Department of Cell and Developmental Biology, Oregon Health and Science University, Portland, Oregon, United States of America.
PLoS One. 2012;7(5):e36044. doi: 10.1371/journal.pone.0036044. Epub 2012 May 14.
Some inflammatory stimuli trigger activation of the NLRP3 inflammasome by inducing efflux of cellular potassium. Loss of cellular potassium is known to potently suppress protein synthesis, leading us to test whether the inhibition of protein synthesis itself serves as an activating signal for the NLRP3 inflammasome. Murine bone marrow-derived macrophages, either primed by LPS or unprimed, were exposed to a panel of inhibitors of ribosomal function: ricin, cycloheximide, puromycin, pactamycin, and anisomycin. Macrophages were also exposed to nigericin, ATP, monosodium urate (MSU), and poly I:C. Synthesis of pro-IL-ß and release of IL-1ß from cells in response to these agents was detected by immunoblotting and ELISA. Release of intracellular potassium was measured by mass spectrometry. Inhibition of translation by each of the tested translation inhibitors led to processing of IL-1ß, which was released from cells. Processing and release of IL-1ß was reduced or absent from cells deficient in NLRP3, ASC, or caspase-1, demonstrating the role of the NLRP3 inflammasome. Despite the inability of these inhibitors to trigger efflux of intracellular potassium, the addition of high extracellular potassium suppressed activation of the NLRP3 inflammasome. MSU and double-stranded RNA, which are known to activate the NLRP3 inflammasome, also substantially inhibited protein translation, supporting a close association between inhibition of translation and inflammasome activation. These data demonstrate that translational inhibition itself constitutes a heretofore-unrecognized mechanism underlying IL-1ß dependent inflammatory signaling and that other physical, chemical, or pathogen-associated agents that impair translation may lead to IL-1ß-dependent inflammation through activation of the NLRP3 inflammasome. For agents that inhibit translation through decreased cellular potassium, the application of high extracellular potassium restores protein translation and suppresses activation of the NLRP inflammasome. For agents that inhibit translation through mechanisms that do not involve loss of potassium, high extracellular potassium suppresses IL-1ß processing through a mechanism that remains undefined.
一些炎症刺激物通过诱导细胞内钾外流来触发 NLRP3 炎性体的激活。众所周知,细胞内钾的流失会强烈抑制蛋白质合成,这促使我们测试蛋白质合成本身的抑制是否作为 NLRP3 炎性体的激活信号。用 LPS 或未用 LPS 预刺激的鼠源骨髓来源的巨噬细胞暴露于一系列核糖体功能抑制剂中:蓖麻毒素、环己亚胺、嘌呤霉素、 pactamycin 和 anisomycin。巨噬细胞还暴露于 Nigericin、ATP、单钠尿酸盐(MSU)和聚 I:C。通过免疫印迹和 ELISA 检测这些试剂刺激下细胞中前 IL-ß 的合成和 IL-1ß 的释放。通过质谱法测量细胞内钾的释放。测试的每种翻译抑制剂的翻译抑制均导致 IL-1ß 的加工,其从细胞中释放。NLRP3、ASC 或 caspase-1 缺陷细胞中 IL-1ß 的加工和释放减少或缺失,证明了 NLRP3 炎性体的作用。尽管这些抑制剂不能触发细胞内钾外流,但高细胞外钾的添加抑制了 NLRP3 炎性体的激活。MSU 和双链 RNA,已知能激活 NLRP3 炎性体,也能显著抑制蛋白质翻译,支持翻译抑制与炎性体激活之间的密切关联。这些数据表明,翻译抑制本身构成了以前未被识别的 IL-1ß 依赖炎症信号传导的机制,并且其他物理、化学或病原体相关的可导致翻译受损的试剂可能通过激活 NLRP3 炎性体导致 IL-1ß 依赖的炎症。对于通过降低细胞内钾抑制翻译的试剂,高细胞外钾的应用可恢复蛋白质翻译并抑制 NLRP 炎性体的激活。对于通过不涉及钾流失的机制抑制翻译的试剂,高细胞外钾通过仍未定义的机制抑制 IL-1ß 的加工。