Pharmacological characterization of ligand-receptor interactions at the zebrafish bradykinin receptor

T. Bromee, J. P. Kukkonen, P. Andersson, J. M. Conlon, D. Larhammar

Research output: Contribution to journalArticleScientificpeer-review

Abstract

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.
Original languageEnglish
JournalBritish Journal of Pharmacology
Volume144
Issue number1
Pages (from-to)11-16
Number of pages6
ISSN0007-1188
DOIs
Publication statusPublished - 2005
Externally publishedYes
MoE publication typeA1 Journal article-refereed

Bibliographical note

Bromee, Torun Kukkonen, Jyrki P Andersson, Per Conlon, J Michael Larhammar, Dan Comparative Study Research Support, Non-U.S. Gov't England British journal of pharmacology Br J Pharmacol. 2005 Jan;144(1):11-6.

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