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, Grant Barish, Philip M. Murphy, Ji Liang Gao*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

94 Scopus citations

Abstract

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 cherootaxis in human embryonic kidney (HEK) 293 cells stably transfected with FPR2. The EC50s, κ5 μM for calcium flux and cherootaxis, were κ100-fold greater than the corresponding values for mouse FPR- transfected HEK 293 cells. Consistent with this, fMLF induced two distinct concentration optima for cherootaxis 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.

Original languageEnglish (US)
Pages (from-to)741-747
Number of pages7
JournalJournal of Experimental Medicine
Volume190
Issue number5
DOIs
StatePublished - Sep 6 1999

Keywords

  • Chemoattractant
  • G protein-coupled receptor
  • Inflammation
  • Neutrophil
  • Phagocyte

ASJC Scopus subject areas

  • Immunology and Allergy
  • Immunology

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