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Inflammasomes: too big to miss
Andrea Stutz, … , Douglas T. Golenbock, Eicke Latz
Andrea Stutz, … , Douglas T. Golenbock, Eicke Latz
Published December 1, 2009
Citation Information: J Clin Invest. 2009;119(12):3502-3511. https://doi.org/10.1172/JCI40599.
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Science in Medicine

Inflammasomes: too big to miss

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Abstract

Inflammation is the coordinated immune response to harmful stimuli that appear during infections or after tissue damage. Cells of the innate immune system are the central players in mediating inflammatory tissue responses. These cells are equipped with an array of signaling receptors that detect foreign molecular substances or altered endogenous molecules that appear under situations of stress. This review provides an overview of recent progress in elucidating the molecular mechanisms that lead to inflammatory reactions. We discuss the current knowledge of the mechanisms leading to the activation of cytoplasmic, multimolecular protein complexes, termed “inflammasomes,” which regulate the activity of caspase-1 and the maturation and release of IL-1β.

Authors

Andrea Stutz, Douglas T. Golenbock, Eicke Latz

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Figure 1

Graphical depiction of known inflammasomes.

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Graphical depiction of known inflammasomes.
(A) NLRP1 contains, in addit...
(A) NLRP1 contains, in addition to the NLR-typical LRR and NBD domains, a PYD, a FIIND, and a CARD. NLRP1 can recruit pro–caspase-1 and -5 and possibly forms a complex with NOD2. Recruitment of ASC enhances activation of pro–caspase-1. (B) NLRC4 contains a CARD that can directly recruit pro–caspase-1. Reports further demonstrate a role for ASC and possibly NAIP5 in NLRC4 inflammasome activation. (C) NLRP3 activates pro–caspase-1 via recruitment of ASC. (D) AIM2 is a bipartite protein consisting of a PYD and DNA-binding HIN200 domain and recognizes cytoplasmic double-stranded DNA and assembles the DNA inflammasome with ASC and pro–caspase-1.

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