scholarly journals Paeonol Inhibits the Development of Rheumatoid Arthritis Through the Formyl Peptide Receptor 2

2021 ◽  
Author(s):  
shao yubao ◽  
Ji Dan ◽  
Bao Lanxin ◽  
Li Wenhao ◽  
Dai Jinchen ◽  
...  
Keyword(s):  
Rheumatoid Arthritis ◽  
Autoimmune Disease ◽  
Inhibitory Effect ◽  
Formyl Peptide Receptor ◽  
Inflammatory Factors ◽  
Systemic Autoimmune Disease ◽  
Data Sets ◽  
Peptide Receptor ◽  
Formyl Peptide ◽  
Key Genes

Abstract Rheumatoid arthritis (RA) is a refractory systemic autoimmune disease associated with synovial inflammation. Previous studies postulate that paeonol has good anti-arthritis effects on RA. However, its systematic description remains unknown. Herein, we used bioinformatics tools to evaluate the mechanism of paeonol in arthritis systematically. A macrophage model was employed to study the differentially expressed genes between the inflammation and normal group, revealing 169 inflammation-related genes. Another 275 key genes affected by paeonol were identified in the same model. Three key genes, FPR2, Cd83, and Cfb, were obtained after combining the two data sets. Paeonol inhibited the release of inflammatory factors and the proliferation of synovial. However, its inhibitory effect was blocked by Fpr2 blocker WRW4. In summary, paeonol can inhibit the development of arthritis through FPR2. This provides new scope for the design and development of FPR2 ligands.

scholarly journals A Ganoderma-Derived Compound Exerts Inhibitory Effect Through Formyl Peptide Receptor 2

2020 ◽  
Vol 11 ◽  
Author(s):  
Huirong Wang ◽  
Xingrong Peng ◽  
Yunjun Ge ◽  
Shuo Zhang ◽  
Zhenyi Wang ◽  
...  
Keyword(s):  
Inhibitory Effect ◽  
Formyl Peptide Receptor ◽  
Peptide Receptor ◽  
Formyl Peptide

scholarly journals Antiflammin-2 Activates the Human Formyl-Peptide Receptor Like 1

2006 ◽  
Vol 6 ◽  
pp. 1375-1384 ◽  
Author(s):  
Ahmad M. Kamal ◽  
Richard P.G. Hayhoe ◽  
Anbalakan Paramasivam ◽  
Dianne Cooper ◽  
Roderick J. Flower ◽  
...  
Keyword(s):  
Receptor Activation ◽  
Inhibitory Effect ◽  
Formyl Peptide Receptor ◽  
Annexin A1 ◽  
Hek 293 ◽  
Peptide Receptor ◽  
293 Cells ◽  
Formyl Peptide ◽  
Anti Inflammatory ◽  
Extracellular Regulated Kinase

The anti-inflammatory actions of the nonapeptide antiflammin-2, identified by homology with uteroglobin and annexin-A1 sequences, have been described in some detail, yet its mechanisms of action remain elusive. Since recent data indicate an involvement of the formyl peptide receptor (FPR)-like 1 (or FPRL-1) in the effects of annexin-A1, we have tested here the effect of antiflammin-2 with respect to this receptor family. Using HEK-293 cells expressing either human FPR and FPRL-1, and an annexin-A1 peptide as tracer ([125I-Tyr]-Ac2-26), we found that antiflammin-2 competed for binding only at FPRL-1, and not FPR, with an approximate EC50of 1 μM. In line with data produced for the full-length protein, genuine receptor activation by antiflammin-2 was confirmed by rapid phosphorylation of extracellular-regulated kinase 1 and 2. Finally, study of the neutrophil interaction with activated endothelium under flow demonstrated an inhibitory effect of antiflammin-2, thus providing functional support to a role for the antiflammin-2/FPRL-1 anti-inflammatory axis.

Chemotactic factor binding by metastatic tumour cells: evidence for a formyl-peptide receptor on a non-myelogenous cell

1985 ◽  
Vol 73 (1) ◽  
pp. 121-134
Author(s):  
W.A. Marasco ◽  
P.A. Ward ◽  
D.E. Feltner ◽  
J. Varani
Keyword(s):  
Binding Sites ◽  
Competitive Inhibition ◽  
Inhibitory Effect ◽  
Tumour Cells ◽  
Formyl Peptide Receptor ◽  
Metastatic Tumour ◽  
Binding Studies ◽  
Peptide Receptor ◽  
Formyl Peptide ◽  
Equilibrium Dissociation

Analysis of fMet-Leu-[3H]Phe binding to Walker 256 carcinosarcoma cells demonstrated both saturable and reversible binding, and indicated the presence of a single population of binding sites having an equilibrium dissociation constant: KD = 15.7 +/− 3.3 X 10(−9) M, and with 2425 +/− 204 binding sites per cell. The specificity of the binding site was investigated by competitive inhibition of fMet-Leu-[3H]Phe binding studies using 10 oligoformyl peptides. These results demonstrated an order of peptide reactivity with marked similarity in specificity to the leucocyte binding sites for the formyl-peptides. The most active peptides also had potent agonist activity as determined by their ability to increase the cells' adherence response to nylon-wool fibres. In addition, a competitive antagonist of the formyl-peptide receptor, tert-butoxy-Phe-Leu-Phe-Leu-Phe, completely abolished the adherence response induced by fMet-Leu-Phe, but had no inhibitory effect on the adherence response caused by the tumour-promoting agent, phorbol myristate acetate. These data demonstrate that formyl-peptide receptors may be more common than we have anticipated and may be found on cells not derived from the myeloid series. Furthermore, these studies advance our understanding of stimulus-coupled responses in tumour cells.

scholarly journals Novel formyl peptide receptor (FPR) agonists with pyridinone and pyrimidindione scaffolds that are potentially useful for the treatment of rheumatoid arthritis

2020 ◽  
Vol 100 ◽  
pp. 103880 ◽  
Author(s):  
Letizia Crocetti ◽  
Claudia Vergelli ◽  
Gabriella Guerrini ◽  
Niccolò Cantini ◽  
Liliya N. Kirpotina ◽  
...  
Keyword(s):  
Rheumatoid Arthritis ◽  
Formyl Peptide Receptor ◽  
Peptide Receptor ◽  
Formyl Peptide
Sign in / Sign up

Export Citation Format

Share Document