Journal
FEBS JOURNAL
Volume 284, Issue 11, Pages 1712-1725Publisher
WILEY
DOI: 10.1111/febs.14075
Keywords
cathepsin G; elastase; IL-1 family; IL-1 alpha, IL-36; inflammation; NETs; neutrophil extracellular traps; protease
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Funding
- Science Foundation Ireland [14/IA/2622]
- Science Foundation Ireland (SFI) [14/IA/2622] Funding Source: Science Foundation Ireland (SFI)
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Activated neutrophils can undergo a mode of regulated cell death, called NETosis, that results in the extrusion of chromatin into the extracellular space, thereby acting as extracellular traps for microorganisms. Neutrophil-derived extracellular traps (NETs) 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 NETs 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 NETs could also serve as platforms for the activation of proinflammatory cytokines. Here, we show that neutrophil NETs potently processed and activated IL-1 as well as IL-36 subfamily cytokines through NET-associated Cat G and elastase. Thus, in addition to their role as antimicrobial traps, NETs can also act as local sites of cytokine processing and activation.
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