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Biological activity of Helicobacter pylori components in mammalian cells: is it independent of proteinase-activated receptors?
Sekiguchi, F; Matsumoto, Y; Maeda, Y; Tsubota-Matsunami, M; Nishikawa, H; Kawabata, A.
Afiliación
  • Sekiguchi F; Division of Pharmacology and Pathophysiology, Kinki University School of Pharmacy, Higashi-Osaka, Japan.
J Physiol Pharmacol ; 63(6): 571-6, 2012 Dec.
Article en En | MEDLINE | ID: mdl-23388472
To clarify the relationship between Helicobacter pylori (H. pylori), a risk factor for gastritis, peptic ulcer and gastric cancer, and proteinase-activated receptors (PARs) that contribute to inflammatory responses, we determined and characterized the biological activity of H. pylori components in the mammalian cells that express PARs. The activity of H. pylori extracts was assessed in distinct cell lines with high expression of PAR1 (RGM1 cells), PAR2 (A549 cells), or PAR2 and PAR4 (HCT-15 cells). A PAR1-activating peptide (AP), but not H. pylori extracts, caused prostaglandin E2 (PGE2) release in RGM1 cells. On the other hand, H. pylori extracts produced release of PGE2 and interleukin-8 (IL-8) in A549 and HCT-15 cells, respectively, as a PAR2-AP did. The activity of H. pylori extracts in A549 cells was not affected by a proteinase inhibitor or exposure to boiling, but abolished by inhibitors of lipopolysaccharide (LPS), IRAK-1/4 or NF-κB. The activity of H. pylori extracts in HCT-15 cells was partially suppressed by boiling or the proteinase inhibitor. In rat platelets that express PAR4 and PAR3, like a PAR4-AP, H. pylori extracts induced aggregation when assessed in platelet rich plasma, an effect unaffected by the proteinase inhibitor, but did not cause aggregation of washed rat platelets that responded to the PAR4-AP or thrombin. The present study thus shows the biological activities of H. pylori extracts in A549 and HCT-15 cells or rat platelets, and suggests that they are not mediated by any PAR-activating proteinases, but may involve the other pathogenic factors including LPS.
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Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Helicobacter pylori / Receptores Proteinasa-Activados Tipo de estudio: Risk_factors_studies Límite: Animals / Humans / Male Idioma: En Revista: J Physiol Pharmacol Asunto de la revista: FARMACOLOGIA / FISIOLOGIA Año: 2012 Tipo del documento: Article País de afiliación: Japón Pais de publicación: Polonia
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Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Helicobacter pylori / Receptores Proteinasa-Activados Tipo de estudio: Risk_factors_studies Límite: Animals / Humans / Male Idioma: En Revista: J Physiol Pharmacol Asunto de la revista: FARMACOLOGIA / FISIOLOGIA Año: 2012 Tipo del documento: Article País de afiliación: Japón Pais de publicación: Polonia