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Formylpeptide receptor 2: Nomenclature, structure, signalling and translational perspectives: IUPHAR review 35
We discuss the fascinating pharmacology of formylpeptide receptor 2 (FPR2; often referred to as FPR2/ALX since it binds lipoxin A(4)). Initially identified as a low‐affinity ‘relative’ of FPR1, FPR2 presents complex and diverse biology. For instance, it is activated by several classes of agonists (f...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
John Wiley and Sons Inc.
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9545948/ https://www.ncbi.nlm.nih.gov/pubmed/35797341 http://dx.doi.org/10.1111/bph.15919 |
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author | Qin, Cheng Xue Norling, Lucy V. Vecchio, Elizabeth A. Brennan, Eoin P. May, Lauren T. Wootten, Denise Godson, Catherine Perretti, Mauro Ritchie, Rebecca H. |
author_facet | Qin, Cheng Xue Norling, Lucy V. Vecchio, Elizabeth A. Brennan, Eoin P. May, Lauren T. Wootten, Denise Godson, Catherine Perretti, Mauro Ritchie, Rebecca H. |
author_sort | Qin, Cheng Xue |
collection | PubMed |
description | We discuss the fascinating pharmacology of formylpeptide receptor 2 (FPR2; often referred to as FPR2/ALX since it binds lipoxin A(4)). Initially identified as a low‐affinity ‘relative’ of FPR1, FPR2 presents complex and diverse biology. For instance, it is activated by several classes of agonists (from peptides to proteins and lipid mediators) and displays diverse expression patterns on myeloid cells as well as epithelial cells and endothelial cells, to name a few. Over the last decade, the pharmacology of FPR2 has progressed from being considered a weak chemotactic receptor to a master‐regulator of the resolution of inflammation, the second phase of the acute inflammatory response. We propose that exploitation of the biology of FPR2 offers innovative ways to rectify chronic inflammatory states and represents a viable avenue to develop novel therapies. Recent elucidation of FPR2 structure will facilitate development of the anti‐inflammatory and pro‐resolving drugs of next decade. |
format | Online Article Text |
id | pubmed-9545948 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | John Wiley and Sons Inc. |
record_format | MEDLINE/PubMed |
spelling | pubmed-95459482022-10-14 Formylpeptide receptor 2: Nomenclature, structure, signalling and translational perspectives: IUPHAR review 35 Qin, Cheng Xue Norling, Lucy V. Vecchio, Elizabeth A. Brennan, Eoin P. May, Lauren T. Wootten, Denise Godson, Catherine Perretti, Mauro Ritchie, Rebecca H. Br J Pharmacol Invited Review We discuss the fascinating pharmacology of formylpeptide receptor 2 (FPR2; often referred to as FPR2/ALX since it binds lipoxin A(4)). Initially identified as a low‐affinity ‘relative’ of FPR1, FPR2 presents complex and diverse biology. For instance, it is activated by several classes of agonists (from peptides to proteins and lipid mediators) and displays diverse expression patterns on myeloid cells as well as epithelial cells and endothelial cells, to name a few. Over the last decade, the pharmacology of FPR2 has progressed from being considered a weak chemotactic receptor to a master‐regulator of the resolution of inflammation, the second phase of the acute inflammatory response. We propose that exploitation of the biology of FPR2 offers innovative ways to rectify chronic inflammatory states and represents a viable avenue to develop novel therapies. Recent elucidation of FPR2 structure will facilitate development of the anti‐inflammatory and pro‐resolving drugs of next decade. John Wiley and Sons Inc. 2022-07-29 2022-10 /pmc/articles/PMC9545948/ /pubmed/35797341 http://dx.doi.org/10.1111/bph.15919 Text en © 2022 The Authors. British Journal of Pharmacology published by John Wiley & Sons Ltd on behalf of British Pharmacological Society. https://creativecommons.org/licenses/by/4.0/This is an open access article under the terms of the http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Invited Review Qin, Cheng Xue Norling, Lucy V. Vecchio, Elizabeth A. Brennan, Eoin P. May, Lauren T. Wootten, Denise Godson, Catherine Perretti, Mauro Ritchie, Rebecca H. Formylpeptide receptor 2: Nomenclature, structure, signalling and translational perspectives: IUPHAR review 35 |
title | Formylpeptide receptor 2: Nomenclature, structure, signalling and translational perspectives: IUPHAR review 35 |
title_full | Formylpeptide receptor 2: Nomenclature, structure, signalling and translational perspectives: IUPHAR review 35 |
title_fullStr | Formylpeptide receptor 2: Nomenclature, structure, signalling and translational perspectives: IUPHAR review 35 |
title_full_unstemmed | Formylpeptide receptor 2: Nomenclature, structure, signalling and translational perspectives: IUPHAR review 35 |
title_short | Formylpeptide receptor 2: Nomenclature, structure, signalling and translational perspectives: IUPHAR review 35 |
title_sort | formylpeptide receptor 2: nomenclature, structure, signalling and translational perspectives: iuphar review 35 |
topic | Invited Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9545948/ https://www.ncbi.nlm.nih.gov/pubmed/35797341 http://dx.doi.org/10.1111/bph.15919 |
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