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Published online before print June 10, 2005
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,1
* Department of Rheumatology and Inflammation Research, Göteborg University, Göteborg, Sweden;
DRDC/BBSI (UMR 5092, CEA/CNRS/UJF), Grenoble, France; and
Department of Clinical Virology, Göteborg University, Göteborg, Sweden
1Correspondence: Department of Clinical Virology, Göteborg University, Guldhedsgatan 10, S-413 46 Göteborg, Sweden. E-mail: charlotta.movitz{at}microbio.gu.se
Truncation of the N-terminal part of the calcium-regulated and phospholipid-binding protein annexin AI has been shown to change the functional properties of the protein and to generate immunoregulatory peptides. Proinflammatory as well as anti-inflammatory signals are triggered by these peptides, and the two formyl peptide receptor (FPR) family members expressed in neutrophils, FPR and FPR-like 1 (FPRL1), have been suggested to transduce these signals. We now report that an annexin AI peptide (Ac9–25) activates, as well as inhibits, the neutrophil release of superoxide anions. Results obtained from experiments with receptor antagonists/inhibitors, desensitized cells, and transfected cells reveal that the Ac9–25 peptide activates the neutrophil reduced nicotinamide adenine dinucleotide phosphate oxidase through FPR but not through FPRL1. The Ac9–25 peptide also inhibits the oxidase activity in neutrophils triggered, not only by the FPR-specific agonist N-formyl-Met-Leu-Phe but also by several other agonists operating through different G protein-coupled receptors. Our data show that the two signals generated by the Ac9–25 peptide are transmitted through different receptors, the inhibitory signal being transduced by a not-yet identified receptor distinct from FPR and FPRL1.
Key Words: granulocytes • inflammation • resolution • cell activation • signal transduction
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