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The murine neutrophil NLRP3 inflammasome is activated by soluble but not particulate or crystalline agonists.

Abstract：

:Neutrophils express pattern recognition receptors (PRRs) and regulate immune responses via PRR-dependent cytokine production. An emerging theme is that neutrophil PRRs often exhibit cell type-specific adaptations in their signalling pathways. This prompted us to examine inflammasome signalling by the PRR NLRP3 in murine neutrophils, in comparison to well-established NLRP3 signalling pathways in macrophages. Here, we demonstrate that while murine neutrophils can indeed signal via the NLRP3 inflammasome, neutrophil NLRP3 selectively responds to soluble agonists but not to the particulate/crystalline agonists that trigger NLRP3 activation in macrophages via phagolysosomal rupture. In keeping with this, alum did not trigger IL-1β production from human PMN, and the lysosomotropic peptide Leu-Leu-OMe stimulated only weak NLRP3-dependent IL-1β production from murine neutrophils, suggesting that lysosomal rupture is not a strong stimulus for NLRP3 activation in neutrophils. We validated our in vitro findings for poor neutrophil NLRP3 responses to particles in vivo, where we demonstrated that neutrophils do not significantly contribute to alum-induced IL-1β production in mice. In all, our studies highlight that myeloid cell identity and the nature of the danger signal can strongly influence signalling by a single PRR, thus shaping the nature of the resultant immune response.

journal_name

Eur J Immunol

journal_title

European journal of immunology

authors

Chen KW,Bezbradica JS,Groß CJ,Wall AA,Sweet MJ,Stow JL,Schroder K

doi

10.1002/eji.201545943

subject

Has Abstract

pub_date

2016-04-01 00:00:00

pages

1004-10

issue

4

eissn

0014-2980

issn

1521-4141

journal_volume

46

pub_type

杂志文章

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