ABSTRACT
Objective:To study the mechanism of protein kinase C regulating CD44 gene expression in vascular endothelial cells.Methods:Human umbilical vein endothelial cells (HUVECs)were taken as study model.The extract of Raf-1 kinase by immunoprecipitation was used for the Western blot analysis,and its activity was determined by enhanced chemiluminescene assay.CD44 gene expression was detected with RT-PCR,and phosphorylation was measurated by autoradiography.Results:CD44 phosphorylation in HUVECs was enhanced by 10ng/ml PMA treatment as compared with untreated cells, which reached the highest level at 30 minutes. Raf-1 kinase activity increased significantly after exposure to 10ng /ml PMA, and 0.05 ?mol/L Calphostinc could inhibit the role of Protein kinase C(PKC). CD44 gene expression level increased obviously after exposure to 10 ng /ml PMA (PKC activator) for only 1 minute(P