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两种新型A20样蛋白的分离与鉴定

Isolation and characterization of two novel A20-like proteins.

作者信息

Evans P C, Taylor E R, Coadwell J, Heyninck K, Beyaert R, Kilshaw P J

机构信息

Molecular Immunology Programme, The Babraham Institute, Babraham, Cambridge CB2 4AT, UK.

出版信息

Biochem J. 2001 Aug 1;357(Pt 3):617-23. doi: 10.1042/0264-6021:3570617.

Abstract

The transcription factor nuclear factor kappa B (NF-kappa B) plays a pivotal role in inflammatory processes through induction of adhesion molecules and chemokines. The zinc finger molecule A20 is an important negative regulator of NF-kappa B. The mechanism utilized by A20 is not fully understood, but A20 has been shown to bind to tumour-necrosis-factor-receptor-associated factor (TRAF) molecules, which are necessary for pro-inflammatory cytokine signalling. We report two novel genes, Cezanne (cellular zinc finger anti-NF-kappa B) and TRABID (TRAF-binding domain), with sequence similarity to A20. Co-immunoprecipitation studies indicated that TRAF6 was able to interact with both Cezanne and TRABID. In contrast, reporter gene experiments revealed a specific ability of Cezanne to down-regulate NF-kappa B. It is likely, therefore, that Cezanne participates in the regulation of inflammatory processes.

摘要

转录因子核因子κB(NF-κB)通过诱导黏附分子和趋化因子在炎症过程中起关键作用。锌指分子A20是NF-κB的重要负调节因子。A20所利用的机制尚未完全阐明,但已表明A20可与肿瘤坏死因子受体相关因子(TRAF)分子结合,而TRAF分子是促炎细胞因子信号传导所必需的。我们报告了两个与A20具有序列相似性的新基因,即Cezanne(细胞锌指抗NF-κB)和TRABID(TRAF结合域)。免疫共沉淀研究表明,TRAF6能够与Cezanne和TRABID相互作用。相比之下,报告基因实验揭示了Cezanne下调NF-κB的特定能力。因此,Cezanne可能参与炎症过程的调节。

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Isolation and characterization of two novel A20-like proteins.两种新型A20样蛋白的分离与鉴定
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