Bei M, Lavigne M C, Foegh M L, Ramwell P W, Clarke R
Department of Physiology and Biophysics, Georgetown University Medical School, Washington DC 20007, USA.
J Steroid Biochem Mol Biol. 1996 Apr;58(1):83-8. doi: 10.1016/0960-0760(96)00005-2.
We report the expression and characteristics of the estrogen receptor in rat coronary artery-derived smooth muscle cells. Polymerase chain reaction analyses of total and poly(A) + mRNA from rat coronary artery-derived smooth muscle cells indicate the presence of estrogen receptor mRNA. Binding analyses reveal the presence of high affinity binding sites for 17 beta-estradiol, with a Kd equivalent to that observed for authentic estrogen receptors in other estrogen responsive tissues. Scatchard and Hill plot analyses of the properties of receptor-ligand binding indicate the presence of a single site, and the absence of cooperative binding. Unlabeled E2 but not testosterone, dexamethasone or progesterone compete with [3H] 17 beta-estradiol for binding sites. The affinity, specificity and non-cooperative nature of the estrogen binding sites are identical to those observed in other estrogen-responsive tissues. These cells may provide a novel model in which to study the effects of estrogens on the proliferation, differentiation and function of vascular smooth muscle cells.
我们报道了大鼠冠状动脉来源的平滑肌细胞中雌激素受体的表达及特性。对大鼠冠状动脉来源的平滑肌细胞的总mRNA和聚腺苷酸加尾mRNA进行聚合酶链反应分析，结果表明存在雌激素受体mRNA。结合分析显示存在对17β-雌二醇的高亲和力结合位点，其解离常数与在其他雌激素反应性组织中观察到的真实雌激素受体的解离常数相当。对受体-配体结合特性进行Scatchard和Hill作图分析表明存在单一结合位点，且不存在协同结合。未标记的雌二醇（E2）而非睾酮、地塞米松或孕酮能与[3H] 17β-雌二醇竞争结合位点。雌激素结合位点的亲和力、特异性和非协同性质与在其他雌激素反应性组织中观察到的相同。这些细胞可能为研究雌激素对血管平滑肌细胞增殖、分化和功能的影响提供一个新的模型。
