Helicobacter pylori infection and CagA protein translocation in human primary gastric epithelial cell culture.
BACKGROUND
Increasing evidence has shown that Helicobacter pylori CagA protein translocation into gastric epithelial cells plays an important role in the development of gastric inflammation and malignancy. Translocated CagA undergoes tyrosine phosphorylation in gastric adenocarcinoma cell line cells, and CagA involves disruption of cellular apical-junction complex in Madin-Darby canine kidney cells.


METHODS
To elucidate whether these events take place in normal human gastric epithelium, we infected human primary gastric epithelial cells with H. pylori.


RESULTS
Our results demonstrate that CagA protein was translocated into primary gastric epithelial cells and tyrosine phosphorylated. The translocated CagA induces cytoskeletal rearrangement and the disruption of tight junctions in primary gastric epithelial cells.


CONCLUSIONS
This study provides direct evidence of the modulation of gastric epithelial cells by CagA protein translocation, and advances our understanding of the pathogenesis of H. pylori infection.
Lai
Yo-Ping
YP
Department of Internal Medicine, National Taiwan University Hospital, Taipei, Taiwan.
Yang
Jyh-Chin
JC
Lin
Tzu-Zung
TZ
Lin
Jaw-Town
JT
Wang
Jin-Town
JT
D016475:3T3 Cells; D000818:Animals; D000942:Antigens, Bacterial / Q000378:metabolism*; D001426:Bacterial Proteins / Q000378:metabolism*; D045744:Cell Line, Tumor; D002478:Cells, Cultured; D004285:Dogs; D004847:Epithelial Cells / Q000382:microbiology*; D005753:Gastric Mucosa / Q000382:microbiology*; D016481:Helicobacter Infections / Q000382:microbiology; D016480:Helicobacter pylori / Q000378:metabolism*; D006801:Humans; D051379:Mice; D010766:Phosphorylation; D021381:Protein Transport; D019108:Tight Junctions / Q000378:metabolism
D000942:Antigens, Bacterial; D001426:Bacterial Proteins; C080866:cagA protein, Helicobacter pylori