In vitro experiments using gastric tumor cell lines, murine models and one clinical study provided evidence for a potential role of PAR2 in Helicobacter pylori-induced gastritis. Aim:  To investigate PAR2 expression in H. pylori-infected patients and correlation with proinflammatory IL-8, IL-1β as well as histologic changes of the mucosa. Furthermore, PAR2 expression was studied in context to mucosal selleck screening library amounts of secretory leukocyte protease inhibitor (SLPI), a putative

regulator of PAR2. Methods:  Twenty-two H. pylori-infected patients and 72 H. pylori-negative subjects underwent upper GI endoscopy. In antrum-derived mucosal biopsies, PAR2, IL-1β, Sirolimus mw IL-8, and SLPI expression was analyzed by quantitative RT-PCR, and in part by ELISA and immunohistochemistry. Histopathologic evaluation of gastritis was performed according to the updated Sydney classification. Results: IL-8 gene expression was 5-fold increased in the mucosa of H. pylori-infected patients compared with

non-infected (p < .0001), whereas no differences for PAR2 and IL-1β mRNA amounts were observed between both groups. PAR2 gene expression correlated positively with transcript levels of IL-8, IL-1β as well mucosal SLPI levels in H. pylori-infected patients (r: 0.47–0.84; p < .0001), whereas no correlation was found with the degree of gastritis. Conclusions:  PAR2 represents an additive pathway of IL-8 secretion and proinflammatory effects in H. pylori-induced gastritis. Reduced SLPI

levels leading to higher serine protease activities in the mucosa of infected subjects might regulate PAR2 activation. “
“Background:  High-molecular-weight cell-associated proteins (HM-CAP) assay is the most popular serological immunoassay worldwide and has been developed from US isolates as the antigens. The accuracy is reduced when the sera are from adults and children in East Asia including MCE Japan. To overcome the reduced accuracy, an enzyme immunoassay using Japanese strain–derived HM-CAP (JHM-CAP) was developed, in which the antigens were prepared by exactly the same procedure as HM-CAP. The performance of JHM-CAP was better than that of HM-CAP in Japanese adults as well as in children. The higher sensitivity was because of the presence of 100-kDa protein that was absent in the preparation of HM-CAP antigen. Materials and Methods:  Immunoblot analysis and peptide mass fingerprinting methods were used to identify the distinctive 100-kDa protein present in JHM-CAP antigens. The peptide sequence and identification were analyzed by Mascot Search on the database of Helicobacter pylori. The identified protein was confirmed by immunoblot with a specific antibody and inhibition assay by the sera.