• 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>Clinical immunology: The official journal of the Clinical Immunology Society >Fas (CD95) ligation inhibits activation of NF-kappa B by targeting p65-Rel A in a caspase-dependent manner.
【24h】

Fas (CD95) ligation inhibits activation of NF-kappa B by targeting p65-Rel A in a caspase-dependent manner.

机译：Fas（CD95）连接以胱天蛋白酶依赖性方式靶向p65-Rel A，从而抑制NF-κB的活化。

获取原文
获取原文并翻译 | 示例
           
页面导航
  • 摘要
  • 著录项
  • 相似文献
  • 相关主题

摘要

Apoptosis is an important mechanism in T cell regulation. Initiation of apoptosis can be activated through two signaling pathways via proteins that bind the death domain, the MAPK-JNK pathway mediated by DAXX and the caspase pathway mediated by FADD. T cell proliferation is initiated by ligation of the T cell receptor (TCR) and activation of NF-kappaB, a transcription factor that has antiapoptotic functions. These pathways however are not isolated, and potential crosstalk between elements of the apoptotic pathway and growth pathway may be essential in determining cell survival. We studied the interaction between Fas- and the TCR-initiated pathways in Jurkat T cell as these pathways lead to opposing consequences. We show that Fas activation can inhibit TCR- and PMA/ionophore-initiated activation of NF-kappaB activity. The inhibition is caspase-dependent since an inhibitor of caspase activation, DEVD, can block the suppression of NF-kappaB activity following crosslinking of Fas. Analysis of the expression of the subunits of NF-kappaB revealed that the levels of p50 remained constant, whereas the levels of p65 were markedly decreased by crosslinking of Fas. These findings suggest that the Fas-ligation-mediated suppression preferentially targets p65 protein expression as a mechanism for suppression of antiapoptotic activities of NF-kappaB during apoptosis.
机译：凋亡是调节T细胞的重要机制。凋亡的启动可以通过两个信号途径通过与死亡域结合的蛋白质激活，DAXX介导的MAPK-JNK途径和FADD介导的半胱天冬酶途径。 T细胞增殖是通过T细胞受体（TCR）的连接和NF-kappaB（具有抗凋亡功能的转录因子）的激活而开始的。然而，这些途径不是孤立的，并且凋亡途径和生长途径的元件之间的潜在串扰对于确定细胞存活可能是必不可少的。我们研究了Jurkat T细胞中Fas和TCR起始途径之间的相互作用，因为这些途径导致相反的结果。我们显示Fas激活可以抑制TCR和PMA /离子载体启动的NF-κB激活。该抑制是胱天蛋白酶依赖性的，因为胱天蛋白酶激活的抑制剂DEVD可以阻断Fas交联后对NF-κB活性的抑制。对NF-κB亚基表达的分析表明，p50的水平保持恒定，而p65的水平由于Fas的交联而显着降低。这些发现表明，Fas-连接介导的抑制作用优先靶向p65蛋白表达，作为抑制细胞凋亡过程中NF-κB抗凋亡活性的机制。

著录项

相似文献

  • 外文文献
  • 中文文献
  • 专利
获取原文

客服邮箱：kefu@zhangqiaokeyan.com

京公网安备：11010802029741号 ICP备案号：京ICP备15016152号-6 六维联合信息科技 (北京) 有限公司©版权所有

  • 客服微信

  • 服务号