Open AccessInduction of host signal transduction pathways by Helicobacter pylori
Author(s) -
E. Segal,
Cleston C. Lange,
Antonello Covacci,
Lucy S. Tompkins,
Stanley Falkow
Publication year - 1997
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.94.14.7595
Subject(s) - helicobacter pylori , tyrosine phosphorylation , phosphorylation , biology , signal transduction , phosphoprotein , tyrosine kinase , tyrosine , microbiology and biotechnology , biochemistry , genetics
Adherence ofHelicobacter pylori to cultured gastric epithelial cells is associated with several cellular events, including the tyrosine phosphorylation of a 145-kDa host protein; the reorganization of the host cell actin and associated cellular proteins, like vasodilator-stimulated phosphoprotein, adjacent to the attached bacterial cell; and the subsequent release of the cytokine, interleukin 8 (IL-8).H. pylori isolated from patients with ulcer disease and gastric cancer contain a DNA insertion, the cag pathogenicity island (PAI), that is not present in bacteria isolated from individuals with asymptomatic infection. Mutations in a number of PAI genes abolish tyrosine phosphorylation and IL-8 synthesis but not the cytoskeletal rearrangements. Kinase inhibition studies suggest there are two distinct pathways operative in stimulating IL-8 release from host cells and one of theseH. pylori pathways is independent of the tyrosine phosphorylation step.