ZFIN ID: ZDB-PUB-041208-13
Pharmacological characterization of ligand-receptor interactions at the zebrafish bradykinin receptor
Bromee, T., Kukkonen, J.P., Andersson, P., Conlon, J.M., and Larhammar, D.
Date: 2005
Source: British journal of pharmacology   144(1): 11-16 (Journal)
Registered Authors: Larhammar, Dan
Keywords: none
MeSH Terms:
  • Alanine/chemistry
  • Amino Acid Substitution
  • Amino Acids/chemistry
  • Animals
  • Bradykinin/analogs & derivatives*
  • Bradykinin/chemistry
  • Bradykinin/metabolism
  • Bradykinin/pharmacology*
  • Bradykinin Receptor Antagonists*
  • Cell Line
  • Humans
  • Inositol Phosphates/analysis
  • Inositol Phosphates/biosynthesis
  • Ligands
  • Molecular Structure
  • Receptors, Bradykinin/drug effects*
  • Receptors, Bradykinin/genetics
  • Species Specificity
  • Transfection
  • Zebrafish/physiology*
PubMed: 15644864 Full text @ Br. J. Pharmacol.
Ligand interactions of a piscine bradykinin (BK) receptor expressed in vitro have been characterized for the first time by measuring inositol phosphate accumulation. 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. 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. 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.