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Neutrophil NADPH-oxidase activation by an annexin AI peptide is transduced by the formyl peptide receptor (FPR), whereas an inhibitory signal is generated independently of the FPR family receptors

Journal article
Authors Jennie Karlsson
Huamei Fu
F. Boulay
Claes Dahlgren
Kristoffer Hellstrand
Charlotta Movitz
Published in Journal of leukocyte biology
Volume 78
Issue 3
Pages 762-71
ISSN 0741-5400 (Print)
Publication year 2005
Published at Institute of Internal Medicine, Dept of Rheumatology and Inflammation Research
Institute of Laboratory Medicine, Dept of Clinical Virology
Pages 762-71
Language en
Keywords Annexin A1/immunology, Calcium/metabolism, Cell Differentiation/drug effects, Enzyme Activation/drug effects, HL-60 Cells, Humans, N-Formylmethionine Leucyl-Phenylalanine/pharmacology, NADPH Oxidase/antagonists & inhibitors/*immunology, Neutrophils/drug effects/*enzymology/immunology, Receptors, Formyl Peptide/*antagonists & inhibitors/immunology, Signal Transduction/*drug effects/immunology, Superoxides/antagonists & inhibitors/metabolism, Time Factors
Subject categories Microbiology in the medical area


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.

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