|ZFIN ID: ZDB-PUB-020618-3|
Cloning, structural characterization and functional expression of a zebrafish bradykinin B2-related receptor
Dunér, T., Conlon, J.M., Kukkonen, J.P., Akerman, K.E.O., Yan, Y.-L., Postlethwait, J.H., and Larhammar, D.
|Source:||The Biochemical journal 364(3): 817-824 (Journal)|
|Registered Authors:||Dunér, Torun, Larhammar, Dan, Postlethwait, John H., Yan, Yi-Lin|
|Keywords:||Ca2+; chromosome; G-protein-coupled receptor; evolution; teleost; trout|
|PubMed:||12049646 Full text @ Biochem. J.|
Dunér, T., Conlon, J.M., Kukkonen, J.P., Akerman, K.E.O., Yan, Y.-L., Postlethwait, J.H., and Larhammar, D. (2002) Cloning, structural characterization and functional expression of a zebrafish bradykinin B2-related receptor. The Biochemical journal. 364(3):817-824.
ABSTRACTThe actions of bradykinin (BK) in mammals are mediated through the activation of the B1 and B2 BK receptors. The only BK receptor that has been cloned from a non-mammalian species is a B2-like receptor from the chicken (termed the ornithokinin receptor). Pharmacological studies have demonstrated the presence of BK receptors in tissues of teleost fishes , such as trout and cod, but the ligand-binding properties of these receptors differ appreciably from those of the mammalian and chicken receptors. We report here the cloning of a B2-like receptor in zebrafish that shares 35% identity with human B2 and 30% identity with human B1. Phylogenetic analyses confirm a closer relationship with B2 than B1. The receptor gene was mapped to linkage group 17, which is syntenic to the human B2-B1 gene region. After functional expression of the zebrafish B2 receptor in mammalian cells, nanomolar concentrations of trout BK ([Arg (0),Trp(5),Leu(8)]-BK) and the derivative [des-Arg(0),Trp(5),Leu(8)]-BK (where 'des' indicates a missing amino acid) induced a significant transient rise in intracellular free Ca(2+). The B1-selective analogue [ Arg(0),Trp(5),Leu(8),des-Arg(9)]-BK was inactive at nanomolar concentrations. Taken together, these results strongly support the gene' s identity as a piscine orthologue of the mammalian B2 receptor.