A new approach to the molecular characterization of the c-ANCA antigen in Wegener's granulomatosis.
Classic anti-neutrophil cytoplasmic antibodies (c-ANCA) specific for constituents of neutrophil primary granules and monocyte lysosomes have been implicated in the pathogenesis of Wegener's Granulomatosis (WG). The revised amino-terminal sequence of Proteinase 3 (PR-3) as ANCA antigen, suggested that PR-3 is identical to myeloblastin (MBN). As it has been proposed that autoantibodies recognize a conformational epitope on c-ANCA, prokaryotic expressed protein might not be recognized by the patients sera. Therefore we set up an in vitro translation in an eukaryotic cell-free system using an internal ATG (amino acid 15 of the mature protein).
Bleil
L
L
Department of Medicine III, University of Erlangen-Nürnberg, FRG.
Winkler
T H
TH
Fehr
H K
HK
Bautz
E K
EK
Kalden
J R
JR
D019268:Antibodies, Antineutrophil Cytoplasmic; D000941:Antigens / Q000737:chemistry* / Q000235:genetics; D001323:Autoantibodies / Q000276:immunology*; D001483:Base Sequence; D001665:Binding Sites; D018076:DNA, Complementary / Q000737:chemistry; D014890:Granulomatosis with Polyangiitis / Q000276:immunology*; D006801:Humans; D007074:Immunoglobulin G / Q000276:immunology*; D007163:Immunosorbent Techniques; D008969:Molecular Sequence Data; D053146:Myeloblastin; D014176:Protein Biosynthesis; D012697:Serine Endopeptidases / Q000737:chemistry / Q000235:genetics
D019268:Antibodies, Antineutrophil Cytoplasmic; D000941:Antigens; D001323:Autoantibodies; D018076:DNA, Complementary; D007074:Immunoglobulin G; D012697:Serine Endopeptidases; D053146:Myeloblastin