| First Author | Pesquero JB | Year | 1996 |
| Journal | Biochem Biophys Res Commun | Volume | 220 |
| Issue | 1 | Pages | 219-25 |
| PubMed ID | 8602848 | Mgi Jnum | J:31998 |
| Mgi Id | MGI:79500 | Doi | 10.1006/bbrc.1996.0384 |
| Citation | Pesquero JB, et al. (1996) Molecular cloning and functional characterization of a mouse bradykinin B1 receptor gene. (Correction: vol 224(1): 281). Biochem Biophys Res Commun 220(1):219-25 |
| abstractText | The gene encoding a putative mouse bradykinin B1 receptor was cloned from a genomic library by low stringency screening. Analysis of two isolated clones revealed a region which contains an open reading frame uninterrupted by introns and encodes a 334 amino acid protein, which exhibits seven potential transmembrane domains and is 68% identical to the human and rabbit bradykinin B1 receptors. Lipopolysaccharide-treatment induces B1 receptor transcripts in the heart, liver, and lung. Stable expression of the coding region in COS-7 cells resulted in high levels of binding sites for the specific B1 ligand des-ARG10 kallidin (Kd = 1.3 nM; Bmax = 51 fmol/mg protein). The rank order of affinity of the receptor for the agonists and antagonists was: des-Arg9BKdes-Arg9Leu8BKdes- Arg10kallidin >> Hoe-140=bradykinin. Functional coupling of the cloned receptor was demonstrated by the dose-dependent effects of des-Arg(9)BK on the extracellular acidification rate in stably transfected COS-7 cells. This effect was not produced by bradykinin and could be blocked by the B1 antagonist des-Arg9Leu8BK. |
