Tu1932 Endoscopic Features of Food Protein-Induced Proctocolitis in Neonates and Infants

Abstract

Background and aim: Intestinal-type gastric carcinomas progress through chronic inflammation and atrophic gastritis. Heat shock protein 27(HSP27), a stress-induced molecular chaperone, inhibit reactive oxygen species (ROS) accumulation. In previous reports have been suggested that HSP27 plays an important role in inflammation and carcinogenesis. We investigated HSP27 expression in gastric neoplasia and background gastric mucosa to assess its involvement in gastric carcinogenesis. Methods:We used real-time quantitative polymerase chain reaction to examine HSP27 expression in gastric neoplasias and in gastric mucosae of 30 patients with intraepithelial neoplasias and in gastric mucosae of 30 patients without gastric neoplasia. Immunohistochemical staining was performed on 30 advanced gastric cancer tissues. Results: HSP27 expression was negatively associated with atrophic gastritis. HSP27 expression in the background gastric mucosa of those without gastric neoplasia(P= 0.004).In tumor necrosis factor -treated gastric cancer cell,HSP27 knockdown increased cell death and ROS accumulation that link inflammation to cancer. Poorly differentiated tumors most frequently had high HSP27 levels. Dedifferentiated of cancer cells is associated with an epithelial-mesenchymal transition signaling pathway. In gastric cancer MKN-1 cells, HSP27 knockdown upregulated E-cadherin and downregulated vimentin and smooth muscle actin, but this did not occur in MKN-74 cells. Conclusion: HSP27 expression in gastric mucosae is negatively correlated with intraepithelial neoplasia, a probable precursor to gastric cancer and HSP27 expression in cancer is positively correlated with poor differentiation.