Role of saliva proteinase 3 in dental caries

Salivary analysis can be used to assess the severity of caries. Of the known salivary proteins, a paucity of information exists concerning the role of proteinase 3（PR3）, a serine protease of the chymotrypsin family, in dental caries. Whole, unstimulated saliva was collected from children with varying degrees of active caries and tested using a Human Protease Array Kit and an enzyme-linked immunosorbent assay.A significantly decreased concentration of salivary PR3 was noted with increasing severity of dental caries（P,0.01）; a positive correlation（r50.87; P,0.01; Pearson’s correlation analysis） was also observed between salivary p H and PR3 concentration. In an antibacterial test,a PR3 concentration of 250 ng？m L21 or higher significantly inhibited Streptococcus mutans UA159 growth after 12 h of incubation（P,0.05）. These studies indicate that PR3 is a salivary factor associated with the severity of dental caries, as suggested by the negative relationship between salivary PR3 concentration and the severity of caries as well as the susceptibility of S. mutans to PR3.

Epitope mapping on Wegener's granulomatosis autoantigen proteinase 3

Abstract:Objective To map the epitopes on Wegener's granulomatosis autoantigen proteinase 3.Methods Antigenicity of proteinase 3 was studied with Western blot analysis in which proteinase 3 was prepared under reducing and non-reducing conditions. Two anti-proteinase 3 monoclonal antibodies, HZ1F12 and HZ1H3, were used to inhibit each other and to inhibit 22 anti-proteinase 3 positive sera from patients with Wegener's granulomatosis in competitive inhibition enzyme-linked immunosorbent assays (ELISA) and Western blot analysis. Results All monoclonal antibodies and patient sera recognized proteinase 3 under non-reducing conditions in Western blot analysis. HZ1F12 was inhibited 74% by HZ1H3. 10/22 (46%) sera were completely or partially inhibited by HZ1F12; 9/22 (41%) sera were partially inhibited by HZ1H3; and 6/22 (27%) were inhibited by both monoclonal antibodies. In inhibition Western blot analysis, the binding of patient sera to proteinase 3 could be inhibited by HZ1F12. Conclusions The epitopes of Wegener's granulomatosis autoantigen were conformational. Anti-proteinase 3 monoclonal HZ1F12 and HZ1H3 recognized similar or overlapping epitopes on the proteinase 3 molecule. Epitopes of proteinase 3 recognized by anti-proteinase 3 positive sera were not restricted.

"Triple-positive" renal limited vasculitis presenting with rapidly progressive glomerulonephritis: A case report

Rationale:Coexistence of anti-glomerular basement membrane(anti-GBM)disease with anti-neutrophil cytoplasmic antibody(ANCA)in a case of glomerulonephritis is often identified as a"double-positive"disease.Interestingly,the majority of"double positive"ANCA is myeloperoxidase(MPO)-ANCA and some of the MPO-ANCA positive cases showed intrarenal arteritis,suggesting an ANCA-associated kidney lesion.Proteinase 3-ANCA positive diseases are also rarely reported.Patients positive for all three antibodies,i.e.,triple-positive patients,are extremely rare.Patient's Concern:A 53 year-old female presented with anasarca and oliguria of 2 months'duration.Diagnosis:Pauci-immune type renal limited crescentic glomerulonephritis positive for MPO-ANCA,proteinase 3-ANCA,and anti-GBM antibody(triple-positive).Interventions:Intravenous high dose cyclophosphamide,oral azathioprine,intravenous methylprednisolone,and plasma exchange as per British Health Professionals in Rheumatology Guidelines.Outcomes:After one-month follow-up,anasarca and proteinuria were lessened,serum creatinine was normalized,titers of MPO-ANCA levels were decreased,and anti-GBM antibody levels were normalized.Lessons:Triple-positive renal limited vasculitis is rare and response to combined immunosuppressive therapy and plasma exchange can contribute to successful remission.