Harris Daniel P, Chandrasekharan Unnikrishnan M, Bandyopadhyay Smarajit, Willard Belinda, DiCorleto Paul E
Department of Cellular and Molecular Medicine, Cleveland Clinic Lerner Research Institute and Cleveland Clinic Lerner College of Medicine of Case Western Reserve University, Cleveland, Ohio, United States of America.
Department of Physiology and Biophysics, School of Medicine, Case Western Reserve University, Cleveland, Ohio, United States of America.
PLoS One. 2016 Feb 22;11(2):e0148905. doi: 10.1371/journal.pone.0148905. eCollection 2016.
Inflammatory agonists differentially activate gene expression of the chemokine family of proteins in endothelial cells (EC). TNF is a weak inducer of the chemokine CXCL11, while TNF and IFN-γ costimulation results in potent CXCL11 induction. The molecular mechanisms underlying TNF plus IFN-γ-mediated CXCL11 induction are not fully understood. We have previously reported that the protein arginine methyltransferase PRMT5 catalyzes symmetrical dimethylation of the NF-κB subunit p65 in EC at multiple arginine residues. Methylation of Arg30 and Arg35 on p65 is critical for TNF induction of CXCL10 in EC. Here we show that PRMT5-mediated methylation of p65 at Arg174 is required for induction of CXCL11 when EC are costimulated with TNF and IFN-γ. Knockdown of PRMT5 by RNAi reduced CXCL11 mRNA and protein levels in costimulated cells. Reconstitution of p65 Arg174Ala or Arg174Lys mutants into EC that were depleted of endogenous p65 blunted TNF plus IFN-γ-mediated CXCL11 induction. Mass spectrometric analyses showed that p65 Arg174 arginine methylation is enhanced by TNF plus IFN-γ costimulation, and is catalyzed by PRMT5. Chromatin immunoprecipitation assays (ChIP) demonstrated that PRMT5 is necessary for p65 association with the CXCL11 promoter in response to TNF plus IFN-γ. Further, reconstitution of p65 Arg174Lys mutant in EC abrogated this p65 association with the CXCL11 promoter. Finally, ChIP and Re-ChIP assays revealed that symmetrical dimethylarginine-containing proteins complexed with the CXCL11 promoter were diminished in p65 Arg174Lys-reconstituted EC stimulated with TNF and IFN-γ. In total, these results indicate that PRMT5-mediated p65 methylation at Arg174 is essential for TNF plus IFN-γ-mediated CXCL11 gene induction. We therefore suggest that the use of recently developed small molecule inhibitors of PRMT5 may present a therapeutic approach to moderating chronic inflammatory pathologies.
炎症激动剂在内皮细胞(EC)中差异激活趋化因子家族蛋白的基因表达。肿瘤坏死因子(TNF)是趋化因子CXCL11的弱诱导剂,而TNF与干扰素-γ(IFN-γ)共同刺激可导致CXCL11的强力诱导。TNF加IFN-γ介导的CXCL11诱导的分子机制尚未完全了解。我们之前报道过,蛋白精氨酸甲基转移酶PRMT5催化内皮细胞中NF-κB亚基p65多个精氨酸残基的对称二甲基化。p65上Arg30和Arg35的甲基化对于内皮细胞中TNF诱导CXCL10至关重要。在此我们表明,当内皮细胞与TNF和IFN-γ共同刺激时,PRMT5介导的p65在Arg174处的甲基化是诱导CXCL11所必需的。通过RNA干扰敲低PRMT5可降低共同刺激细胞中CXCL11的mRNA和蛋白水平。将p65 Arg174Ala或Arg174Lys突变体重组到内源性p65缺失的内皮细胞中,可减弱TNF加IFN-γ介导的CXCL11诱导。质谱分析表明,TNF加IFN-γ共同刺激可增强p65 Arg174的精氨酸甲基化,且由PRMT5催化。染色质免疫沉淀分析(ChIP)表明,PRMT5是p65响应TNF加IFN-γ与CXCL11启动子结合所必需的。此外,在内皮细胞中重组p65 Arg174Lys突变体可消除这种p65与CXCL11启动子的结合。最后,ChIP和再ChIP分析表明,在TNF和IFN-γ刺激的p65 Arg174Lys重组内皮细胞中,与CXCL11启动子结合的含对称二甲基精氨酸的蛋白减少。总体而言,这些结果表明PRMT5介导的p65在Arg174处的甲基化对于TNF加IFN-γ介导的CXCL11基因诱导至关重要。因此,我们建议使用最近开发的PRMT5小分子抑制剂可能是一种调节慢性炎症病理的治疗方法。