Antiflammin-2 Activates the Human Formyl-Peptide Receptor Like 1
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...
Saved in:
Main Authors: | , , , , , , |
---|---|
Format: | Article |
Language: | English |
Published: |
Wiley
2006-01-01
|
Series: | The Scientific World Journal |
Online Access: | http://dx.doi.org/10.1100/tsw.2006.247 |
Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
_version_ | 1832545481456091136 |
---|---|
author | Ahmad M. Kamal Richard P.G. Hayhoe Anbalakan Paramasivam Dianne Cooper Roderick J. Flower Egle Solito Mauro Perretti |
author_facet | Ahmad M. Kamal Richard P.G. Hayhoe Anbalakan Paramasivam Dianne Cooper Roderick J. Flower Egle Solito Mauro Perretti |
author_sort | Ahmad M. Kamal |
collection | DOAJ |
description | 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 EC50 of 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. |
format | Article |
id | doaj-art-f5939587e79f46a59d0e9f2b49c69f48 |
institution | Kabale University |
issn | 1537-744X |
language | English |
publishDate | 2006-01-01 |
publisher | Wiley |
record_format | Article |
series | The Scientific World Journal |
spelling | doaj-art-f5939587e79f46a59d0e9f2b49c69f482025-02-03T07:25:43ZengWileyThe Scientific World Journal1537-744X2006-01-0161375138410.1100/tsw.2006.247Antiflammin-2 Activates the Human Formyl-Peptide Receptor Like 1Ahmad M. Kamal0Richard P.G. Hayhoe1Anbalakan Paramasivam2Dianne Cooper3Roderick J. Flower4Egle Solito5Mauro Perretti6William Harvey Research Institute, Charterhouse Square, London EC1M 6BQ, UKWilliam Harvey Research Institute, Charterhouse Square, London EC1M 6BQ, UKWilliam Harvey Research Institute, Charterhouse Square, London EC1M 6BQ, UKWilliam Harvey Research Institute, Charterhouse Square, London EC1M 6BQ, UKWilliam Harvey Research Institute, Charterhouse Square, London EC1M 6BQ, UKDivision of Neuroscience and Mental Health Imperial College London Hammersmith Hospital Campus, London W12 0NN, UKWilliam Harvey Research Institute, Charterhouse Square, London EC1M 6BQ, UKThe 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 EC50 of 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.http://dx.doi.org/10.1100/tsw.2006.247 |
spellingShingle | Ahmad M. Kamal Richard P.G. Hayhoe Anbalakan Paramasivam Dianne Cooper Roderick J. Flower Egle Solito Mauro Perretti Antiflammin-2 Activates the Human Formyl-Peptide Receptor Like 1 The Scientific World Journal |
title | Antiflammin-2 Activates the Human Formyl-Peptide Receptor Like 1 |
title_full | Antiflammin-2 Activates the Human Formyl-Peptide Receptor Like 1 |
title_fullStr | Antiflammin-2 Activates the Human Formyl-Peptide Receptor Like 1 |
title_full_unstemmed | Antiflammin-2 Activates the Human Formyl-Peptide Receptor Like 1 |
title_short | Antiflammin-2 Activates the Human Formyl-Peptide Receptor Like 1 |
title_sort | antiflammin 2 activates the human formyl peptide receptor like 1 |
url | http://dx.doi.org/10.1100/tsw.2006.247 |
work_keys_str_mv | AT ahmadmkamal antiflammin2activatesthehumanformylpeptidereceptorlike1 AT richardpghayhoe antiflammin2activatesthehumanformylpeptidereceptorlike1 AT anbalakanparamasivam antiflammin2activatesthehumanformylpeptidereceptorlike1 AT diannecooper antiflammin2activatesthehumanformylpeptidereceptorlike1 AT roderickjflower antiflammin2activatesthehumanformylpeptidereceptorlike1 AT eglesolito antiflammin2activatesthehumanformylpeptidereceptorlike1 AT mauroperretti antiflammin2activatesthehumanformylpeptidereceptorlike1 |