title: Helicobacter pylori lipopolysaccharide hinders polymorphonuclear leucocyte apoptosis.
abstract: A prominent histologic feature of Helicobacter pylori infection is a dense infiltration of polymorphonuclear leukocytes (PMNL) in gastric mucosa. H. pylori lipopolysaccharide (LPS) has been recognized as a primary virulence factor evoking acute mucosal inflammatory reaction. Previous works have shown that H. pylori LPS immunologic activities are lower than those of enterobacterial LPS. However, the effect of H. pylori LPS on spontaneous PMNL apoptosis, and mechanisms by which this H. pylori LPS may promote PMNL survival remain to be established. In this study, we investigated, by both morphologic and biochemical approaches, the action of H. pylori LPS on PMNL apoptosis in vitro, using broth culture filtrates (BCF) of H. pylori strains with different genotypes. We found that BCF from H. pylori caused a significant delay in spontaneous PMNL apoptosis and this delay was independent of the VacA, cag pathogenicity island and urease status. We demonstrated that LPS in BCF is responsible for this effect because it was abrogated by the LPS antagonist B287 (a synthetic analog of Rhodobactersphaeroides lipid A). Moreover, BCF from H. pylori induced P42/44MAP kinase activation in PMNL. Similar results were obtained with BCF of an Escherichia coli strain. Taken together these data suggest that longer survival of PMNL induced by H. pylori LPS may increase gastric epithelium injury in H. pylori-associated diseases.
authors: Laboratoire d'Anatomie-Pathologique, Faculté de Médecine, Nice, France.
authors: V
authors: V
authors: Hofman
authors: V
authors: V
authors: Ricci
authors: B
authors: B
authors: Mograbi
authors: P
authors: P
authors: Brest
authors: F
authors: F
authors: Luciano
authors: P
authors: P
authors: Boquet
authors: B
authors: B
authors: Rossi
authors: P
authors: P
authors: Auberger
authors: P
authors: P
authors: Hofman
mesh_terms: D017209:Apoptosis / Q000276:immunology*; D053148:Caspase 3; D053181:Caspase 8; D053453:Caspase 9; D020169:Caspases / Q000378:metabolism; D002478:Cells, Cultured; D017077:Culture Media, Conditioned / Q000494:pharmacology; D004269:DNA, Bacterial / Q000032:analysis; D004789:Enzyme Activation / Q000276:immunology; D004792:Enzyme Precursors / Q000378:metabolism; D016481:Helicobacter Infections / Q000276:immunology / Q000473:pathology*; D016480:Helicobacter pylori / Q000235:genetics / Q000472:pathogenicity*; D006801:Humans; D020287:In Situ Nick-End Labeling; D008070:Lipopolysaccharides / Q000276:immunology*; D019950:Mitogen-Activated Protein Kinase 1 / Q000378:metabolism; D048052:Mitogen-Activated Protein Kinase 3; D020928:Mitogen-Activated Protein Kinases / Q000378:metabolism; D009504:Neutrophils / Q000166:cytology* / Q000201:enzymology / Q000276:immunology; D014774:Virulence
chemical_list: D017077:Culture Media, Conditioned; D004269:DNA, Bacterial; D004792:Enzyme Precursors; D008070:Lipopolysaccharides; D019950:Mitogen-Activated Protein Kinase 1; D048052:Mitogen-Activated Protein Kinase 3; D020928:Mitogen-Activated Protein Kinases; C505407:CASP3 protein, human; C505530:CASP8 protein, human; C506433:CASP9 protein, human; D053148:Caspase 3; D053181:Caspase 8; D053453:Caspase 9; D020169:Caspases