Helicobacter pylori induces an increase in inositol phosphates in cultured epithelial cells

• Published in: FEMS microbiology letters Vol. 129; no. 2-3; p. 293
• Main Authors: Pucciarelli, M G, Ruschkowski, S, Trust, T J, Finlay, B B
• Format: Journal Article
• Language: English
• Published: England 15-06-1995
• Subjects: Cell Line; Cytoskeleton - metabolism; Epithelium - metabolism; Epithelium - microbiology; Epithelium - pathology; Helicobacter pylori - metabolism; Humans; Inositol Phosphates - biosynthesis; Signal Transduction
• ISSN: 0378-1097
• DOI: 10.1111/j.1574-6968.1995.tb07595.x

Helicobacter pylori is a bacterial pathogen of humans that infects the gastric mucosa. This infection has been associated with gastritis, peptic ulcers, and gastric carcinomas. Diverse in vitro studies have described efficient adherence of H. pylori to different types of epithelial cells. Because of its varied effects on host cells, we have analysed signal transduction events in H. pylori-infected epithelial cells. Our results show that H. pylori induces an increase in inositol phosphates in all cultured epithelial cells used, including HeLa, Henle 407, Hep-2, and the human gastric adenocarcinoma cell line AGS. Bacterial growth medium supernatants induce a similar response in the host cell. The increase in inositol phosphates is not related to redistribution of cytoskeletal proteins such as actin or alpha-actinin nor tyrosine-phosphorylation of host cell proteins. The inositol phosphate increase is also observed in cells infected with low or non-adherent H. pylori mutants or mutants defective in the vacuolating toxin or urease holoenzyme. These results indicate that inositol phosphate release in H. pylori-infected cells is not dependent on bacterial adherence, and that a soluble bacterial factor, but not the vacuolating toxin or urease holoenzyme, mediates such an effect.