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Virogen谷胱甘肽抗体101-A现货文献应用五

更新时间:2024-06-10   点击次数:134次

品牌:Virogen

货号:101-A

代理:靶点科技

名称:ANTI-GLUTATHIONE MAB 100

论文题目Glutaredoxin-1 regulates TRAF6 activation and the IL-1 receptor/TLR4 signalling

期刊:Biochemical and Biophysical Research Communications (BBRC). Volume 403, Issues 3–4, 17 December 2010, Pages 335-339


摘要:戊二醇-1 (GRX-1) 是一种细胞质酶,对抗氧化防御系统有很大贡献。它催化谷胱甘肽-蛋白质混合二硫化物的可逆还原,这一过程称为脱谷胱甘肽化。在这里,我们通过使用 HEK293 和 HeLa 细胞中的 RNA 干扰 (RNAi) 研究了 GRX-1 在白细胞介素-1/Toll 样受体 4 (IL-1R/TLR4) 触发的通路中的作用。TNF 受体相关因子 6 (TRAF6) 是一种中间信号分子,参与白细胞介素-1/Toll 样受体 (IL-1R/TLR) 家族成员的信号转导。TRAF6 具有 E3 泛素连接酶活性,该活性取决于氨基末端非常有趣的新基因 (RING) 手指基序的完整性。受体激活后,TRAF6 发生 K63 连接的自体多泛素化,介导蛋白质-蛋白质相互作用和信号传播。我们的数据表明,IL-1R 和 TLR4 介导的 NF-κB 诱导在 GRX-1 敲低细胞中严重降低。我们发现 TRAF6 的无名指基序在正常条件下是 S-谷胱甘肽化的。此外,在 IL-1 刺激下,TRAF6 经历由 GRX-1 催化的去谷胱甘肽化。TRAF6 的去谷胱氨酰化对其自动多泛素化和随后的激活至关重要。综上所述,我们的研究结果揭示了另一种受 S-谷胱甘肽化影响的信号分子,并揭示了 GRX-1 在 IL-1R/TLR 对 NF-κB 的 TRAF6 依赖性激活中的关键作用。


Abstract:

Glutaredoxin-1 (GRX-1) is a cytoplasmic enzyme that highly contributes to the antioxidant defense system. It catalyzes the reversible reduction of glutathione–protein mixed disulfides, a process called deglutathionylation. Here, we investigated the role of GRX-1 in the pathway triggered by interleukin-1/Toll-like receptor 4 (IL-1R/TLR4) by using RNA interference (RNAi) in HEK293 and HeLa cells. TNF receptor-associated factor 6 (TRAF6) is an intermediate signalling molecule involved in the signal transduction by members of the interleukin-1/Toll-like receptor (IL-1R/TLR) family. TRAF6 has an E3 ubiquitin ligase activity which depends on the integrity of an amino-terminal really interesting new gene (RING) finger motif. Upon receptor activation, TRAF6 undergoes K63-linked auto-polyubiquitination which mediates protein–protein interactions and signal propagation. Our data showed that IL-1R and TLR4-mediated NF-κB induction was severely reduced in GRX-1 knockdown cells. We found that the RING-finger motif of TRAF6 is S-glutathionylated under normal conditions. Moreover, upon IL-1 stimulation TRAF6 undergoes deglutathionylation catalyzed by GRX-1. The deglutathionylation of TRAF6 is essential for its auto-polyubiquitination and subsequent activation. Taken together, our findings reveal another signalling molecule affected by S-glutathionylation and uncover a crucial role for GRX-1 in the TRAF6-dependent activation of NF-κB by IL-1R/TLRs.


谷胱甘肽检测抗体:

Virogen谷胱甘肽抗体101-A现货文献应用五

靶点科技(北京)有限公司

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