Cutting Edge: Blockade of Inhibitor of Apoptosis Proteins Sensitizes Neutrophils to TNF- but Not Lipopolysaccharide-Mediated Cell Death and IL-1β Secretion.

Details

Serval ID
serval:BIB_849FCC274A42
Type
Article: article from journal or magazin.
Collection
Publications
Title
Cutting Edge: Blockade of Inhibitor of Apoptosis Proteins Sensitizes Neutrophils to TNF- but Not Lipopolysaccharide-Mediated Cell Death and IL-1β Secretion.
Journal
Journal of immunology
Author(s)
Chen K.W., Lawlor K.E., von Pein J.B., Boucher D., Gerlic M., Croker B.A., Bezbradica J.S., Vince J.E., Schroder K.
ISSN
1550-6606 (Electronic)
ISSN-L
0022-1767
Publication state
Published
Issued date
15/05/2018
Peer-reviewed
Oui
Volume
200
Number
10
Pages
3341-3346
Language
english
Notes
Publication types: Journal Article
Publication Status: ppublish
Abstract
The mammalian inhibitor of apoptosis proteins (IAPs) are key regulators of cell death and inflammation. A major function of IAPs is to block the formation of a cell death-inducing complex, termed the ripoptosome, which can trigger caspase-8-dependent apoptosis or caspase-independent necroptosis. Recent studies report that upon TLR4 or TNF receptor 1 (TNFR1) signaling in macrophages, the ripoptosome can also induce NLRP3 inflammasome formation and IL-1β maturation. Whether neutrophils have the capacity to assemble a ripoptosome to induce cell death and inflammasome activation during TLR4 and TNFR1 signaling is unclear. In this study, we demonstrate that murine neutrophils can signal via TNFR1-driven ripoptosome assembly to induce both cell death and IL-1β maturation. However, unlike macrophages, neutrophils suppress TLR4-dependent cell death and NLRP3 inflammasome activation during IAP inhibition via deficiencies in the CD14/TRIF arm of TLR4 signaling.
Pubmed
Web of science
Create date
22/09/2018 19:57
Last modification date
21/08/2019 5:33
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