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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 (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 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 Social Bookmarking                   What's this? Submitted May 16, 2002 Accepted September 17, 2002 Serum amyloid A induces IL-8 secretion through a G protein-coupled receptor, FPRL1/LXA4R Rong He, Hairong Sang, and Richard D Ye* Department of Pharmacology, University of Illinois at Chicago, Chicago, IL, USA * Corresponding author; email: yer{at}uic.edu. 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 pro-inflammatory cytokines IL-8 and, to a lesser extent, TNF. The induction of IL-8 secretion by SAA involves both transcription and translation, and correlates with NF-B activation. The proximal signaling events induced by SAA includes 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. Over-expression 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. 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