| First Author | Hess JF | Year | 1994 |
| Journal | Braz J Med Biol Res | Volume | 27 |
| Issue | 8 | Pages | 1725-31 |
| PubMed ID | 7749364 | Mgi Jnum | J:26931 |
| Mgi Id | MGI:74355 | Citation | Hess JF, et al. (1994) Cloning and pharmacological characterization of bradykinin receptors. Braz J Med Biol Res 27(8):1725-31 |
| abstractText | A human B2 bradykinin receptor cDNA was cloned from the lung fibroblast cell line, CCD-Lu. This clone was utilized to isolate a genomic clone of a mouse B2 bradykinin receptor. Both clones encode a protein that has the predicted characteristics of a seven transmembrane domain G-protein-coupled receptor. The DNA sequence of these two clones is 84% identical in the putative coding region. The clones have been heterologously expressed in a mammalian cell line lacking endogenous bradykinin receptors, COS-7, and a comparative analysis of their pharmacology was done. Both clones exhibit properties characteristic of the B2 bradykinin receptor, binding bradykinin with high affinity (KD = 0.1-0.2 nM) and binding des-Arg9 bradykinin with a very low affinity (IC50 > 5 microM). Interestingly, the mouse B2 bradykinin receptor has a 60-80 fold higher affinity than the human B2 bradykinin receptor for the peptide antagonists D-Arg0[Hyp3,Thi5,8,D-Phe7]bradykinin and D-Arg0[Hyp3,D-Phe7]bradykinin. |
