Formylpeptide receptors in GtoPdb v.2021.2

Magnus Bäck; François Boulay; Nan Chiang; Sven-Erik Dahlén; Claes Dahlgren; Jeffrey Drazen; Jilly F. Evans; Craig Gerard; Philip M. Murphy; Marc Parmentier; Mark Quinn; G. Enrico Rovati; Charles N. Serhan; Takao Shimizu; Ji Ming Wang; Richard D. Ye; Takehiko Yokomizo

doi:10.2218/gtopdb/F23/2021.2

Magnus Bäck Karolinska Institutet https://orcid.org/0000-0003-0853-5141
François Boulay Commissariat à l’Energie Atomique
Nan Chiang Brigham and Women's Hospital https://orcid.org/0000-0003-1963-1585
Sven-Erik Dahlén Karolinska Institutet https://orcid.org/0000-0002-4993-4002
Claes Dahlgren University of Göteborg
Jeffrey Drazen Harvard University
Jilly F. Evans PharmAkea
Craig Gerard Harvard Medical School and Children's Hospital
Philip M. Murphy National Institutes of Health
Marc Parmentier Université Libre de Bruxelles
Mark Quinn Montana State University
G. Enrico Rovati University of Milan https://orcid.org/0000-0002-8788-9783
Charles N. Serhan Harvard University https://orcid.org/0000-0003-4627-8545
Takao Shimizu University of Tokyo
Ji Ming Wang Frederick National Laboratory for Cancer Research
Richard D. Ye The Chinese University of Hong Kong, Shenzhen
Takehiko Yokomizo Juntendo University

Abstract

The formylpeptide receptors (nomenclature agreed by the NC-IUPHAR Subcommittee on the formylpeptide receptor family [196]) respond to exogenous ligands such as the bacterial product fMet-Leu-Phe (fMLP) and endogenous ligands such as lipoxin A₄ (LXA₄), 15-epi-lipoxin A₄, annexin I , cathepsin G, amyloid β42, serum amyloid A and spinorphin, derived from β-haemoglobin. FPR1 also serves as a plague receptor for selective destruction of human immune cells by Y. pestis [135]. The FPR1/2 agonists 'compound 17b' and 'compound 43' have shown cardiac protective functions [149, 64].

DOI: https://doi.org/10.2218/gtopdb/F23/2021.2