Signal Transduction of Hyaluronic Acid−Peptide Conjugate for Formyl Peptide Receptor Like 1 Receptor

2008 ◽  
Vol 19 (12) ◽  
pp. 2401-2408 ◽  
Author(s):  
Eun Ju Oh ◽  
Jung-Wook Kim ◽  
Ji-Hyun Kong ◽  
Sung Ho Ryu ◽  
Sei Kwang Hahn
Keyword(s):  
Signal Transduction ◽  
Hyaluronic Acid ◽  
Formyl Peptide Receptor ◽  
Peptide Receptor ◽  
Formyl Peptide

scholarly journals N-Formyl peptide receptor subtypes in human neutrophils activate l-plastin phosphorylation through different signal transduction intermediates

2004 ◽  
Vol 377 (2) ◽  
pp. 469-477 ◽  
Author(s):  
Marie-Hélène PACLET ◽  
Clare DAVIS ◽  
Peter KOTSONIS ◽  
Jasminka GODOVAC-ZIMMERMANN ◽  
Anthony W. SEGAL ◽  
...  
Keyword(s):  
Signal Transduction ◽  
Formyl Peptide Receptor ◽  
Actin Binding ◽  
Human Neutrophils ◽  
Receptor Subtypes ◽  
Peptide Receptor ◽  
High Affinity ◽  
Formyl Peptide ◽  
Fmlp Receptor ◽  
Phosphoinositide 3 Kinase

We investigated the coupling of the fMLP (N-formyl-l-methionyl-l-leucyl-l-phenylalanine; ‘chemotactic peptide’) receptor with phosphorylation of the actin-binding protein l-plastin in neutrophils. Using two-dimensional IEF (isoelectric focusing)/PAGE and MALDI–TOF (matrix-assisted laser desorption ionization–time-of-flight)-MS, l-plastin was identified as a major phosphoprotein in fMLP-stimulated neutrophils whose phosphorylation was dependent on phosphoinositide 3-kinase, PLD (phospholipase D) and PKC (protein kinase C) activity. Two fMLP receptor subtypes were identified in neutrophils, characterized by a distinct sensitivity to fMLP and antagonistic peptides. Both receptor subtypes induced the phosphorylation of l-plastin. l-plastin phosphorylation induced by low-affinity fMLP receptors involves an action of phosphoinositide 3-kinase, PLD and PKC isotypes. In contrast, none of these intermediates are utilized by high-affinity fMLP receptors in the phosphorylation of l-plastin. However, the PKC inhibitor Ro-31-8220 inhibits l-plastin phosphorylation induced by the high-affinity fMLP receptor. Thus, an as yet unknown Ro-31-8220-sensitive kinase regulates l-plastin phosphorylation in response to the high-affinity fMLP receptor. The results suggest a model in which receptor subtypes induce a similar endpoint event through different signal-transduction intermediates. This may be relevant in the context of cell migration in which one receptor subpopulation may become desensitized in a concentration gradient of chemoattractant.

Synergetic Roles of Formyl Peptide Receptor 1 Oligomerization in Ligand-Induced Signal Transduction

2020 ◽  
Vol 15 (9) ◽  
pp. 2577-2587
Author(s):  
Tomoki Nishiguchi ◽  
Hideaki Yoshimura ◽  
Rinshi S. Kasai ◽  
Takahiro K. Fujiwara ◽  
Takeaki Ozawa
Keyword(s):  
Signal Transduction ◽  
Formyl Peptide Receptor ◽  
Peptide Receptor ◽  
Formyl Peptide ◽  
Induced Signal

Chemotaxis of chinese hamster ovary cells expressing the human neutrophil formyl peptide receptor: role of signal transduction molecules and alpha5beta1 integrin

1998 ◽  
Vol 111 (14) ◽  
pp. 1921-1928 ◽  
Author(s):  
H.M. Miettinen ◽  
J.M. Gripentrog ◽  
A.J. Jesaitis
Keyword(s):  
Signal Transduction ◽  
Chinese Hamster Ovary ◽  
Cho Cells ◽  
Kinase Inhibitor ◽  
Chinese Hamster ◽  
Formyl Peptide Receptor ◽  
Chemotactic Migration ◽  
Peptide Receptor ◽  
Formyl Peptide ◽  
Phosphoinositide 3 Kinase

Activation of the N-formyl peptide receptor (FPR) of human neutrophils by ligands such as N-formyl-methionine-leucine-phenylalanine (fMLP) induces mobilization of intracellular calcium, cell adhesion, chemotaxis, superoxide production and degranulation. Chinese hamster ovary (CHO) cells are normally devoid of FPR and unresponsive to fMLP, but when stably transfected with a human FPR cDNA, exhibited some of these same responses. Specifically, stimulation with fMLP resulted in release of intracellular calcium and chemotactic migration toward a gradient of fMLP. As in neutrophils, both processes were inhibited through receptor desensitization by prior exposure to a higher or equal concentration of ligand or by treatment with pertussis toxin. Soluble and membrane-bound fibronectin greatly increased fMLP-induced chemotaxis of CHO cells expressing FPR, but not of wild-type CHO cells, suggesting a role for FPR in activation of integrin function. Evidence for this hypothesis was obtained by demonstrating that CHO cells expressing FPR rapidly increased their adhesion to a fibronectin-coated surface after stimulation with fMLP. Both chemotaxis and adhesion were largely inhibited by RGDS peptide and a function-blocking antibody against alpha5 integrin. FPR-mediated chemotaxis of the CHO transfectants was partly inhibited by a tyrosine kinase inhibitor, herbimycin A, and blocked by a phosphoinositide 3-kinase inhibitor, wortmannin. These data suggest that stimulation of CHO FPR transfectants with a gradient of fMLP results in phosphoinositide 3-kinase-dependent chemotactic migration, which is enhanced by binding of activated alpha5beta1 to fibronectin. This non-myeloid, non-lymphoid fibroblastic cell line will thus serve as a useful model to investigate additional requirements of signal transduction molecules, adhesion molecules and cytoskeletal elements in FPR-mediated chemotaxis.

scholarly journals Signal Transduction by the Formyl Peptide Receptor

1995 ◽  
Vol 270 (47) ◽  
pp. 28010-28013 ◽  
Author(s):  
T. Amatruda Thomas ◽  
Sasa Dragas-Graonic ◽  
Richard Holmes ◽  
H. Daniel Perez
Keyword(s):  
Signal Transduction ◽  
Formyl Peptide Receptor ◽  
Peptide Receptor ◽  
Formyl Peptide
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