TGF-β1以受体和Smad7依赖的方式活化ERK  

TGF-β1 Induces Activation of Extracellular Signal-Regulated Kinase Through TβRⅡ and Smad7

作　　者：何欣蓉[1,2] 霍艳英[1] 胡迎春[1] 李刚[1] 刘敏丽[3] 宋博强[4] 米璨[3] 吴德昌[1] 

机构地区：[1]军事医学科学院放射医学研究所 [2]重庆医科大学病理学教研室,重庆400016 [3]重庆医科大学病理学教研室 [4]军事医学科学院附属医院

出　　处：《生物技术通讯》2006年第1期22-23,共2页Letters in Biotechnology

基　　金：国家自然科学基金项目(30200329)

摘　　要：目的:探讨人永生化BEP2D细胞中TGF-β活化ERK/MAPK通路的机制。方法:用RNA干扰的方法设计siRNAs使人永生化BEP2D细胞中TβRⅡ、Smad7基因沉默,用Westernblot分析TGF-β1诱导的ERK激酶磷酸化的变化。结果:当Smad7表达沉默后,TGF-β1诱导的ERK激酶磷酸化水平显著降低;当TβRⅡ和Smad7表达同时发生沉默后,细胞内TGF-β1诱导的ERK激酶磷酸化水平进一步降低到基础水平以下。结论:TGF-β1以受体和Smad7依赖的方式活化ERK/MAPK通路。Objective： To investigate the mechanism of TGF-β on the phosphorylation of extracellular signal-regulated kinase（ERK or p44/42） in human bronchial epithelial BEP2D cells. Methods： siRNAs were designed to specifically target TβR Ⅱ and Smad7 of BEP2D cells, siRNA transfection and Western blot were performed to examine the phosphorylation of ERK. Results： Smacl7 gene silencing leads to the phosphorylation level of ERK decreased. When expression of TβR Ⅱ and Smad7 was knock-down at the same time, TGF-β1-induced phosphorylation level of ERK is decreased further and lower than the control cells. Conclusions： TGF-β1 activate ERK/MAPK signaling in a TβR Ⅱ and Smad7 dependent manner.

关 键 词：TGF-Β1 SMAD7 ERK RNA干扰 

分 类 号：Q75[生物学—分子生物学] Q78