Ectosomes released by polymorphonuclear neutrophils induce a MerTK-dependent anti-inflammatory pathway in macrophages

J Biol Chem. 2010 Dec 17;285(51):39914-21. doi: 10.1074/jbc.M110.126748. Epub 2010 Oct 19.

Abstract

At the earliest stage of activation, human polymorphonuclear neutrophils release vesicles derived directly from the cell surface. These vesicles, called ectosomes (PMN-Ect), expose phosphatidylserine in the outer membrane leaflet. They inhibit the inflammatory response of human monocyte-derived macrophages and dendritic cells to zymosan A (ZymA) and LPS and induce TGF-β1 release, suggesting a reprogramming toward a tolerogenic phenotype. The receptors and signaling pathways involved have not yet been defined. Here, we demonstrate that PMN-Ect interfered with ZymA activation of macrophages via inhibition of NFκB p65 phosphorylation and NFκB translocation. The MerTK (Mer receptor tyrosine kinase) and PI3K/Akt pathways played a key role in this immunomodulatory effect as shown using specific MerTK-blocking antibodies and PI3K inhibitors LY294002 and wortmannin. As a result, PMN-Ect reduced the transcription of many proinflammatory genes in ZymA-activated macrophages. In sum, PMN-Ect interacted with the macrophages by activation of the MerTK pathway responsible for down-modulation of the proinflammatory signals generated by ZymA.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Androstadienes / pharmacology
  • Cell-Derived Microparticles / metabolism*
  • Chromones / pharmacology
  • Humans
  • Inflammation / metabolism
  • Lipopolysaccharides / pharmacology
  • Macrophage Activation / drug effects
  • Macrophage Activation / physiology*
  • Macrophages / metabolism*
  • Morpholines / pharmacology
  • Neutrophils / metabolism*
  • Phosphatidylinositol 3-Kinases / metabolism
  • Phosphorylation / drug effects
  • Phosphorylation / physiology
  • Protein Kinase Inhibitors / pharmacology
  • Proto-Oncogene Proteins / metabolism*
  • Proto-Oncogene Proteins c-akt / metabolism
  • Receptor Protein-Tyrosine Kinases / metabolism*
  • Signal Transduction / drug effects
  • Signal Transduction / physiology
  • Transcription Factor RelA / metabolism
  • Transforming Growth Factor beta1 / metabolism
  • Wortmannin
  • Zymosan / pharmacology
  • c-Mer Tyrosine Kinase

Substances

  • Androstadienes
  • Chromones
  • Lipopolysaccharides
  • Morpholines
  • Protein Kinase Inhibitors
  • Proto-Oncogene Proteins
  • RELA protein, human
  • Transcription Factor RelA
  • Transforming Growth Factor beta1
  • 2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-one
  • Zymosan
  • Phosphatidylinositol 3-Kinases
  • MERTK protein, human
  • Receptor Protein-Tyrosine Kinases
  • c-Mer Tyrosine Kinase
  • Proto-Oncogene Proteins c-akt
  • Wortmannin