The N-formylpeptide receptor (FPR) is a G protein–coupled receptor that mediates mammalian phagocyte chemotactic responses to bacterial N-formylpeptides. Here we show that a mouse gene named Fpr-rs2 encodes a second N-formylpeptide receptor subtype selective for neutrophils which we have provisionally named FPR2. The prototype N-formylpeptide fMLF induced calcium flux and chemotaxis in human embryonic kidney (HEK) 293 cells stably transfected with FPR2. The EC50s, ∼5 μM for calcium flux and chemotaxis, were ∼100-fold greater than the corresponding values for mouse FPR-transfected HEK 293 cells. Consistent with this, fMLF induced two distinct concentration optima for chemotaxis of normal mouse neutrophils, but only the high concentration optimum for chemotaxis of neutrophils from FPR knockout mice. Based on these data, we hypothesize that high- and low-affinity N-formylpeptide receptors, FPR and FPR2, respectively, may function in vivo as a relay mediating neutrophil migration through the high and low concentration portions of N-formylpeptide gradients.
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6 September 1999
Brief Definitive Report|
September 06 1999
N-Formylpeptides Induce Two Distinct Concentration Optima for Mouse Neutrophil Chemotaxis by Differential Interaction with Two N-Formylpeptide Receptor (Fpr) Subtypes: Molecular Characterization of Fpr2, a Second Mouse Neutrophil Fpr
Jennifer K. Hartt,
Jennifer K. Hartt
aFrom the Laboratory of Host Defenses, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland 20892
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Grant Barish,
Grant Barish
aFrom the Laboratory of Host Defenses, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland 20892
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Philip M. Murphy,
Philip M. Murphy
aFrom the Laboratory of Host Defenses, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland 20892
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Ji-Liang Gao
Ji-Liang Gao
aFrom the Laboratory of Host Defenses, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland 20892
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Jennifer K. Hartt
aFrom the Laboratory of Host Defenses, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland 20892
Grant Barish
aFrom the Laboratory of Host Defenses, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland 20892
Philip M. Murphy
aFrom the Laboratory of Host Defenses, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland 20892
Ji-Liang Gao
aFrom the Laboratory of Host Defenses, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland 20892
G. Barish's present address is University of Michigan School of Medicine, Ann Arbor, MI 48105.
J.K. Hartt's present address is Immunology Department, Harvard Medical School, 200 Longwood Ave., Bldg. D-2, Rm. 137, Boston, MA 02115.
Received:
March 29 1999
Revision Requested:
June 25 1999
Accepted:
July 06 1999
Online ISSN: 1540-9538
Print ISSN: 0022-1007
© 1999 The Rockefeller University Press
1999
The Rockefeller University Press
J Exp Med (1999) 190 (5): 741–748.
Article history
Received:
March 29 1999
Revision Requested:
June 25 1999
Accepted:
July 06 1999
Citation
Jennifer K. Hartt, Grant Barish, Philip M. Murphy, Ji-Liang Gao; N-Formylpeptides Induce Two Distinct Concentration Optima for Mouse Neutrophil Chemotaxis by Differential Interaction with Two N-Formylpeptide Receptor (Fpr) Subtypes: Molecular Characterization of Fpr2, a Second Mouse Neutrophil Fpr. J Exp Med 6 September 1999; 190 (5): 741–748. doi: https://doi.org/10.1084/jem.190.5.741
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