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为了研究TGF-β1对α5β1整合蛋白所介导的信号转导通路是否有快速的信号调节作用,本文用TGF-β1短时(10min)处理SMMC-7721细胞,发现当经TGF-β1预处理的细胞与Fn粘附时,细胞与Fn的粘附力下降,由Fn与整合蛋白的结合而诱导发生的FAK的酪氨酸磷酸化随着TGF-β1浓度的增加而降低。而TGF-β1短时处理并未改变整合蛋白α5、β1亚基的表达。此外,贴壁生长于培养皿的细胞的FAK磷酸化程度在TGF-β1短时处理后也下降,甚至检测不出。提示TGF-β1可能通过某种信号通路快速调节了整合蛋白与配体的亲和力以及下游信号分子FAK的磷酸化。从而影响了细胞内骨架蛋白结构的完整性,使细胞发生去极性化,有利于细胞在迁移早期的松脱。
To investigate whether TGF-β1 has a rapid signal-regulatory effect on α5β1 integrin-mediated signal transduction pathways, SMMC-7721 cells were treated with TGF-β1 for a short time (10 min) and found to be pretreated with TGF-β1. When cells attach to Fn, the adhesion of cells to Fn decreases, and the tyrosine phosphorylation of FAK induced by the binding of Fn to integrin decreases as the concentration of TGF-β1 increases. The short-term treatment of TGF-β1 did not alter the expression of integrin α5, β1 subunits. In addition, the degree of FAK phosphorylation of cells adhering to the culture dish was also decreased after treatment with TGF-β1 for a short time, and even detected. This suggests that TGF-β1 may regulate the affinity of integrin and ligand and the phosphorylation of downstream signaling molecule FAK through a signal pathway. As a result, the integrity of the cytoskeletal protein structure is affected, and the cells are depolarized, which facilitates the release of cells in the early stages of migration.