J. Exp. Med., Volume 189, Number 2, January 18, 1999 395-402

A Seven-transmembrane, G Protein-coupled Receptor, FPRL1, Mediates the Chemotactic Activity of Serum Amyloid A for Human Phagocytic Cells

By Shao Bo Su,^* Wanghua Gong, Ji-Liang Gao,^§ Weiping Shen,^* Philip M. Murphy,^§ Joost J. Oppenheim,^* and Ji Ming Wang^*

From the ^* Laboratory of Molecular Immunoregulation, Division of Basic Sciences; the  Intramural Research Support Program, SAIC Frederick, National Cancer Institute-Frederick Cancer Research and Development Center, Frederick, Maryland 21702-1201; and the ^§ Laboratory of Host Defenses, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland 20892

We have previously reported (Badolato, R., J.M. Wang, W.J. Murphy, A.R. Lloyd, D.F. Michiel, L.L. Bausserman, D.J. Kelvin, and J.J. Oppenheim. 1994. J. Exp. Med. 180:203; Xu, L., R. Badolato, W.J. Murphy, D.L. Longo, M. Anver, S. Hale, J.J. Oppenheim, and J.M. Wang. 1995. J. Immunol. 155:1184.) that the acute phase protein serum amyloid A (SAA) is a potent chemoattractant for human leukocytes in vitro and mouse phagocytes in vivo. To identify the signaling mechanisms, we evaluated patterns of cross-desensitization between SAA and other leukocyte chemoattrctants. We found that the chemotactic bacterial peptide, N-formyl- methionyl-leucyl-phenylalanine (fMLP), was able to specifically attenuate Ca²⁺ mobilization in human phagocytes induced by SAA, but only at very high concentrations, suggesting that SAA uses a low affinity fMLP receptor. Here we demonstrate that SAA selectively induced Ca²⁺ mobilization and migration of HEK cells expressing FPRL1, a human seven-transmembrane domain phagocyte receptor with low affinity for fMLP, and high affinity for lipoxin A4. Furthermore, radiolabeled SAA specifically bound to human phagocytes and FPRL1-transfected 293 cells. In contrast, SAA was not a ligand or agonist for FPR, the high affinity fMLP receptor. Thus, SAA is the first chemotactic ligand identified for FPRL1. Our results suggest that FPRL1 mediates phagocyte migration in response to SAA.

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• Su, S. B., Gao, J.-l., Gong, W.-h., Dunlop, N. M., Murphy, P. M., Oppenheim, J. J., Wang, J. M. (1999). T21/DP107, A Synthetic Leucine Zipper-Like Domain of the HIV-1 Envelope gp41, Attracts and Activates Human Phagocytes by Using G-Protein-Coupled Formyl Peptide Receptors. J. Immunol. 162: 5924-5930 [Abstract] [Full Text]  
• Mills, J. S., Miettinen, H. M., Cummings, D., Jesaitis, A. J. (2000). Characterization of the Binding Site on the Formyl Peptide Receptor Using Three Receptor Mutants and Analogs of Met-Leu-Phe and Met-Met-Trp-Leu-Leu. J. Biol. Chem. 275: 39012-39017 [Abstract] [Full Text]  
• Christophe, T., Karlsson, A., Dugave, C., Rabiet, M.-J., Boulay, F., Dahlgren, C. (2001). The Synthetic Peptide Trp-Lys-Tyr-Met-Val-Met-NH2 Specifically Activates Neutrophils through FPRL1/Lipoxin A4 Receptors and Is an Agonist for the Orphan Monocyte-expressed Chemoattractant Receptor FPRL2. J. Biol. Chem. 276: 21585-21593 [Abstract] [Full Text]  
• Tiffany, H. L., Lavigne, M. C., Cui, Y.-H., Wang, J.-M., Leto, T. L., Gao, J.-L., Murphy, P. M. (2001). Amyloid-beta Induces Chemotaxis and Oxidant Stress by Acting at Formylpeptide Receptor 2, a G Protein-coupled Receptor Expressed in Phagocytes and Brain. J. Biol. Chem. 276: 23645-23652 [Abstract] [Full Text]  
• Le, Y., Gong, W., Tiffany, H. L., Tumanov, A., Nedospasov, S., Shen, W., Dunlop, N. M., Gao, J.-L., Murphy, P. M., Oppenheim, J. J., Wang, J. M. (2001). Amyloid {beta}42 Activates a G-Protein-Coupled Chemoattractant Receptor, FPR-Like-1. J. Neurosci. 21: RC123-RC123 [Abstract] [Full Text]  

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