Expression of Eotaxin in Gastric Epithelial Cells Stimulated with Helicobacter pylori Vacuolating Cytotoxin.
- Author:
Hyokhan PARK
1
;
Nam In KIM
;
Jung Mogg KIM
;
Joo Sung KIM
;
Yu Kyoung OH
;
Young Jeon KIM
;
Nayoung KIM
;
Hyun Chae JUNG
;
In Sung SONG
Author Information
- Publication Type:Original Article
- Keywords: Helicobacter pylori vacuolating cytotoxin; Eotaxin; STAT6
- MeSH: Binding Sites; Enzyme-Linked Immunosorbent Assay; Eosinophils; Epithelial Cells*; Gastric Mucosa; Helicobacter pylori*; Helicobacter*; Interleukin-4; Luciferases; Neutrophil Infiltration; Neutrophils; Plasmids; Up-Regulation
- From:Journal of Bacteriology and Virology 2006;36(1):11-20
- CountryRepublic of Korea
- Language:Korean
- Abstract: Helicobacter pylori-infected gastric mucosa is characterized by infiltration of various inflammatory cells such as neutrophils and eosinophils. Although several mechanisms for neutrophil infiltration are well known, there has been little known the role of eotaxin, which is a potent chemoattractant for eosinophils, on the inflammatory process of H. pylori infection. The present study was to investigate the mechanisms of eotaxin expression in gastric epithelial cells stimulated with H. pylori vacuolating cytotoxin (VacA). Stimulation with VacA purified from VacA+ H. pylori slightly increased eotaxin expression in MKN-45 gastric epithelial cells. In contrast, the combined stimulation with VacA and IL-4 synergistically increased the eotaxin expression as determined by quantitative RT-PCR and ELISA. In MKN-45 cells transfected with an eotaxin promoter-luciferase reporter plasmid, costimulation with VacA and IL-4 induced more luciferase activity than either VacA or IL-4 alone did. However, such up-regulation was significantly decreased in the cells transfected with luciferase reporter plasmid bearing an eotaxin promoter which has a mutation at STAT6 binding site. These results suggest that the up-regulation of eotaxin in VacA-stimulated gastric epithelial cells may be synergistically facilitated by IL-4 via a STAT6-dependent mechanism.
