Inhibition of Apoptosis in Human Neutrophils by Helicobacter pylori Water-Soluble Surface Proteins

The granulocyte-specific monoclonal antibody, AHN-1, immunoprecipitates two major surface-iodinated proteins of 105,000 and 145,000 to 150,000 daltons from normal human neutrophils. In this study, the effect of AHN- 1 on a number of neutrophil functions was evaluated in vitro. Both complement- and antibody-mediated phagocytosis were inhibited when human neutrophils were pretreated with AHN-1 and opsonized bacteria were used as targets. The inhibition of phagocytosis was specific, in that lysosomal enzyme release and chemotaxis were not altered by treatment with AHN-1. AHN-1 did inhibit superoxide production by neutrophils in response to particulate stimuli, but not in response to the soluble stimulus, 12-O-tetradecanoylphorbol-13-acetate. The data indicate that one or both of these surface proteins may be important in the process of phagocytosis. AHN-1 should be useful in isolating and further characterizing the nature of these molecules.

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Impact of cagPAI and T4SS on the Inflammatory Response of Human Neutrophils to Helicobacter pylori Infection

PLoS ONE ◽

10.1371/journal.pone.0064623 ◽

2013 ◽

Vol 8 (6) ◽

pp. e64623 ◽

Cited By ~ 17

Author(s):

Norma Angélica Sánchez-Zauco ◽

Javier Torres ◽

Gloria Erandi Pérez-Figueroa ◽

Lourdes Álvarez-Arellano ◽

Margarita Camorlinga-Ponce ◽

...

Keyword(s):

Helicobacter Pylori ◽

Inflammatory Response ◽

Helicobacter Pylori Infection ◽

Human Neutrophils

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Comparison of CXC Chemokines ENA-78 and Interleukin-8 Expression in Helicobacter pylori-Associated Gastritis

Infection and Immunity ◽

10.1128/iai.69.1.81-88.2001 ◽

2001 ◽

Vol 69 (1) ◽

pp. 81-88 ◽

Cited By ~ 29

Author(s):

Gabriele Rieder ◽

Wolfgang Einsiedl ◽

Rudolf A. Hatz ◽

Manfred Stolte ◽

Georg A. Enders ◽

...

Keyword(s):

Helicobacter Pylori ◽

Protein Expression ◽

Outer Membrane Proteins ◽

Water Soluble ◽

Interleukin 8 ◽

Gastric Epithelium ◽

Mrna Levels ◽

Rt Pcr ◽

H Pylori

ABSTRACT Colonization of the gastric mucosa with Helicobacter pylori is associated with a dense infiltration of granulocytes into the lamina propria in the active phase of gastritis. In this study, we investigated the involvement of epithelial cell-derived neutrophil-activating protein 78 (ENA-78) in development of H. pylori-associated gastritis. Antral biopsies from 27 patients with H. pylori-associated gastritis and 25 from H. pylori-negative individuals were first analyzed for ENA-78 and interleukin-8 (IL-8) mRNA by semiquantitative reverse transcription (RT)-PCR. In H. pylori-positive patients, significantly elevated levels were found for both chemokines (P < 0.05). Only IL-8 mRNA levels differed significantly (P< 0.05) in H. pylori-infected individuals who had serum antibodies for cytotoxin-associated protein CagA versus H. pylori-infected CagA-negative persons. Quantification of ENA-78 transcript levels by competitive RT-PCR yielded a significant 45-fold upregulation for ENA-78 transcripts in biopsies of H. pylori-positive versus H. pylori-negative patients (P < 0.05). In contrast to earlier findings with IL-8, the degree of ENA-78 mRNA upregulation was independent of the grade of activity of gastritis. Immunofluorescence studies on tissues of antral biopsies localized ENA-78 protein expression mainly to the gastric epithelium of H. pylori-positive patients, while control tissues were negative. Upregulation of ENA-78 and IL-8 mRNA and protein expression was also observed in an in vitro system using a gastric adenocarcinoma cell line. Only viable H. pyloriyielded a strong ENA-78 and IL-8 induction, while H. pyloriouter membrane proteins or water-soluble proteins had no significant effect. These data provide evidence for the importance of both IL-8 and ENA-78 in the development and perpetuation of H. pylori-associated gastritis.

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