2. Academic Validation
  3. Cloning and pharmacological characterization of a human bradykinin (BK-2) receptor

Cloning and pharmacological characterization of a human bradykinin (BK-2) receptor

  • Biochem Biophys Res Commun. 1992 Apr 15;184(1):260-8. doi: 10.1016/0006-291x(92)91187-u.
J F Hess 1,  J A Borkowski,  G S Young,  C D Strader,  R W Ransom
Affiliations

Affiliation

  • 1 Merck Research Laboratories, Department of Molecular Pharmacology and Biochemistry, Rahway, N.J. 07065.
PMID: 1314587 DOI: 10.1016/0006-291x(92)91187-u
Abstract

A human BK-2 Bradykinin Receptor was cloned from the lung fibroblast cell line CCD-16Lu. The cDNA clone encodes a 364 amino acid protein that has the characteristics of a seven transmembrane domain G-protein coupled receptor. The predicted amino acid sequence of the human BK-2 receptor is 81% identical to the smooth muscle rat BK-2 receptor (1). Transfection of the human BK-2 receptor cDNA into COS-7 cells results in the expression of high levels of specific BK binding sites. Saturation binding analysis indicates that the human BK-2 receptor expressed in COS-7 cells binds BK with a KD of 0.13 nM. Pharmacological characterization of the expressed BK receptor is consistent with the cDNA encoding a receptor of the BK-2 subtype. The BK-2 receptor antagonist Hoe 140 (2), D-Arg0[Hyp3, Thi5, D-Tic7, Oic8]BK has a high affinity (IC50 = 65 pM) for the cloned human receptor. The tissue distribution of the human BK-2 receptor was analyzed by competitive PCR with human tissue cDNA and is similar to that determined for the BK-2 receptor in the rat.

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