IL-33 induction and signaling are controlled by glutaredoxin-1 in mouse macrophages

PLoS One. 2019 Jan 25;14(1):e0210827. doi: 10.1371/journal.pone.0210827. eCollection 2019.

Abstract

Interleukin (IL)-33 is an interleukin-1 like cytokine that enhances Th2 responses and mediates mucosal immunity and allergic inflammation but the mechanism regulating endogenous IL-33 production are still under investigation. In macrophages, lipopolysaccharide (LPS) administration resulted in marked induction of IL-33 mRNA that was blunted in macrophages from glutaredoxin-1 (Glrx) knockout mice and in RAW264.7 macrophages with Glrx knockdown by siRNA. Glutaredoxin-1 is a small cytosolic thioltransferase that controls a reversible protein thiol modification, S-glutationylation (protein-GSH adducts), thereby regulating redox signaling. In this study, we examined the mechanism of Glrx regulation of endogenous IL-33 induction in macrophages. Glrx knockdown resulted in impaired de-glutathionylation of TRAF6, which is required for TRAF6 activation, and inhibited downstream IKKβ and NF-κB activation. Inhibitors of NF-κB suppressed IL-33 induction and chromatin IP sequencing data analysis confirmed that IL-33 is an NF-κB-responsive gene. Since TRAF6-NF-κB activation is also essential for IL-33 signaling through its receptor, ST2L, we next tested the involvement of Glrx in exogenous IL-33 responses in RAW264.7 cells. Recombinant IL-33 (rIL-33) administration induced IL-33 mRNA expression in RAW264.7 macrophages, and this was inhibited by Glrx knockdown. Interestingly, rIL-33-induced IL-33 protein was identified as the 20 kDa cleaved form whereas LPS-induced IL-33 protein was identified as full-length IL-33, which may be less active than the cleaved form. In a clinically-relevant mouse model of asthma, intra-tracheal cockroach antigen treatment induced Glrx protein in wild type mouse lungs but Glrx induction was attenuated in IL-33 knockout mouse lungs, suggesting that IL-33 may regulate Glrx induction in vivo in response to allergen challenge. In summary, our data reveal a novel mechanism by which Glrx controls both LPS- and IL-33-mediated NF-κB activation leading to IL-33 production, and paracrine IL-33 can induce Glrx to further regulate inflammatory reactions.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Allergens / administration & dosage
  • Animals
  • Asthma / etiology
  • Asthma / immunology
  • Asthma / metabolism
  • Disease Models, Animal
  • Gene Expression / drug effects
  • Gene Knockdown Techniques
  • Glutaredoxins / deficiency
  • Glutaredoxins / genetics
  • Glutaredoxins / metabolism*
  • Glutathione / metabolism
  • Interleukin-33 / biosynthesis*
  • Interleukin-33 / genetics*
  • Lipopolysaccharides / pharmacology
  • Lung / immunology
  • Lung / metabolism
  • Macrophages / drug effects
  • Macrophages / immunology*
  • Macrophages / metabolism*
  • Mice
  • Mice, Knockout
  • NF-kappa B / metabolism
  • RAW 264.7 Cells
  • RNA, Messenger / genetics
  • RNA, Messenger / metabolism
  • RNA, Small Interfering / genetics
  • Signal Transduction
  • TNF Receptor-Associated Factor 6 / metabolism

Substances

  • Allergens
  • Glrx protein, mouse
  • Glutaredoxins
  • Il33 protein, mouse
  • Interleukin-33
  • Lipopolysaccharides
  • NF-kappa B
  • RNA, Messenger
  • RNA, Small Interfering
  • TNF Receptor-Associated Factor 6
  • TRAF6 protein, mouse
  • allergen CRa, cockroach
  • Glutathione