Extracellular signal-regulated kinase induces phosphorylation of IkappaBalpha in Helicobacter pylori-infected gastric epithelial AGS cells

Inflammopharmacology. 2007 Feb;15(1):26-30. doi: 10.1007/s10787-006-1547-z.

Abstract

In Helicobacter pylori (H. pylori)-induced gastric ulceration, NF-kappaB regulates the expression of inflammatory genes. NF-kappaB is activated by phosphorylation of its endogenous inhibitor, IkappaBalpha. The possible involvement of mitogen-activated protein kinase (MAPK) on NF-kappaB activation has been suggested in various cells. Present study aims to investigate whether H. pylori in a Korean isolate induces phosphorylation of IkappaBalpha and whether H. pylori-induced phosphorylation of IkappaBalpha is mediated by MAPK in gastric epithelial AGS cells. AGS cells were treated with MAPK inhibitors (U0126 for extracellular signal-regulated kinase, SB203580 for p38 kinase, SP600125 for c-Jun NH2-terminal protein kinases) and stimulated with H. pylori. As a result, H. pylori increased phospho-specific IkappaBalpha accompanied with the decrease in control IkappaBalpha. H. pylori-induced phosphorylation of IkappaBalpha was inhibited by treatment of U0126, but not by SB203580 or SP600125. In conclusion, extracellular signal-regulated kinase induces phosphorylation of IkappaBalpha in H. pylori-infected AGS cells.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Proteins / metabolism
  • Cell Line, Tumor
  • DNA, Bacterial*
  • Epithelial Cells / enzymology
  • Gastric Mucosa / enzymology
  • Helicobacter Infections / pathology*
  • Helicobacter pylori / pathogenicity*
  • Humans
  • I-kappa B Kinase / metabolism*
  • Mitogen-Activated Protein Kinases / metabolism*
  • NF-kappa B / metabolism*
  • Phosphorylation

Substances

  • Bacterial Proteins
  • DNA, Bacterial
  • NF-kappa B
  • I-kappa B Kinase
  • Mitogen-Activated Protein Kinases