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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...

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Autores principales: Qin, Cheng Xue, Norling, Lucy V., Vecchio, Elizabeth A., Brennan, Eoin P., May, Lauren T., Wootten, Denise, Godson, Catherine, Perretti, Mauro, Ritchie, Rebecca H.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley and Sons Inc. 2022
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.
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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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