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Updated: Dec 18, 2025

Detection of Inflammasome Activation and Pyroptotic Cell Death in Murine Bone Marrow-derived Macrophages
Published on: May 21, 2018
Increasing complexity of NLRP3 inflammasome regulation
Julien Moretti1,2, J Magarian Blander1,2,3,4,5
1The Jill Roberts Institute for Research in Inflammatory Bowel Disease, Weill Cornell Graduate School of Medical Science, Weill Cornell Medicine, Cornell University, New York, New York, USA.
Abstract:
Inflammasomes are multiprotein complexes that assemble upon detection of danger signals to activate the inflammatory enzyme caspase-1, trigger secretion of the highly proinflammatory cytokine IL-1β, and induce an inflammatory cell death called pyroptosis. Distinctiveness of the nucleotide-binding oligomerization (NOD), Leucine-rich repeat (LRR)-containing protein (NLRP3) inflammasome resides in the diversity of molecules that induce its activation, indicating a certain intricacy. Furthermore, besides the canonical activation of NLRP3 in response to various stimuli, caspase-11-dependent detection of intracellular LPS activates NLRP3 through a noncanonical pathway. Several aspects of the NLRP3 inflammasome are not characterized or remain unclear. In this review, we summarize the different modes of NLRP3 activation. We describe recent insights into post-translational and cellular regulation that confer further complexity to NLRP3 inflammasomes.
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