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Inflammasome priming by lipopolysaccharide is dependent upon ERK signaling and proteasome function.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Ghonime, Mohammed G. Fernandes-Alnemri, Teresa Das, Srabani Alnemri, Emad S. Wewers, Mark D. Eldomany, Ramadan A. Gavrilin, Mikhail A. Shamaa, Obada R.
Description	Author Affiliation: Ghonime MG ( Division of Pulmonary, Allergy, Critical Care, and Sleep Medicine, Dorothy M. Davis Heart and Lung Research Institute, The Ohio State University, Columbus, OH 43210)
Abstract	Caspase-1 activation is a central event in innate immune responses to many pathogenic infections and tissue damage. The NLRP3 inflammasome, a multiprotein scaffolding complex that assembles in response to two distinct steps, priming and activation, is required for caspase-1 activation. However, the detailed mechanisms of these steps remain poorly characterized. To investigate the process of LPS-mediated NLRP3 inflammasome priming, we used constitutively present pro-IL-18 as the caspase-1-specific substrate to allow study of the early events. We analyzed human monocyte caspase-1 activity in response to LPS priming, followed by activation with ATP. Within minutes of endotoxin priming, the NLRP3 inflammasome is licensed for ATP-induced release of processed IL-18, apoptosis-associated speck-forming complex containing CARD, and active caspase-1, independent of new mRNA or protein synthesis. Moreover, extracellular signal-regulated kinase 1 (ERK1) phosphorylation is central to the priming process. ERK inhibition and small interfering RNA-mediated ERK1 knockdown profoundly impair priming. In addition, proteasome inhibition prevents ERK phosphorylation and blocks priming. Scavenging reactive oxygen species with diphenylene iodonium also blocks both priming and ERK phosphorylation. These findings suggest that ERK1-mediated posttranslational modifications license the NLRP3 inflammasome to respond to the second signal ATP by inducing posttranslational events that are independent of new production of pro-IL-1ß and NOD-like receptor components.
ISSN	00221767
e-ISSN	15506606
DOI	10.4049/jimmunol.1301974
Journal	The Journal of Immunology
Issue Number	8
Volume Number	192
Language	English
Publisher	The American Association of Immunologists
Publisher Date	2014-04-15
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Inflammasomes Lipopolysaccharides Immunology Map Kinase Signaling System Proteasome Endopeptidase Complex Metabolism Carrier Proteins Caspase 1 Gene Expression Regulation Drug Effects Immunity, Innate Inflammation Genetics Interleukin-18 Interleukin-1beta Mitogen-activated Protein Kinase 1 Mitogen-activated Protein Kinase 3 Models, Biological Monocytes Oxidants Pharmacology Protein Kinase Inhibitors Research Support, N.i.h., Extramural Discipline Immunology
Content Type	Text
Resource Type	Article
Subject	Immunology and Allergy Immunology

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