Characterization of a recombinant proteinase 3, the autoantigen in Wegener's granulomatosis and its reactivity with anti-neutrophil cytoplasmic autoantibodies.
FEBS Lett
; 382(1-2): 130-6, 1996 Mar 11.
Article
en En
| MEDLINE
| ID: mdl-8612734
ABSTRACT
Using the baculovirus/insect cells system, we have expressed a recombinant proteinase 3 (PR3) -- the neutrophil-derived serine protease autoantigen in Wegener's granulomatosis -- as a glycosylated intracellular and membrane-associated protein. Oligosaccharides accounted for the difference in molecular weights between recombinant (34 kDa) and neutrophil-PR3 (29 kDa). Whereas rabbit-anti-PR3 IgG recognized both recombinant and neutrophil-derived PR3, autoantibodies from Wegener patient sera recognized only neutrophil-derived PR3. Although oligosaccharides were not involved in PR3 epitope recognition, autoantibodies did not recognize the amino acid primary structure of recombinant PR3. Improper disulfide bond formation and/or lack of post-translational events in insect cells, may affect the conformation and/or lack of post-translational events in insect cells, may affect the conformation of PR3, precluding its reactivity with sera from WG patients.
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Banco de datos:
MEDLINE
Asunto principal:
Autoanticuerpos
/
Autoantígenos
/
Serina Endopeptidasas
/
Granulomatosis con Poliangitis
Límite:
Animals
/
Humans
Idioma:
En
Año:
1996
Tipo del documento:
Article