Endosomal NADPH-oxidase is critical for induction of the tissue factor gene in monocytes and endothelial cells. Lessons from the antiphospholipid syndrome

Thromb Haemost. 2013 Mar;109(3):525-31. doi: 10.1160/TH12-06-0421. Epub 2013 Jan 17.

Abstract

Antiphospholipid antibodies (aPL) have been shown to induce tissue factor (TF) expression in monocytes and endothelial cells. However, the underlying signal transduction has been more or less elusive in the past. We have recently shown that aPL enter the lysosomal route in monocytes and dendritic cells, and subsequently activate endosomal NADPH-oxidase (NOX). The generation of superoxide which is dismutated to hydrogen peroxide upregulates the intracellular toll like receptors (TLR) 7 and 8, and leads to robust production of inflammatory cytokines. Here we show that induction of TF by aPL follows the same signaling pathway. Inhibition of endosomal NOX by the anion channel blocker niflumic acid or capture of superoxide by the radical scavenger N-acetylcysteine blocks TF induction by aPL. Furthermore, monocytes from mice deficient in NOX2 do not increase TF surface expression in response to aPL, while cells from mice deficient in glutathione peroxidase-1 (GPx-1) show an increased response. Unexpectedly, also induction of TF by tumour necrosis factor (TNF)α and lipopolysaccharide (LPS) was strongly dependent on the activation of endosomal NOX. While TNFα apparently depends alm ost fully on endosomal NOX, signalling of LPS is only partially dependent on this pathway. These data provide further insight into the well-known role of reactive oxygen species in the induction of TF expression and suggest that endosomal signalling may represent a central coordinating point in this process.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acetylcysteine / pharmacology
  • Animals
  • Antiphospholipid Syndrome / metabolism*
  • Endosomes / metabolism*
  • Endothelial Cells / cytology*
  • Female
  • Free Radical Scavengers / pharmacology
  • Glutathione Peroxidase / genetics
  • Glutathione Peroxidase GPX1
  • Human Umbilical Vein Endothelial Cells
  • Humans
  • Hydrogen Peroxide / metabolism
  • Lipopolysaccharides / metabolism
  • Membrane Glycoproteins / genetics
  • Mice
  • Mice, Inbred C57BL
  • Monocytes / cytology*
  • NADPH Oxidase 2
  • NADPH Oxidases / genetics
  • NADPH Oxidases / metabolism*
  • Niflumic Acid / metabolism
  • Superoxides / metabolism
  • Thromboplastin / genetics*
  • Thromboplastin / metabolism*
  • Tumor Necrosis Factor-alpha / metabolism

Substances

  • Free Radical Scavengers
  • Lipopolysaccharides
  • Membrane Glycoproteins
  • Tumor Necrosis Factor-alpha
  • Superoxides
  • Niflumic Acid
  • Thromboplastin
  • Hydrogen Peroxide
  • Glutathione Peroxidase
  • Cybb protein, mouse
  • NADPH Oxidase 2
  • NADPH Oxidases
  • Acetylcysteine
  • Glutathione Peroxidase GPX1