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 N-formyl peptide receptors in human neutrophils display distinct membrane distribution and lateral mobility when labeled with agonist and antagonist.

1993 ◽  
Vol 121 (6) ◽  
pp. 1281-1289 ◽  
Author(s):  
B Johansson ◽  
M P Wymann ◽  
K Holmgren-Peterson ◽  
K E Magnusson
Keyword(s):  
Confocal Microscopy ◽  
Lateral Diffusion ◽  
Formyl Peptide Receptor ◽  
Human Neutrophils ◽  
Lateral Mobility ◽  
Peptide Receptors ◽  
Tetrazolium Chloride ◽  
Formyl Peptide Receptors ◽  
Peptide Receptor ◽  
Formyl Peptide

Receptors for bacterial N-formyl peptides are instrumental for neutrophil chemotactic locomotion and activation at sites of infection. As regulatory mechanisms for signal transduction, both rapid coupling of the occupied receptor to cytoskeletal components, and receptor lateral redistribution, have been suggested (Jesaitis et al., 1986, 1989). To compare the distribution and lateral diffusion of the nonactivated and activated neutrophil N-formyl-peptide receptor, before internalization, we used a new fluorescent N-formyl-peptide receptor antagonist, tertbutyloxycarbonyl-Phe(D)-Leu-Phe(D)-Leu-Phe-OH (Boc-FLFLF, 0.1-1 microM), and the fluorescent receptor agonist formyl-Nle-Leu-Phe-Nle-Tyr-Lys (fnLLFnLYK, 0.1-1 microM). Fluorescent Boc-FLFLF did not elicit an oxidative burst in the neutrophil at 37 degrees C, as assessed by chemiluminescence and reduction of p-nitroblue tetrazolium chloride, but competed efficiently both with formyl-methionyl-leucyl-phenylalanine (fMLF) and fnLLFnLYK. It was not internalized, as evidenced by confocal microscopy and acid elution of surface bound ligand. The lateral mobility characteristics of the neutrophil fMLF receptor were investigated with the technique of FRAP. The diffusion coefficient (D) was similar for antagonist- and agonist-labeled receptors (D approximately 5 x 10(-10) cm2/s), but the fraction of mobile receptors was significantly lower in agonist- compared to antagonist-labeled cells, approximately 40% in contrast to approximately 60%. This reduction in receptor mobile fraction was slightly counteracted, albeit not significantly, by dihydrocytochalasin B (dhcB, 5 microM). To block internalization of agonist-labeled receptors, receptor mobility measurements were done at 14 degrees C. At this temperature, confocal microscopy revealed clustering of receptors in response to agonist binding, compared to a more uniform receptor distribution in antagonist-labeled cells. The pattern of agonist-induced receptor clustering was less apparent after dhcB treatment. To summarize, this work shows that activated N-formyl peptide receptors aggregate and immobilize in the plane of the neutrophil plasma membrane before internalization, a process that is affected, but not significantly reversed, by cytochalasin. The results are consistent with a model where arrested receptors are associated mainly with a cytochalasin-insensitive pool of cytoskeletal elements.

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.

FORMYL PEPTIDE RECEPTOR 2 DNA APTAMERS FOR TARGETED THERAPY OF WOUND REPAIR

2022 ◽  
Author(s):  
M.C. Arriba ◽  
G. Fernández ◽  
E. Chacón-Solano ◽  
M. Mataix ◽  
L. Martínez-Santamaría ◽  
...  
Keyword(s):  
Targeted Therapy ◽  
Wound Repair ◽  
Formyl Peptide Receptor ◽  
Dna Aptamers ◽  
Peptide Receptor ◽  
Formyl Peptide

Intracellular formyl peptide receptor regulates naïve CD4 T cell migration

2018 ◽  
Vol 497 (1) ◽  
pp. 226-232 ◽  
Author(s):  
Ha Young Lee ◽  
Yu Sun Jeong ◽  
Mingyu Lee ◽  
Hee-Seok Kweon ◽  
Yang Hoon Huh ◽  
...  
Keyword(s):  
Cell Migration ◽  
T Cell ◽  
Cd4 T Cell ◽  
Formyl Peptide Receptor ◽  
Peptide Receptor ◽  
T Cell Migration ◽  
Formyl Peptide

scholarly journals Formyl-Peptide Receptor Activation Enhances Phagocytosis of Community-Acquired Methicillin-Resistant Staphylococcus aureus

2019 ◽  
Author(s):  
Elisabeth Weiß ◽  
Katja Schlatterer ◽  
Christian Beck ◽  
Andreas Peschel ◽  
Dorothee Kretschmer
Keyword(s):  
Staphylococcus Aureus ◽  
Methicillin Resistant Staphylococcus Aureus ◽  
Receptor Activation ◽  
Formyl Peptide Receptor ◽  
Peptide Receptors ◽  
Highly Pathogenic ◽  
Methicillin Resistant ◽  
Formyl Peptide Receptors ◽  
Formyl Peptide ◽  
First Time

Abstract Background Formyl-peptide receptors (FPRs) are important pattern recognition receptors that sense specific bacterial peptides. Formyl-peptide receptors are highly expressed on neutrophils and monocytes, and their activation promotes the migration of phagocytes to sites of infection. It is currently unknown whether FPRs may also influence subsequent processes such as bacterial phagocytosis and killing. Staphylococcus aureus, especially highly pathogenic community-acquired methicillin-resistant S aureus strains, release high amounts of FPR2 ligands, the phenol-soluble modulins. Methods We demonstrate that FPR activation leads to upregulation of complement receptors 1 and 3 as well as FCγ receptor I on neutrophils and, consequently, increased opsonic phagocytosis of S aureus and other pathogens. Results Increased phagocytosis promotes killing of S aureus and interleukin-8 release by neutrophils. Conclusions We show here for the first time that FPRs govern opsonic phagocytosis. Manipulation of FPR2 activation could open new therapeutic opportunities against bacterial pathogens.

N-Formyl Peptide Receptors Display an Asymmetric Distribution In Migrating Human Neutrophils

1999 ◽  
Vol 5 (S2) ◽  
pp. 1126-1127
Author(s):  
Vesa-Matti Loitto ◽  
Birgitta Rasmusson ◽  
Karl-Eric Magnusson
Keyword(s):  
Cell Movement ◽  
Ccd Camera ◽  
Formyl Peptide Receptor ◽  
Human Neutrophils ◽  
Asymmetric Distribution ◽  
Phagocytic Cells ◽  
Peptide Receptors ◽  
Directed Movement ◽  
Formyl Peptide Receptors ◽  
Formyl Peptide

A debated and yet unanswered question, in regard to polarization and directed movement of phagocytic cells, concerns the distribution of chemoattractant receptors during cell locomotion1. We have therefore studied the instantaneous distribution of N-formyl-peptide receptors on living neutrophils. Using a fluorescent N-formyl-peptide receptor antagonist, tert-butyloxycarbonyl-Phe(D)-Leu-Phe(D)-Leu-Phe-OH (Boc-FLFLF), and a fluorescent receptor agonist, formyl-Nle-Leu-Phe-Nle-Tyr-Lys (fnLLFnLYK), the localization of the chemoattractant receptors could be followed during random migratio2. Neutrophils were adhered to plasma-coated coverslips. A Nomarski differential interference contrast (DIC)- image was taken, and rapidly followed by a fluorescence-image captured with a water-cooled, slow-scan CCD-camera. Then a second DIC-image was directly recorded to reveal the direction of cell movement.Using fnLLFnLYK we observed that the distribution of N-formyl-peptide receptors was clearly heterogeneous as shown in figure. Fluorescence was concentrated mainly at the rear and front of elongated locomoting cells, leaving the cell body almost non-fluorescent.

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