Formyl Peptide Receptors in Cellular Differentiation and Inflammatory Diseases

2017 ◽  
Vol 118 (6) ◽  
pp. 1300-1307 ◽  
Author(s):  
Ha Young Lee ◽  
Mingyu Lee ◽  
Yoe-Sik Bae
Keyword(s):  
Cellular Differentiation ◽  
Inflammatory Diseases ◽  
Peptide Receptors ◽  
Formyl Peptide Receptors ◽  
Formyl Peptide

scholarly journals A long-lived peptide-conjugated iridium(iii) complex as a luminescent probe and inhibitor of the cell migration mediator, formyl peptide receptor 2

2018 ◽  
Vol 9 (43) ◽  
pp. 8171-8177 ◽  
Author(s):  
Kasipandi Vellaisamy ◽  
Guodong Li ◽  
Wanhe Wang ◽  
Chung-Hang Leung ◽  
Dik-Lung Ma
Keyword(s):  
Cell Migration ◽  
Wound Repair ◽  
Inflammatory Diseases ◽  
Formyl Peptide Receptor ◽  
Luminescent Probe ◽  
Peptide Receptors ◽  
Formyl Peptide Receptors ◽  
Peptide Receptor ◽  
Formyl Peptide

Formyl peptide receptors play important biological and therapeutic roles in wound repair and inflammatory diseases.

scholarly journals The Role of Formyl Peptide Receptors in Permanent and Low-Grade Inflammation: Helicobacter pylori Infection as a Model

2021 ◽  
Vol 22 (7) ◽  
pp. 3706
Author(s):  
Paola Cuomo ◽  
Marina Papaianni ◽  
Rosanna Capparelli ◽  
Chiara Medaglia
Keyword(s):  
Helicobacter Pylori ◽  
Inflammatory Responses ◽  
Inflammatory Diseases ◽  
Formyl Peptide Receptor ◽  
Surface Pattern ◽  
Low Grade ◽  
Peptide Receptors ◽  
Formyl Peptide Receptors ◽  
Formyl Peptide

Formyl peptide receptors (FPRs) are cell surface pattern recognition receptors (PRRs), belonging to the chemoattractant G protein-coupled receptors (GPCRs) family. They play a key role in the innate immune system, regulating both the initiation and the resolution of the inflammatory response. FPRs were originally identified as receptors with high binding affinity for bacteria or mitochondria N-formylated peptides. However, they can also bind a variety of structurally different ligands. Among FPRs, formyl peptide receptor-like 1 (FPRL1) is the most versatile, recognizing N-formyl peptides, non-formylated peptides, and synthetic molecules. In addition, according to the ligand nature, FPRL1 can mediate either pro- or anti-inflammatory responses. Hp(2-20), a Helicobacter pylori-derived, non-formylated peptide, is a potent FPRL1 agonist, participating in Helicobacter pylori-induced gastric inflammation, thus contributing to the related site or not-site specific diseases. The aim of this review is to provide insights into the role of FPRs in H. pylori-associated chronic inflammation, which suggests this receptor as potential target to mitigate both microbial and sterile inflammatory diseases.

The Role of Formyl Peptide Receptors in Microbial Infection and Inflammation

2003 ◽  
Vol 2 (1) ◽  
pp. 83-93 ◽  
Author(s):  
Yingying Le ◽  
Ronghua Sun ◽  
Guoguang Ying ◽  
Pablo Iribarren ◽  
Ji Wang
Keyword(s):  
Microbial Infection ◽  
Peptide Receptors ◽  
Formyl Peptide Receptors ◽  
Formyl Peptide ◽  
Infection And Inflammation

scholarly journals G-protein–coupled formyl peptide receptors play a dual role in neutrophil chemotaxis and bacterial phagocytosis

2019 ◽  
Vol 30 (3) ◽  
pp. 346-356 ◽  
Author(s):  
Xi Wen ◽  
Xuehua Xu ◽  
Wenxiang Sun ◽  
Keqiang Chen ◽  
Miao Pan ◽  
...  
Keyword(s):  
G Protein ◽  
Receptor Tyrosine Kinase ◽  
Tyrosine Kinases ◽  
Actin Polymerization ◽  
G Protein Coupled Receptors ◽  
Peptide Receptors ◽  
Tyrosine Kinase Signaling ◽  
Formyl Peptide Receptors ◽  
Formyl Peptide ◽  
G Protein Coupled

A dogma of innate immunity is that neutrophils use G-protein–coupled receptors (GPCRs) for chemoattractant to chase bacteria through chemotaxis and then use phagocytic receptors coupled with tyrosine kinases to destroy opsonized bacteria via phagocytosis. Our current work showed that G-protein–coupled formyl peptide receptors (FPRs) directly mediate neutrophil phagocytosis. Mouse neutrophils lacking formyl peptide receptors (Fpr1/2–/–) are defective in the phagocytosis of Escherichia coli and the chemoattractant N-formyl-Met-Leu-Phe (fMLP)-coated beads. fMLP immobilized onto the surface of a bead interacts with FPRs, which trigger a Ca2+response and induce actin polymerization to form a phagocytic cup for engulfment of the bead. This chemoattractant GPCR/Gi signaling works independently of phagocytic receptor/tyrosine kinase signaling to promote phagocytosis. Thus, in addition to phagocytic receptor-mediated phagocytosis, neutrophils also utilize the chemoattractant GPCR/Gi signaling to mediate phagocytosis to fight against invading bacteria.

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