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Prepublished online as a Blood First Edition Paper on January 30, 2003; DOI 10.1182/blood-2002-11-3411. This Article Full Text (PDF) All Versions of this Article: 2002-11-3411v1 101/10/4140    most recent Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Rights and Permissions Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Gavins, F. N E Articles by Perretti, M. Search for Related Content PubMed PubMed Citation Articles by Gavins, F. N E Articles by Perretti, M. Social Bookmarking                   What's this? Submitted November 12, 2002 Accepted December 28, 2002 Leukocyte anti-adhesive actions of annexin 1: ALXR and FPR related anti-inflammatory mechanisms Felicity N E Gavins, Simon Yona, Ahmad M Kamal, Roderick J Flower, and Mauro Perretti* Department of Biochemical Pharmacology, William Harvey Research Institute, London, United Kingdom * Corresponding author; email: m.perretti{at}qmul.ac.uk. Recent investigations conducted with human neutrophils have indicated an involvement for the receptor for formylated peptides, termed FPR, and its analogue FPRL1 (or ALXR since it is the receptor for the endogenous ligand lipoxin A4) in the in vitro inhibitory actions of the glucocorticoid-regulated protein annexin 1 and its peptido-mimetics. To translate these findings in in-vivo settings, we have used an ischemia/reperfusion (I/R) procedure to promote leukocyte-endothelium interactions in the mouse mesenteric microcirculation. In naive mice, the annexin 1 mimetic peptide Ac2-26 (20-100 µg administered i.v. prior to reperfusion) abolished I/R induced the cell adhesion and emigration, but not rolling. In FPR deficient mice, peptide Ac2-26 retained significant inhibitory actions (~50% of the effects in naive mice), and these were blocked by an FPR antagonist, termed buthyloxycarbonyl-Phe-Leu-Phe-Leu-Phe or Boc2. In vitro, neutrophils taken from these animals could be activated at high concentrations of formyl-Met-Leu-Phe (30 µM; fMLP) and this effect was blocked by cell incubation with peptide Ac2-26 (66 µM) or Boc2 (100 µM). FPR deficient neutrophils expressed ALXR mRNA and protein. Both ALXR agonists, lipoxin A4 and peptide Ac2-26, provoked detachment of adherent leukocytes equally in naive and FPR deficient mice, whereas the CXC chemokine KC or fMLP were inactive. 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