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NADPH-oxidase activation in murine neutrophils via formyl peptide receptors

Journal article
Authors Johan Bylund
Marie Samuelsson
Vincent Collins
Anna Karlsson
Published in Exp Cell Res
Volume 282
Issue 2
Pages 70-7
Publication year 2003
Published at Institute of Internal Medicine, Dept of Rheumatology and Inflammation Research
Pages 70-7
Language en
Links www.ncbi.nlm.nih.gov/entrez/query.f...
Keywords Animals, Cytochalasin B/pharmacology, Enzyme Activation/drug effects, Humans, Kinetics, Lipopolysaccharides/pharmacology, Mice, Mice, Inbred C3H, Mice, Inbred C57BL, N-Formylmethionine Leucyl-Phenylalanine/pharmacology, NADPH Oxidase/drug effects/*metabolism, Neutrophil Activation/drug effects, Neutrophils/drug effects/*enzymology/metabolism, Oligopeptides/pharmacology, Reactive Oxygen Species/metabolism, Receptors, Formyl Peptide, Receptors, Immunologic/agonists/*physiology, Receptors, Peptide/agonists/*physiology
Subject categories Medical and Health Sciences

Abstract

Neutrophils play a key role at inflammatory sites where, in addition to destroying infecting microorganisms, they may also have deleterious effects on host tissues. Both activities involve activation of the NADPH-oxidase that produces bactericidal and tissue-destructive reactive oxygen species (ROS). We activated the murine NADPH-oxidase using different types of neutrophil activators and characterized the oxidative responses with respect to magnitude, localization, and kinetics. We show that agonist-induced activation of murine neutrophils results exclusively in extracellular release of ROS and no intracellular production could be detected. We also show that the formylated peptide, formyl-Met-Leu-Phe (fMLF), is a much less potent activator of the murine NADPH-oxidase than of the human analogue. Nevertheless, fMLF responses can be primed by pretreating the murine neutrophils with either cytochalasin B or bacterial lipopolysaccharide. Finally, we show that a synthetic hexapeptide, WKYMVM, is a more potent stimulus than fMLF for murine neutrophils and that these two agonists probably act via nonidentical high-affinity receptors.

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