| First Author | Jenne DE | Year | 1997 |
| Journal | FEBS Lett | Volume | 408 |
| Issue | 2 | Pages | 187-90 |
| PubMed ID | 9187364 | Mgi Jnum | J:40592 |
| Mgi Id | MGI:707940 | Doi | 10.1016/s0014-5793(97)00418-3 |
| Citation | Jenne DE, et al. (1997) Cloning and functional expression of the murine homologue of proteinase 3: implications for the design of murine models of vasculitis. FEBS Lett 408(2):187-90 |
| abstractText | Anti-neutrophil cytoplasmic autoantibodies recognizing conformational epitopes (c-ANCA) of proteinase 3 (PR3) from azurophil granules are a diagnostic hallmark in Wegener's granulomatosis (WG). Because a functional PR3 homologue has not been identified in rodents, it is difficult to assess immunopathological responses in rats or mice immunized with patients' derived c-ANCA or human PR3. Here we report the full length cDNA cloning and functional expression of murine PR3 in HMC-1 cells. Recombinant murine PR3 shows highly similar substrate specificities towards synthetic peptides and is inhibited by human alpha1-proteinase inhibitor like human PR3. However, neither human c-ANCA, rabbit sera nor mouse monoclonal antibodies to human PR3 recognize the murine homologue. Consequently, it is unlikely that disease observed in mice after immunization with c-ANCA or human PR3 is caused by pathogenic antibodies directed against mouse PR3. Recombinant human-mouse chimaeric variants will be a valuable new tool to localize the disease-specific immunodominant epitopes in human PR3. |
