechanism.

Methods: Western blotting was employed to assess the protein abundance of p-tau and BAX, MTT assay to decipher the cells viability.

Results: Leptin decreased tau phosphorylation, an effect was dependent on the activation of JAK2.

Conclusion: The data suggest that JAK2 is involved in AD-related pathways.

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来源期刊

Neurosignals 医学-神经科学

CiteScore

3.40

自引率

0.00%

发文量

审稿时长

>12 weeks

期刊介绍： Neurosignals is an international journal dedicated to publishing original articles and reviews in the field of neuronal communication. Novel findings related to signaling molecules, channels and transporters, pathways and networks that are associated with development and function of the nervous system are welcome. The scope of the journal includes genetics, molecular biology, bioinformatics, (patho)physiology, (patho)biochemistry, pharmacology & toxicology, imaging and clinical neurology & psychiatry. Reported observations should significantly advance our understanding of neuronal signaling in health & disease and be presented in a format applicable to an interdisciplinary readership.