Sato N, Kyakumoto S, Sawano K, Ota M
Department of Biochemistry Iwate Medical University School of Dentistry, Japan.
Biochem Mol Biol Int. 1996 Mar;38(3):597-606.
We examined the proliferative signal transduction by EGF in HSG-AZA 3, a subclone of HSG cell line. The treatment of cells with EGF resulted in an increase in [3H]thymidine incorporation into DNA depending upon EGF concentrations. In addition, the nuclear proto-oncogene c-fos was rapidly induced by EGF. Moreover, EGF induced transient expression of EGF receptor mRNA followed by the de novo synthesis of EGF receptor protein. On the other hand, treatment of the cells with EGF occurred phosphorylation by tyrosine kinase comprised in the EGF receptor, autophosphorylation, followed by activation of MAP kinase. These results indicate that the proliferative response to EGF is modulated by the phosphorylation cascade mediating EGF receptor-associated tyrosine kinase and MAP kinase, and transient activation of c-fos protein is implicated in the cell proliferation.
我们检测了HSG细胞系的一个亚克隆HSG-AZA 3中表皮生长因子（EGF）介导的增殖信号转导。用EGF处理细胞后，[3H]胸苷掺入DNA的量增加，且这一增加依赖于EGF的浓度。此外，EGF能快速诱导核原癌基因c-fos。而且，EGF诱导EGF受体mRNA的瞬时表达，随后是EGF受体蛋白的从头合成。另一方面，用EGF处理细胞会导致EGF受体中所含的酪氨酸激酶发生磷酸化，即自身磷酸化，随后丝裂原活化蛋白激酶（MAP激酶）被激活。这些结果表明，对EGF的增殖反应是由介导EGF受体相关酪氨酸激酶和MAP激酶的磷酸化级联反应调节的，c-fos蛋白的瞬时激活与细胞增殖有关。
