华西口腔医学杂志 ›› 2012, Vol. 30 ›› Issue (6): 574-578.doi: 10.3969/j.issn.1000-1182.2012.06.004

• 基础研究 • 上一篇    下一篇

p38丝裂素活化蛋白激酶信号通路在应力调控成肌细胞分化中的作用

李菲菲1 阎潇2 王庆1 曲竹丽1 袁晓2 郭杰1   

  1. 1.山东大学口腔医院正畸科; 山东省口腔生物医学重点实验室, 济南250012; 2.青岛大学医学院附属青岛市立医院口腔医学中心正畸科; 青岛大学医学院附属医院中心实验室, 青岛266075
  • 收稿日期:2012-03-16 修回日期:2012-09-20 出版日期:2012-12-01 发布日期:2012-12-01
  • 通讯作者: 郭杰,Tel:0531-88382069
  • 作者简介:李菲菲(1987—),女,山东人,硕士
  • 基金资助:

    山东省自然科学基金资助项目(ZR2009CM109);山东省科技发展计划基金资助项目(2007GG30002035)

Effect of p38 mitogen-activated protein kinase signaling pathway during stretch-induced differentiation process of C2C12 myoblasts

Li Feifei1, Yan Xiao2, Wang Qing1, Qu Zhuli1, Yuan Xiao2, Guo Jie1.   

  1. 1. Dept. of Orthodontics, School of Stomatology, Shandong University; Shandong Provincial Key Laboratory of Oral Biomedicine, Jinan 250012, China; 2. Dept. of Orthodontics, Center of Stomatology, Qingdao Municipal Hospital, Qingdao University Medical College; Center Laboratory, The Affiliated Hospital of Qingdao University Medical College, Qingdao 266075, China
  • Received:2012-03-16 Revised:2012-09-20 Online:2012-12-01 Published:2012-12-01

摘要:

目的研究在C2C12细胞成肌分化过程中应力对丝裂原活化蛋白激酶(MAPKs)信号通路中p38丝裂素活化蛋白激酶(p38MAPK)信号通路的影响。方法将6孔Bio Flex培养板上贴壁培养的C2C12细胞,以0.5 Hz的加载频率和10%的细胞拉伸变形幅度,分别进行拉伸培养2、6、12、24 h,应用Western blot免疫印迹检测总p38和磷酸化p-p38(Thr180/Tyr182)蛋白的表达情况。结果周期性机械拉伸在调控C2C12成肌细胞分化过程中,p38MAPK信号通路被激活。p38MAPK信号通路蛋白磷酸化水平在较高水平;而p38MAPK通路总蛋白表达维持在一基线水平,各组之间差异无统计学意义。加入p38MAPK信号通路特异性抑制剂SB203580后再加力,Myogenin的表达明显降低。结论p38MAPK信号通路在应力介导的C2C12成肌细胞分化过程中发挥重要作用,但不是这一调控过程的唯一通路。

关键词: p38丝裂素活化蛋白激酶, 分化, 成肌细胞

Abstract:

Objective To investigate the effect of cyclic stretch on p38 mitogen-activated protein kinase(p38MAPK) signaling pathway during stretch -induced differentiation process of C2C12 myoblasts. Methods C2C12 cells were seeded on Bio Flex 6-well plates, and cells were subsequently subjected to cyclic stretch at an optimal magnitude (10%) and frequency(0.5 Hz). The effects of cyclic stretch were examined at 2, 6, 12, 24 h. Antibodies specific to p38MAPK phosphorylated forms and the total protein levels of the p38MAPK were examined using Western blot analysis. Results These results indicated that p38MAPK was activated during stretch-induced C2C12 cell differentiation. The level of phosphorylated protein was higher in the p38MAPK signaling pathway. The expression of total protein was maintained at baseline level. There were no significant differences between groups. Treatment of cells with specific p38MAPK inhibitor SB203580 could decrease the expression of myogenin, but not completely abolish the myogenin expression after stretch. Conclusion p38MAPK signaling pathway plays an important role during stretch-induced differentiation process of C2C12 myoblasts, but is not activated exclusively in this process.

Key words: p38 mitogen-activated protein kinase, differentiation, myoblast