RelB 核易位独立促进 LPS 诱导的黏附
p52-Independent nuclear translocation of RelB promotes LPS-induced attachment.
机构信息
Laboratory of Immunology, National Institute on Aging, NIH Biomedical Research Center, Baltimore, MD 21224, USA.
出版信息
Biochem Biophys Res Commun. 2010 Jan 1;391(1):235-41. doi: 10.1016/j.bbrc.2009.11.039. Epub 2009 Nov 10.
The NF-kappaB signaling pathways have a critical role in the development and progression of various cancers. In this study, we demonstrated that the small cell lung cancer cell line (SCLC) H69 expressed a unique NF-kappaB profile as compared to other cancer cell lines. The p105/p50, p100/p52, c-Rel, and RelB protein and mRNA transcripts were absent in H69 cells but these cells expressed RelA/p65. The activation of H69 cells by lipopolysaccharide (LPS) resulted in the induction of RelB and p100 expression. The treatment also induced the nuclear translocation of RelB without the processing of p100 to p52. Furthermore, LPS-induced beta1 integrin expression and cellular attachment through an NF-kappaB-dependent mechanism. Blocking RelB expression prevented the increase in the expression of beta1 integrin and the attachment of H69. Taken together, the results suggest that RelB was responsible for the LPS-mediated attachment and may play an important role in the progression of some cancers.
NF-κB 信号通路在各种癌症的发生和发展中起着关键作用。在这项研究中，我们证明与其他癌细胞系相比，小细胞肺癌细胞系（SCLC）H69 表达了独特的 NF-κB 谱。H69 细胞中缺乏 p105/p50、p100/p52、c-Rel 和 RelB 蛋白和 mRNA 转录本，但这些细胞表达 RelA/p65。脂多糖（LPS）激活 H69 细胞导致 RelB 和 p100 的表达诱导。该处理还诱导了 RelB 的核易位，而没有将 p100 加工成 p52。此外，LPS 诱导通过 NF-κB 依赖机制表达 β1 整联蛋白和细胞附着。阻断 RelB 表达可防止 β1 整联蛋白表达增加和 H69 的附着。总之，这些结果表明 RelB 负责 LPS 介导的附着，并且可能在某些癌症的进展中起重要作用。
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