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Neutrophil extracellular traps can serve as platforms for processing and activation of IL ‐1 family cytokines
Author(s) -
Clancy Danielle M.,
Henry Conor M.,
Sullivan Graeme P.,
Martin Seamus J.
Publication year - 2017
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/febs.14075
Subject(s) - neutrophil extracellular traps , proteases , neutrophil elastase , extracellular , cathepsin g , proinflammatory cytokine , microbiology and biotechnology , elastase , chemistry , immunology , biology , inflammation , biochemistry , enzyme
Activated neutrophils can undergo a mode of regulated cell death, called NET osis, that results in the extrusion of chromatin into the extracellular space, thereby acting as extracellular traps for microorganisms. Neutrophil‐derived extracellular traps ( NET s) are comprised of DNA decorated with histones, antimicrobial proteins and neutrophil granule proteases, such as elastase and cathepsin G (Cat G). NET ‐associated factors are thought to enhance the antimicrobial properties of these structures and localisation of antimicrobial molecules on NET s may serve to increase their local concentration. Because neutrophil‐derived proteases have been implicated in the processing and activation of several members of the extended interleukin ( IL )‐1 family, we wondered whether neutrophil NET s could also serve as platforms for the activation of proinflammatory cytokines. Here, we show that neutrophil NET s potently processed and activated IL ‐1α as well as IL ‐36 subfamily cytokines through NET ‐associated Cat G and elastase. Thus, in addition to their role as antimicrobial traps, NET s can also act as local sites of cytokine processing and activation.