p38丝裂原活化蛋白激酶参与大肠杆菌诱导的U937细胞凋亡。

Jia-He Wang, Yi-Jun Zhou, Ping He, Bai-Yi Chen
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引用次数: 0

摘要

目的:探讨大肠杆菌是否通过激活p38丝裂原活化蛋白激酶(MAPK)介导U937细胞株凋亡。方法:用大肠杆菌不同时间或与p38抑制剂SB203580联合作用于U937细胞系。流式细胞术检测细胞凋亡。Western blotting检测p38活性。结果:大肠杆菌诱导培养的U937细胞株凋亡呈时间依赖性。p38的磷酸化在感染10分钟后被诱导,20分钟后达到峰值,30分钟后开始下降。而p38总蛋白水平在整个实验期内均无明显变化。SB203580抑制p38可显著抑制大肠杆菌诱导的U937细胞凋亡。结论:大肠杆菌激活U937细胞株p38 MAPK是介导细胞凋亡的主要途径。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Involvement of p38 mitogen-activated protein kinase in E. coli-induced U937 apoptosis.

Objective: To investigate whether the effect of E. coli on U937 cell lines apoptosis is mediated via p38 mitogen-activated protein kinase (MAPK) activation.

Methods: The U937 cell lines were treated with E. coli at different time or together with SB203580, an inhibitor for p38. Cell apoptosis was analyzed by flow cytometry. p38 activities were detected by Western blotting.

Results: E. coli induced apoptosis in cultured U937 cell lines in a time-dependent manner. The phosphorylation of p38 was induced after 10 minutes infection, reached the peak after 20 minutes, and started to decline after 30 minutes. In contrast, the level of total p38 protein was not changed in whole experimental period. Inhibition of p38 with SB203580 significantly inhibited E. coli induced apoptosis in U937 cells.

Conclusion: The activation of the p38 MAPK in U937 cell lines by E. coli is a major pathway to mediate the apoptosis.

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