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Pharmacological characterization of ligand–receptor interactions at the zebrafish bradykinin receptor
Author(s) -
Bromée Torun,
Kukkonen Jyrki P,
Andersson Per,
Conlon J Michael,
Larhammar Dan
Publication year - 2005
Publication title -
british journal of pharmacology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.432
H-Index - 211
eISSN - 1476-5381
pISSN - 0007-1188
DOI - 10.1038/sj.bjp.0706032
Subject(s) - receptor , agonist , bradykinin , bradykinin receptor , competitive antagonist , ligand (biochemistry) , chemistry , kinin , receptor antagonist , biochemistry , biology , antagonist
1 Ligand interactions of a piscine bradykinin (BK) receptor expressed in vitro have been characterized for the first time by measuring inositol phosphate accumulation. 2 The ligands were analogues of zebrafish BK with serial substitutions by D ‐amino acids or alanine. Substitutions at residues Arg 1 , Gly 4 , Ser 6 , Pro 7 , Leu 8 and Arg 9 caused greatly reduced potency and maximum response. The Pro 3 → Ala analogue had higher potency but lower maximum response. 3 The peptide HOE140 was a weak partial agonist although it is an antagonist at the human B2 receptor and a potent agonist at chicken B2. 4 Thus, cloned zebrafish BK receptor reveals a ligand‐interaction profile that is distinct from mammalian B1 and B2 receptors and from the previously characterized BK receptor in trout stomach, but similar to the receptor in cod intestine. These results increase our understanding of the evolution of BK receptors and the functions of the kallikrein–kinin system.British Journal of Pharmacology (2005) 144 , 11–16. doi: 10.1038/sj.bjp.0706032