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Published online before print June 10, 2005
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Article |
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Departments of *Rheumatology and Inflammation Research and Réponse et Dynamique Cellulaires/Laboratoire de Biochimie et Biophysique des Systèmes Intégrés (UMR 5092, CEA/CNRS/UJF), Grenoble, Cedex, France; and Department of Clinical Virology, Göteborg University, Sweden
@ To whom correspondence should be addressed. E-mail: charlotta.movitz{at}microbio.gu.se.
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Abstract |
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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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