Mitogen-activated protein kinase is involved in epidermal-growth-factor-regulated protein phosphorylation in nuclear membranes isolated from JEG-3 human choriocarcinoma cells

被引:5
作者
Bian, LJ [1 ]
Lei, ZM [1 ]
Rao, CV [1 ]
机构
[1] Univ Louisville, Hlth Sci Ctr, Dept Obstet & Gynecol, Lab Mol Reprod Biol & Med,Div Basic Sci Res, Louisville, KY 40292 USA
来源
EUROPEAN JOURNAL OF BIOCHEMISTRY | 1998年 / 253卷 / 03期
关键词
epidermal-growth factor receptor; nuclei; human choriocarcinoma cell; phosphorylation; mitogen-activated protein kinase;
D O I
10.1046/j.1432-1327.1998.2530545.x
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The treatment of highly purified nuclear membranes isolated from JEG-3 human choriocarcinoma cells with epidermal growth factor (EGF) resulted in an increase of the receptor autophosphorylation and the phosphorylation of several other proteins, including 44-kDa, 34-kDa and 24-kDa proteins, and a decrease in the phosphorylation of a 40-kDa protein. The kinetics of phosphorylation and the use of RG-13022, a selective inhibitor of EGF-receptor kinase activity, suggested that receptor activation was necessary for the phosphorylation response of the other proteins. Tyr was exclusively phosphorylated in the EGF receptor and 24-kDa proteins, Tyr and Thr were phosphorylated in the 44-kDa protein, and Ser was phosphorylated in the 34-kDa protein and dephosphorylated in the 40-kDa protein. The molecular size, Thr/Tyr phosphorylation, immunoprecipitation and enzymatic activity towards myelin basic protein suggested that the 44-kDa protein was a mitogen-activated protein (MAP) kinase. The EGF treatment not only increased phosphorylation but also catalytic activity of MAP kinase and these increases were prevented by the addition of RG-13022. In summary, this report demonstrates that target cell nuclei contain EGF receptors, which use the MAP kinase signaling pathway.
引用
收藏
页码:545 / 551
页数:7
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