Two new cyclosporin folds observed in the structures of the immunosuppressant cyclosporin G and the formyl peptide receptor antagonist cyclosporin H at ultra-high resolution

2003 ◽  
Vol 1 (9) ◽  
pp. 1466-1474 ◽  
Author(s):  
Brian Potter ◽  
Rex A. Palmer ◽  
Robert Withnall ◽  
Terence C. Jenkins ◽  
Babur Z. Chowdhry
Keyword(s):  
High Resolution ◽  
Receptor Antagonist ◽  
Formyl Peptide Receptor ◽  
Peptide Receptor ◽  
Formyl Peptide ◽  
Cyclosporin H

scholarly journals PET imaging detection of macrophages with a formyl peptide receptor antagonist

2015 ◽  
Vol 42 (4) ◽  
pp. 381-386 ◽  
Author(s):  
Yi Zhang ◽  
Bijoy Kundu ◽  
Min Zhong ◽  
Tao Huang ◽  
Jing Li ◽  
...  
Keyword(s):  
Receptor Antagonist ◽  
Pet Imaging ◽  
Formyl Peptide Receptor ◽  
Peptide Receptor ◽  
Formyl Peptide ◽  
Imaging Detection

The synthetic chemoattractant Trp-Lys-Tyr-Met-Val-DMet activates neutrophils preferentially through the lipoxin A4 receptor

Blood ◽  
2000 ◽  
Vol 95 (5) ◽  
pp. 1810-1818 ◽  
Author(s):  
Claes Dahlgren ◽  
Thierry Christophe ◽  
Francois Boulay ◽  
Phoebus N. Madianos ◽  
Marie J. Rabiet ◽  
...  
Keyword(s):  
Formyl Peptide Receptor ◽  
Neutrophil Chemotaxis ◽  
Lipoxin A4 ◽  
Independent Manner ◽  
Effector Functions ◽  
Peptide Receptor ◽  
Formyl Peptide ◽  
Complement Receptor 3 ◽  
Neutrophil Response ◽  
Cyclosporin H

A D-methionine–containing peptide, Trp-Lys-Tyr-Met-Val-D-Met-NH2 (WKYMVm), featuring a unique receptor specificity was investigated with respect to its ability to activate neutrophil effector functions. The peptide was found to be more potent than the N-formylated peptide N-formyl-Met-Leu-Phe (fMLF) at inducing neutrophil chemotaxis, mobilization of neutrophil complement receptor 3 (CR3), and activation of the neutrophil NADPH-oxidase. The fact that binding of fML[3H]F was inhibited by both fMLF and WKYMVm suggests that N-formyl peptide receptor (FPR) is shared by these peptides. However, the neutrophil response induced by the WKYMVm peptide was insensitive to the fMLF antagonists, cyclosporin H, and Boc-FLFLF that specifically block the function of the FPR. These results suggest that even though WKYMVm may bind FPR the cells are activated preferentially through a receptor distinct from the FPR. Using transfected HL-60 cells expressing either the FPR or its neutrophil homologue FPRL1, also referred to as LXA4R because it has been shown to bind lipoxin A4, we show that WKYMVm is about 300-fold more active at mobilizing intracellular calcium through FPRL1 than through FPR. The WKYMVm activates FPRL1-expressing cells in a cyclosporin H-independent manner with an EC50 of around 75 pmol/L, whereas it activates FPR-expressing cells with an EC50 of around 25 nmol/L. The observation that exudated cells are primed in their response to WKYMVm suggests that FPRL1/LXA4R like FPR is stored in mobilizable organelles.

Cyclosporin H, Boc-MLF and Boc-FLFLF are Antagonists that Preferentially Inhibit Activity Triggered Through the Formyl Peptide Receptor

Inflammation ◽  
2007 ◽  
Vol 30 (6) ◽  
pp. 224-229 ◽  
Author(s):  
Anna-Lena Stenfeldt ◽  
Jennie Karlsson ◽  
Christine Wennerås ◽  
Johan Bylund ◽  
Huamei Fu ◽  
...  
Keyword(s):  
Formyl Peptide Receptor ◽  
Inhibit Activity ◽  
Peptide Receptor ◽  
Formyl Peptide ◽  
Cyclosporin H

scholarly journals An urokinase receptor antagonist that inhibits cell migration by blocking the formyl peptide receptor

FEBS Letters ◽  
2008 ◽  
Vol 582 (7) ◽  
pp. 1141-1146 ◽  
Author(s):  
Katia Bifulco ◽  
Immacolata Longanesi-Cattani ◽  
Lucia Gargiulo ◽  
Ornella Maglio ◽  
Mauro Cataldi ◽  
...  
Keyword(s):  
Cell Migration ◽  
Receptor Antagonist ◽  
Urokinase Receptor ◽  
Formyl Peptide Receptor ◽  
Peptide Receptor ◽  
Formyl Peptide
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