Identification and characterization of an endogenous chemotactic ligand specific for FPRL2

Isabelle Migeotte, Elena Riboldi, Jean Denis Franssen, Françoise Grégoire, Cécile Loison, Valérie Wittamer, Michel Detheux, Patrick Robberecht, Sabine Costagliola, Gilbert Vassart, Silvano Sozzani, Marc Parmentier, David Communi

Research output: Contribution to journalArticle

78 Citations (Scopus)

Abstract

Chemotaxis of dendritic cells (DCs) and monocytes is a key step in the initiation of an adequate immune response. Formyl peptide receptor (FPR) and FPR-like receptor (FPRL)1, two G protein-coupled receptors belonging to the FPR family, play an essential role in host defense mechanisms against bacterial infection and in the regulation of inflammatory reactions. FPRL2, the third member of this structural family of chemoattractant receptors, is characterized by its specific expression on monocytes and DCs. Here, we present the isolation from a spleen extract and the functional characterization of F2L, a novel chemoattractant peptide acting specifically through FPRL2. F2L is an acetylated amino-terminal peptide derived from the cleavage of the human heme-binding protein, an intracellular tetrapyrolle-binding protein. The peptide binds and activates FPRL2 in the low nanomolar range, which triggers intracellular calcium release, inhibition of cAMP accumulation, and phosphorylation of extracellular signal-regulated kinase 1/2 mitogen-activated protein kinases through the G i class of heterotrimeric G proteins. When tested on monocytes and monocyte-derived DCs, F2L promotes calcium mobilization and chemotaxis. Therefore, F2L appears as a new natural chemoattractant peptide for DCs and monocytes, and the first potent and specific agonist of FPRL2.

Original languageEnglish
Pages (from-to)83-93
Number of pages11
JournalJournal of Experimental Medicine
Volume201
Issue number1
DOIs
Publication statusPublished - Jan 3 2005

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Formyl Peptide Receptor
Monocytes
Dendritic Cells
Ligands
Peptides
Chemotactic Factors
Chemotaxis
Calcium
Heterotrimeric GTP-Binding Proteins
Cyclic GMP-Dependent Protein Kinases
Mitogen-Activated Protein Kinase 3
Mitogen-Activated Protein Kinase 1
Defense Mechanisms
G-Protein-Coupled Receptors
Mitogen-Activated Protein Kinases
Bacterial Infections
Carrier Proteins
Spleen
Phosphorylation

ASJC Scopus subject areas

  • Immunology

Cite this

Migeotte, I., Riboldi, E., Franssen, J. D., Grégoire, F., Loison, C., Wittamer, V., ... Communi, D. (2005). Identification and characterization of an endogenous chemotactic ligand specific for FPRL2. Journal of Experimental Medicine, 201(1), 83-93. https://doi.org/10.1084/jem.20041277

Identification and characterization of an endogenous chemotactic ligand specific for FPRL2. / Migeotte, Isabelle; Riboldi, Elena; Franssen, Jean Denis; Grégoire, Françoise; Loison, Cécile; Wittamer, Valérie; Detheux, Michel; Robberecht, Patrick; Costagliola, Sabine; Vassart, Gilbert; Sozzani, Silvano; Parmentier, Marc; Communi, David.

In: Journal of Experimental Medicine, Vol. 201, No. 1, 03.01.2005, p. 83-93.

Research output: Contribution to journalArticle

Migeotte, I, Riboldi, E, Franssen, JD, Grégoire, F, Loison, C, Wittamer, V, Detheux, M, Robberecht, P, Costagliola, S, Vassart, G, Sozzani, S, Parmentier, M & Communi, D 2005, 'Identification and characterization of an endogenous chemotactic ligand specific for FPRL2', Journal of Experimental Medicine, vol. 201, no. 1, pp. 83-93. https://doi.org/10.1084/jem.20041277
Migeotte, Isabelle ; Riboldi, Elena ; Franssen, Jean Denis ; Grégoire, Françoise ; Loison, Cécile ; Wittamer, Valérie ; Detheux, Michel ; Robberecht, Patrick ; Costagliola, Sabine ; Vassart, Gilbert ; Sozzani, Silvano ; Parmentier, Marc ; Communi, David. / Identification and characterization of an endogenous chemotactic ligand specific for FPRL2. In: Journal of Experimental Medicine. 2005 ; Vol. 201, No. 1. pp. 83-93.
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