The extra domain A of fibronectin activates Toll-like receptor 4

J Biol Chem. 2001 Mar 30;276(13):10229-33. doi: 10.1074/jbc.M100099200. Epub 2001 Jan 9.

Abstract

Cellular fibronectin, which contains an alternatively spliced exon encoding type III repeat extra domain A (EDA), is produced in response to tissue injury. Fragments of fibronectin have been implicated in physiological and pathological processes, especially tissue remodeling associated with inflammation. Because EDA-containing fibronectin fragments produce cellular responses similar to those provoked by bacterial lipopolysaccharide (LPS), we examined the ability of recombinant EDA to activate Toll-like receptor 4 (TLR4), the signaling receptor stimulated by LPS. We found that recombinant EDA, but not other recombinant fibronectin domains, activates human TLR4 expressed in a cell type (HEK 293 cells) that normally lacks this Toll-like receptor. EDA stimulation of TLR4 was dependent upon co-expression of MD-2, a TLR4 accessory protein. Unlike LPS, the activity of EDA was heat-sensitive and persisted in the presence of the LPS-binding antibiotic polymyxin B and a potent LPS antagonist, E5564, which completely suppressed LPS activation of TLR4. These observations provided a mechanism by which EDA-containing fibronectin fragments promote expression of genes involved in the inflammatory response.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Animals
  • Anti-Bacterial Agents / pharmacology
  • Antigens, Surface / metabolism
  • Blotting, Western
  • Cell Line
  • Dose-Response Relationship, Drug
  • Drosophila Proteins*
  • Enzyme Activation
  • Exons
  • Fibronectins / chemistry*
  • Fibronectins / metabolism*
  • Hot Temperature
  • Humans
  • Inflammation
  • Interleukin-10 / biosynthesis
  • Lipid A / analogs & derivatives*
  • Lipid A / pharmacology
  • Lipopolysaccharides / antagonists & inhibitors
  • Lipopolysaccharides / pharmacology
  • Lymphocyte Antigen 96
  • Matrix Metalloproteinase 9 / metabolism
  • Membrane Glycoproteins / metabolism*
  • Mice
  • Mice, Inbred C3H
  • Plasmids / metabolism
  • Polymyxin B / pharmacology
  • Protein Structure, Tertiary
  • Receptors, Cell Surface / metabolism*
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / metabolism
  • Reverse Transcriptase Polymerase Chain Reaction
  • Signal Transduction
  • Spleen / cytology
  • Time Factors
  • Toll-Like Receptor 4
  • Toll-Like Receptors
  • Transfection

Substances

  • Anti-Bacterial Agents
  • Antigens, Surface
  • Drosophila Proteins
  • E5564
  • Fibronectins
  • LY96 protein, human
  • Lipid A
  • Lipopolysaccharides
  • Lymphocyte Antigen 96
  • Membrane Glycoproteins
  • Receptors, Cell Surface
  • Recombinant Proteins
  • TLR4 protein, human
  • Toll-Like Receptor 4
  • Toll-Like Receptors
  • Interleukin-10
  • Matrix Metalloproteinase 9
  • Polymyxin B