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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 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 Citation Map 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. Related Collections Phagocytes Cell Adhesion and Motility Chemokines, Cytokines, and Interleukins Social Bookmarking                   What's this?  Previous Article  |  Table of Contents  |  Next Article  Blood, 15 May 2003, Vol. 101, No. 10, pp. 4140-4147 PHAGOCYTES Leukocyte antiadhesive 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 From the William Harvey Research Institute, Bart's and the Royal London, Queen Mary School of Medicine and Dentistry, Charterhouse Square, London, United Kingdom. Recent investigations conducted with human neutrophils have indicated an involvement for the receptor for formylated peptides, termed FPR, and its analog FPRL1 (or ALXR because 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 peptidomimetics. 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 to 100 µg administered intravenously prior to reperfusion) abolished I/R-induced cell adhesion and emigration, but not cell rolling. In FPR-deficient mice, peptide Ac2-26 retained significant inhibitory actions (about 50% of the effects in naive mice), and these were blocked by an FPR antagonist, termed butyloxycarbonyl-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 in naive as well as in FPR-deficient mice, whereas the CXC chemokine KC or fMLP were inactive. The present findings demonstrate that endogenous regulatory autocoids such as lipoxin A4 and annexin 1-derived peptides function to disengage adherent cells during cell-cell interactions. © 2003 by The American Society of Hematology.   CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? This article has been cited by other articles: Y. H. Yang, D. Aeberli, A. Dacumos, J. R. Xue, and E. F. Morand Annexin-1 Regulates Macrophage IL-6 and TNF via Glucocorticoid-Induced Leucine Zipper J. Immunol., July 15, 2009; 183(2): 1435 - 1445. [Abstract] [Full Text] [PDF] R. D. Ye, F. Boulay, J. M. Wang, C. Dahlgren, C. Gerard, M. Parmentier, C. N. Serhan, and P. M. Murphy International Union of Basic and Clinical Pharmacology. LXXIII. 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