Abstract
Leukocyte infiltration is a hallmark of inflammatory responses. This process depends on the bacterial and host tissue-derived chemotactic factors interacting with G-protein-coupled seven-transmembrane receptors (GPCRs) expressed on the cell surface. Formylpeptide receptors (FPRs in human and Fprs in mice) belong to the family of chemoattractant GPCRs that are critical mediators of myeloid cell trafficking in microbial infection, inflammation, immune responses and cancer progression. Both murine Fprs and human FPRs participate in many patho-physiological processes due to their expression on a variety of cell types in addition to myeloid cells. FPR contribution to numerous pathologies is in part due to its capacity to interact with a plethora of structurally diverse chemotactic ligands. One of the murine Fpr members, Fpr2, and its endogenous agonist peptide, Cathelicidin-related antimicrobial peptide (CRAMP), control normal mouse colon epithelial growth, repair and protection against inflammation-associated tumorigenesis. Recent developments in FPR (Fpr) and ligand studies have greatly expanded the scope of these receptors and ligands in host homeostasis and disease conditions, therefore helping to establish these molecules as potential targets for therapeutic intervention.
Highlights
Properties of FPRsFormylpeptide receptors (FPR, Fpr for expression in mice) are G-protein-coupled receptors and were incidentally the first G-protein-coupled seven-transmembrane receptors (GPCRs) to be identified in neutrophils [1]
Leukocyte infiltration is a hallmark of inflammatory responses
FPR1 was the first named of the receptors, and it was initially discovered as the receptor for the formylated bacterial product formyl-methionine-leucyl-phenylalanine, the name of which gave rise to the naming of the receptor in question [6]
Summary
Formylpeptide receptors (FPR, Fpr for expression in mice) are G-protein-coupled receptors and were incidentally the first GPCRs to be identified in neutrophils [1]. Cooray et al [25] demonstrated that the switch between FPR2-mediated pro- and anti-inflammatory cell responses is due to conformational changes of the receptor upon ligand binding: binding of anti-inflammatory ligands such as Anx A1 caused FPRs to form homodimers, which led to the release of inflammation-resolving cytokines like IL-10. Inflammatory ligands such as serum-amyloid alpha (SAA) did not cause receptor homodimerization. Host-derived non-peptides, as well as synthetic or small-molecule ligands will be discussed
Sign-in/Register to view highlights & summary Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
