Abstract
The neutrophil azurophil granule constituent proteinase 3 (PR3) is the principal antigen for anti-neutrophil cytoplasmic antibodies (ANCA) in Wegener's granulomatosis. The conformation of the mature PR3 enzyme results from intracellular post-translational processing. The nascent molecule undergoes proteolytic cleavage of the amino-terminal signal peptide and activation dipeptide and of a carboxy-terminal peptide extension. The conformation of PR3 is stabilized by four disulfide bonds and, to a lesser extent, by asparagine-linked glycosylation. Most anti-neutrophil cytoplasmic antibodies directed against proteinase 3 (PR3-ANCA) recognize conformational epitopes. The expression of recombinant PR3 has provided a better understanding of the significance of the various intracellular processing steps for enzymatic activity and recognition by PR3-ANCA.
Original language | English (US) |
---|---|
Pages (from-to) | 263-267 |
Number of pages | 5 |
Journal | Arthritis Research |
Volume | 2 |
Issue number | 4 |
DOIs | |
State | Published - 2000 |
Keywords
- Anti-neutrophil cytoplasmic antibodies
- Proteinase 3
- Recombinant proteins
ASJC Scopus subject areas
- Rheumatology