炎症体
启动(农业)
GSM演进的增强数据速率
细胞生物学
化学
生物
计算机科学
生物化学
人工智能
植物
受体
发芽
作者
Eric I. Elliott,Alexis N Miller,Balaji Banoth,Shankar S. Iyer,Aleksandr Stotland,Jerrold Weiss,Roberta A. Gottlieb,Fayyaz S. Sutterwala,Suzanne L. Cassel
出处
期刊:Journal of Immunology
[American Association of Immunologists]
日期:2018-03-30
卷期号:200 (9): 3047-3052
被引量:158
标识
DOI:10.4049/jimmunol.1701723
摘要
Abstract The NLRP3 inflammasome is activated in response to microbial and danger signals, resulting in caspase-1–dependent secretion of the proinflammatory cytokines IL-1β and IL-18. Canonical NLRP3 inflammasome activation is a two-step process requiring both priming and activation signals. During inflammasome activation, NLRP3 associates with mitochondria; however, the role for this interaction is unclear. In this article, we show that mouse NLRP3 and caspase-1 independently interact with the mitochondrial lipid cardiolipin, which is externalized to the outer mitochondrial membrane at priming in response to reactive oxygen species. An NLRP3 activation signal is then required for the calcium-dependent association of the adaptor molecule ASC with NLRP3 on the mitochondrial surface, resulting in inflammasome complex assembly and activation. These findings demonstrate a novel lipid interaction for caspase-1 and identify a role for mitochondria as supramolecular organizing centers in the assembly and activation of the NLRP3 inflammasome.
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