中国组织工程研究

中国组织工程研究 ›› 2012, Vol. 16 ›› Issue (41): 7713-7716.doi: 10.3969/j.issn.2095-4344.2012.41.023

• 干细胞与中医药 stem cells and traditional Chinese medicine • 上一篇    下一篇

人参皂苷Rb1对β-淀粉样蛋白25-35诱导神经干细胞分化过程中Tau蛋白过度磷酸化的影响

赵庆霞1，李冰华2，韩雪飞2，许 燕2，吴国华1   

  1. 1郑州大学护理学院，河南省郑州市 450053
    2郑州大学基础医学院干细胞研究中心，河南省郑州市 450053
  • 收稿日期:2012-01-04 修回日期:2012-02-17 出版日期:2012-10-07 发布日期:2012-10-07
  • 通讯作者: 吴国华，副教授，郑州大学护理学院实验中心，河南省郑州市 450053 wgh589@zzu.edu.com
  • 作者简介:赵庆霞★，女，河南省郑州市人，汉族，硕士，讲师，主要从事干细胞分化与调控的研究。 zzuzhaoqingxia@126.com

Ginsenoside Rb1 reduced beta-amyloid peptide 25-35-induced hyperphosphorylation of Tau protein during the differentiation of neural stem cells

Zhao Qing-xia1, Li Bing-hua2, Han Xue-fei2, Xu Yan2, Wu Guo-hua1   

  1. 1Nursing College of Zhengzhou University, Zhengzhou 450053, Henan Province, China
    2Research Center for Stem Cells, School of Basic Medical Sciences, Zhengzhou University, Zhengzhou 450053, Henan Province, China
  • Received:2012-01-04 Revised:2012-02-17 Online:2012-10-07 Published:2012-10-07
  • Contact: Wu Guo-hua, Associate professor, Nursing College of Zhengzhou University, Zhengzhou 450053, Henan Province, China wgh589@zzu.edu.com
  • About author:Zhao Qing-xia★, Master, Lecturer, Nursing College of Zhengzhou University, Zhengzhou 450053, Henan Province, China zzuzhaoqingxia@126.com

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摘要：

背景：前期研究发现，人参皂苷Rb1和β-淀粉样蛋白25-35可调节神经干细胞分化过程中Tau蛋白的磷酸化水平。蛋白磷酸酯酶2A与Tau蛋白过度磷酸化密切相关。
目的：观察β-淀粉样蛋白25-35和人参皂苷Rb1对神经干细胞分化过程中Tau蛋白磷酸化水平和蛋白磷酸酯酶2A活性的影响。
方法：分离、培养新生大鼠海马神经干细胞，诱导第3代神经干细胞分化1周后分组：①空白组：不加其他处理因素继续培养36 h。②β-淀粉样蛋白组：培养24 h后，加入β-淀粉样蛋白25-35继续培养12 h。③预处理组：先加入人参皂苷Rb1预处理24 h，再加入β-淀粉样蛋白25-35继续培养12 h。分别采用免疫荧光细胞化学法和western-blot法检测各组细胞Tau[pS396]、Tau[pS262]表达以及蛋白磷酸酯酶2A活性。
结果与结论：正常神经干细胞分化过程中有Tau[pS396]和Tau[pS262]的表达；β-淀粉样蛋白组细胞的Tau[pS396] 和Tau[pS262]表达上调，蛋白磷酸酯酶2A活性无明显变化；预处理组Tau[pS396]和Tau[pS262]表达下调且蛋白磷酸酯酶2A活性显著增强。提示正常神经干细胞分化过程中Tau蛋白表达一定程度的磷酸化水平，人参皂苷Rb1可通过提高蛋白磷酸酯酶2A活性来减轻β-淀粉样蛋白25-35诱导的神经干细胞分化过程中Tau蛋白过度磷酸化。

关键词: 人参皂苷Rb1, β-淀粉样蛋白25-35, 蛋白磷酸酯酶2A, 神经干细胞, Tau蛋白磷酸化

Abstract:

BACKGROUND: Previous studies have demonstrated that ginsenoside Rb and beta-amyloid peptide 25-35 (Aβ25-35) can regulate the phospholation of Tan protein during the differentiation of neural stem cells (NSCs). Protein phosphatase 2A (PP2A) is closely related to hyperphosphorylation of Tau protein.
OBJECTIVE: To investigate the effects of Aβ25-35 and ginsenoside Rb1 on phosphorylation level of Tau protein and activity of PP2A during the differentiation of NSCs.
METHODS: NSCs were isolated from newborn rat hippocampus. After culture for 1 week, passage 3 NSCs were divided into three groups. In the control group, NSCs were further cultured for 36 hours without any medium added. In the Aβ group, after 24 hours of culture, Aβ25-35 was added for another 12 hours of culture. In the ginsenoside Rb1 froup, ginsenoside Rb1 was added for 24 hour pretreatment, and Aβ25-35 was added for another 12 hours of culture. The expression of Tau[pS396] and Tau[pS262] was tested by the immunofluorescent cytochemical staining and western blot method, and PP2A activity was tested by ELISA.
RESULTS AND CONCLUSION: Cellular expression of Tau[pS396] and Tau[pS262] was detected during the differentiation of NSCs. In the Aβ group, cellular expression of Tau[pS396] and Tau[pS262] was up-regulated, and PP2A activity was not altered obviously. In the ginsenoside Rb1 group, cellular expression of Tau[pS396] and Tau[pS262] was down-regulated and PP2A activity was significantly increased. These findings suggest that during normal differentiation of NSCs, Tau protein was phosphorylated at a certain level, and ginsenoside Rb1 can alleviate Aβ25-35-induced hyperphosphorylation of Tau protein during the differentiation of NSCs by increasing PP2A activity.

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