卡托普利可增加牛冠状动脉内皮细胞中缓激肽受体结合位点的亲和力。

Captopril increases the affinity of bradykinin receptor binding sites in bovine coronary arterial endothelial cells.

作者信息

Miyamoto A, Matsuyama T, Ishiguro S, Nishio A

机构信息

Department of Veterinary Pharmacology, Faculty of Agriculture, Kagoshima University, Japan.

出版信息

Jpn J Pharmacol. 2000 Sep;84(1):82-5. doi: 10.1254/jjp.84.82.

DOI:10.1254/jjp.84.82

PMID:11043459

Abstract

In a radioligand binding study using bovine coronary artery endothelial cell membranes, captopril changed a single bradykinin (BK) binding site (Kd = 1.77 nM, Bmax = 60.2 fmol/mg protein) to high- (Kd = 0.68 pM, Bmax = 17.7 fmol/mg protein) and low- (Kd = 1.00 nM, Bmax = 72.5 fmol/mg protein) affinity binding sites. This effect was reversed by GppNHp. Captopril also enhanced BK-induced endothelium-dependent relaxation in saponin-treated coronary rings, and GppNHp partially suppressed this enhancement. These results suggest that captopril may affect BK receptors that couple to G-proteins.

摘要

在一项使用牛冠状动脉内皮细胞膜的放射性配体结合研究中，卡托普利将单一的缓激肽（BK）结合位点（解离常数Kd = 1.77 nM，最大结合量Bmax = 60.2 fmol/mg蛋白质）转变为高亲和力（Kd = 0.68 pM，Bmax = 17.7 fmol/mg蛋白质）和低亲和力（Kd = 1.00 nM，Bmax = 72.5 fmol/mg蛋白质）结合位点。该效应可被鸟苷5'-三磷酸3'-氨甲基三磷酸（GppNHp）逆转。卡托普利还增强了皂角苷处理的冠状动脉环中BK诱导的内皮依赖性舒张，且GppNHp部分抑制了这种增强作用。这些结果表明，卡托普利可能会影响与G蛋白偶联的BK受体。