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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
Author(s) -
Karlsson Jennie,
Fu Huamei,
Boulay François,
Dahlgren Claes,
Hellstrand Kristoffer,
Movitz Charlotta
Publication year - 2005
Publication title -
journal of leukocyte biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.819
H-Index - 191
eISSN - 1938-3673
pISSN - 0741-5400
DOI - 10.1189/jlb.0305153
Subject(s) - biology , receptor , nadph oxidase , peptide , formyl peptide receptor , inhibitory postsynaptic potential , microbiology and biotechnology , signal transduction , peptide receptor , biochemistry , reactive oxygen species , endocrinology , chemotaxis
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.