Myeloperoxidase binds to vascular endothelial cells, is recognized by ANCA and can enhance complement dependent cytotoxicity.
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.
Savage
C O
CO
Vascular Biology Section, Clinical Research Centre, Harrow, U.K.
Gaskin
G
G
Pusey
C D
CD
Pearson
J D
JD
D019268:Antibodies, Antineutrophil Cytoplasmic; D001323:Autoantibodies / Q000276:immunology*; D002478:Cells, Cultured; D003165:Complement System Proteins / Q000276:immunology; D003602:Cytotoxicity, Immunologic; D004730:Endothelium, Vascular / Q000187:drug effects / Q000201:enzymology* / Q000276:immunology; D006801:Humans; D006861:Hydrogen Peroxide / Q000494:pharmacology; D007074:Immunoglobulin G / Q000494:pharmacology; D009195:Peroxidase / Q000276:immunology / Q000494:pharmacology / Q000502:physiology*
D019268:Antibodies, Antineutrophil Cytoplasmic; D001323:Autoantibodies; D007074:Immunoglobulin G; D003165:Complement System Proteins; D006861:Hydrogen Peroxide; D009195:Peroxidase