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Prepublished online as a Blood First Edition Paper on September 26, 2002; DOI 10.1182/blood-2002-05-1431. This Article Full Text Full Text (PDF) All Versions of this Article: 2002-05-1431v1 101/4/1572    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 He, R. Articles by Ye, R. D. Search for Related Content PubMed PubMed Citation Articles by He, R. Articles by Ye, R. D. Related Collections Phagocytes Signal Transduction Social Bookmarking                   What's this?  Previous Article  |  Table of Contents  |  Next Article  Blood, 15 February 2003, Vol. 101, No. 4, pp. 1572-1581 PHAGOCYTES Serum amyloid A induces IL-8 secretion through a G protein-coupled receptor, FPRL1/LXA4R Rong He, Hairong Sang, and Richard D. Ye From the Department of Pharmacology, College of Medicine, University of Illinois, Chicago. Host response to injury and infection is accompanied by a rapid rise in the blood of acute-phase proteins such as serum amyloid A (SAA). Although SAA has been used as a marker for inflammatory diseases, its role in the modulation of inflammation and immunity has not been defined. Human neutrophils respond to SAA with secretion of the proinflammatory cytokines interleukin 8 (IL-8) and, to a lesser extent, tumor necrosis factor  (TNF-). The induction of IL-8 secretion by SAA involves both transcription and translation and correlates with activation of nuclear factor B (NF-B). The proximal signaling events induced by SAA include mobilization of intracellular Ca2+ and activation of the mitogen-activated protein kinases ERK1/2 and p38, both required for the induced IL-8 secretion. Pertussis toxin effectively blocks SAA-induced IL-8 secretion indicating involvement of a Gi-coupled receptor. Overexpression of FPRL1/LXA4R in HeLa cells results in a significant increase of the expression of NF-B and IL-8 luciferase reporters by SAA, and an antibody against the N-terminal domain of FPRL1/LXA4R inhibits IL-8 secretion. Lipoxin A4, which binds to FPRL1/LXA4R specifically, decreases SAA-induced IL-8 secretion significantly. Collectively, these results indicate that the cytokine-like property of SAA is manifested through activation of the Gi-coupled FPRL1/LXA4R, which has been known to mediate the anti-inflammatory effects of lipoxin A4. The ability of FPRL1/LXA4R to mediate 2 drastically different and opposite functions suggests that it plays a role in the modulation of inflammatory and immune responses. © 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: K. Migita, T. Koga, T. Torigoshi, Y. Maeda, T. Miyashita, Y. Izumi, Y. Aiba, A. Komori, M. Nakamura, S. Motokawa, et al. Serum amyloid A protein stimulates CCL20 production in rheumatoid synoviocytes Rheumatology, July 1, 2009; 48(7): 741 - 747. [Abstract] [Full Text] [PDF] R. D. Ye, F. Boulay, J. M. Wang, C. Dahlgren, C. Gerard, M. Parmentier, C. N. Serhan, and P. M. 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