丝裂原活化蛋白激酶与阿卡塔细胞中EB病毒激活的相互作用。
The interaction of mitogen-activated protein kinases to Epstein-Barr virus activation in Akata cells.
作者信息
Satoh T, Hoshikawa Y, Satoh Y, Kurata T, Sairenji T
机构信息
Department of Biosignaling, School of Life Science, Faculty of Medicine, Tottori University, Yonago, Japan.
出版信息
Virus Genes. 1999;18(1):57-64. doi: 10.1023/a:1008021402908.
To understand the mechanism by which Epstein-Barr virus (EBV) is activated in Akata cells by cross-linking of surface immunoglobulin, the interaction between mitogen-activated protein kinase (MAPK)/extracellular signal-regulated kinase (ERK) and EBV activation was investigated. Immunoblotting using an anti-phosphoMAPK antibody (Ab) revealed that anti-IgG Ab induced rapid phosphorylation of MAPK in the cells. The phosphorylation was inhibited by MAPK/ERK kinase specific inhibitor, PD98059. The expressions of the EBV immediate early BZLF1 mRNA and its protein product ZEBRA, and early antigen were also inhibited by the inhibitor. These results indicate that MAPK is involved in the pathways of EBV activation.
为了解通过表面免疫球蛋白交联在阿卡塔细胞中激活爱泼斯坦-巴尔病毒（EBV）的机制，研究了丝裂原活化蛋白激酶（MAPK）/细胞外信号调节激酶（ERK）与EBV激活之间的相互作用。使用抗磷酸化MAPK抗体（Ab）进行免疫印迹分析显示，抗IgG Ab可诱导细胞中MAPK的快速磷酸化。该磷酸化被MAPK/ERK激酶特异性抑制剂PD98059所抑制。该抑制剂还抑制了EBV即刻早期BZLF1 mRNA及其蛋白产物ZEBRA以及早期抗原的表达。这些结果表明MAPK参与了EBV激活途径。
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