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  • Title: Proinflammatory activity of a cecropin-like antibacterial peptide from Helicobacter pylori.
    Author: Bylund J, Christophe T, Boulay F, Nyström T, Karlsson A, Dahlgren C.
    Journal: Antimicrob Agents Chemother; 2001 Jun; 45(6):1700-4. PubMed ID: 11353614.
    Abstract:
    Helicobacter pylori, the bacterial pathogen associated with gastritis and peptic ulcers, is highly successful in establishing infection in the human gastric mucosa, a process typically associated with massive infiltration of inflammatory cells. Colonization of the mucosa is suggested to be facilitated by H. pylori-produced cecropin-like peptides with antibacterial properties, giving the microbe a competitive advantage over other bacteria. We show that a cecropin-like antibacterial peptide from H. pylori, Hp(2-20), not only has a potent bactericidal effect but also induces proinflammatory activities in human neutrophils, e.g., upregulation of integrins (Mac-1), induction of chemotaxis, and activation of the oxygen radical producing NADPH-oxidase. Furthermore, we show that these effects are mediated through binding of Hp(2-20) to the promiscuous, G-protein-linked lipoxin A(4) receptor-formyl peptide-like receptor 1.
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