炎症体
信号转导衔接蛋白
吡喃结构域
细胞生物学
半胱氨酸蛋白酶1
基因敲除
生物
目标2
分泌物
病菌
化学
微生物学
信号转导
受体
生物化学
细胞培养
遗传学
作者
Beckley K. Davis,Reid A. Roberts,Brianne R. Barker,Joseph A. Duncan,Jenny P.-Y. Ting
出处
期刊:Journal of Immunology
[The American Association of Immunologists]
日期:2012-05-01
卷期号:188 (1_Supplement): 114.8-114.8
被引量:1
标识
DOI:10.4049/jimmunol.188.supp.114.8
摘要
Abstract The nucleotide-binding domain leucine-rich repeat-containing proteins, NLRs, are intracellular sensors of pathogen-associated molecular patterns and damage-associated molecular patterns. A subgroup of NLRs can form inflammasome complexes, which facilitate the maturation of procaspase 1 to caspase 1, leading to IL-1β and IL-18 cleavage and secretion. NLRC5 is predominantly expressed in hematopoietic cells and has not been studied for inflammasome function. RNA interference-mediated knockdown of NLRC5 nearly eliminated caspase 1, IL-1β, and IL-18 processing in response to bacterial infection, pathogen-associated molecular patterns, and damage-associated molecular patterns. This was confirmed in primary human monocytic cells. NLRC5, together with procaspase 1, pro-IL-1β, and the inflammasome adaptor ASC, reconstituted inflammasome activity that showed cooperativity with NLRP3. The range of pathogens that activate NLRC5 inflammasome overlaps with those that activate NLRP3. Furthermore, NLRC5 biochemically associates with NLRP3 in a nucleotide-binding domain-dependent but leucine-rich repeat-inhibitory fashion. These results invoke a model in which NLRC5 interacts with NLRP3 to cooperatively activate the inflammasome
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