Myeloperoxidase binds to vascular endothelial cells, is recognized by ANCA and can enhance complement dependent cytotoxicity

Adv Exp Med Biol. 1993;336:121-3. doi: 10.1007/978-1-4757-9182-2_20.

Abstract

Myeloperoxidase (MPO) and proteinase-3 (Pr-3) can bind to vascular endothelial cells (EC) and are available for recognition by autoantibodies present in P-ANCA or C-ANCA containing sera, respectively. The bound MPO also retains its enzymic functions and effectively interacts with hydrogen peroxide to mediate detachment of endothelial cells from their substratum. EC bound MPO-anti-MPO complexes can contribute to the complement-dependent EC injury demonstrated by some P-ANCA sera.

MeSH terms

  • Antibodies, Antineutrophil Cytoplasmic
  • Autoantibodies / immunology*
  • Cells, Cultured
  • Complement System Proteins / immunology
  • Cytotoxicity, Immunologic*
  • Endothelium, Vascular / drug effects
  • Endothelium, Vascular / enzymology*
  • Endothelium, Vascular / immunology
  • Humans
  • Hydrogen Peroxide / pharmacology
  • Immunoglobulin G / pharmacology
  • Peroxidase / immunology
  • Peroxidase / pharmacology
  • Peroxidase / physiology*

Substances

  • Antibodies, Antineutrophil Cytoplasmic
  • Autoantibodies
  • Immunoglobulin G
  • Complement System Proteins
  • Hydrogen Peroxide
  • Peroxidase