The Interaction of Mitogen-Activated Protein Kinases to Epstein-Barr Virus Activation in Akata Cells
The Interaction of Mitogen-Activated Protein Kinases to Epstein-Barr Virus Activation in Akata Cells
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DOI：
10.1023/a:1008021402908
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发表时间：
2004
期刊：
影响因子：
1.6
通讯作者：
T. Satoh;Y. Hoshikawa;Yukio Satoh;T. Kurata;T. Sairenji
中科院分区：
文献类型：
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作者：
T. Satoh;Y. Hoshikawa;Yukio Satoh;T. Kurata;T. Sairenji
为了解EB病毒(EBV)通过表面免疫球蛋白交联在Akata细胞中被激活的机制，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。用抗磷酸MAPK抗体进行免疫印迹实验表明，抗Ig G抗体可诱导细胞内MAPK的快速磷酸化。MAPK/ERK激酶特异性抑制剂PD98059可抑制该蛋白的磷酸化。抑制EBV即刻早期BZLF1基因及其蛋白产物斑马蛋白和早期抗原的表达。这些结果表明，MAPK参与了EBV的激活途径。
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.