This report describes the characterisation of cloned rat and human bradykin
in B-1 receptors in African green monkey kidney fibroblast (Cos-7) cells. A
ligand binding assay with [H-3]des-Arg(10)-kallidin was used to compare th
eir pharmacology with respect to known bradykinin B-1 and B-2 receptor liga
nds. In addition, the pharmacology of T-kinin and its' derivative des-Arg(1
1)-T-kinin was investigated. The cloned rat receptor had a similar pharmaco
logy to that of the recently described mouse receptor and differs from that
described for the human receptor. The rat receptor had a higher affinity f
or des-Arg(11)-T-kinin than the human receptor. These differences in pharma
cological properties may relate to the presence of T-kinin, bradykinin and
their des-Arg derivatives as the major physiological peptides in rat and th
e predominance of kallidin and its derivatives in human. We confirm that th
e rat bradykinin B-1 receptor gene is organised in a two exon structure and
differs from the human gene which has a three exon structure and we furthe
r examine the inducible expression of this gene in a wide range of tissues
using Northern blotting. (C) 1999 Elsevier Science B.V. All rights reserved
.