Sugimoto T, Kikkawa R, Haneda M, Shigeta Y
Third Department of Medicine, Shiga University of Medical Science, Japan.
Nihon Jinzo Gakkai Shi. 1995 Mar;37(3):151-6.
In order to evaluate the intracellular signaling pathway of endothelin 1 (ET-1), we examined mitogen-activated protein kinase (MAPK) cascade in cultured rat glomerular mesangial cells. Treatment of quiescent mesangial cells with ET-1 increased kinase activities toward bovine myelin basic protein (MBP). Maximal activation was at 10 min and ED50 was about 5 nM. The 44- and 42-kDa kinases were activated in MBP containing gel kinase assay. These kinases were identified as extracellular signal regulated kinase (ERK) 1 and ERK2 with immunoblotting, respectively. MAPK or ERK kinase (MEK), one of the MAPK kinases, was present in rat mesangial cells and ET-1 also activated this MAPK kinase. These results indicate that MAPK kinase and MAP kinase are rapidly activated by ET-1 and may modulate cellular functions in rat mesangial cells.
为了评估内皮素1(ET-1)的细胞内信号通路,我们检测了培养的大鼠肾小球系膜细胞中的丝裂原活化蛋白激酶(MAPK)级联反应。用ET-1处理静止的系膜细胞可增加对牛髓鞘碱性蛋白(MBP)的激酶活性。最大激活在10分钟时出现,半数有效浓度(ED50)约为5 nM。在含MBP的凝胶激酶分析中,44 kDa和42 kDa的激酶被激活。通过免疫印迹分别将这些激酶鉴定为细胞外信号调节激酶(ERK)1和ERK2。MAPK或ERK激酶(MEK)是MAPK激酶之一,存在于大鼠系膜细胞中,ET-1也可激活这种MAPK激酶。这些结果表明,MAPK激酶和MAP激酶可被ET-1快速激活,并可能调节大鼠系膜细胞的细胞功能。