Elliot S J, Conti F G, Striker L J, Striker G E
Renal Cell Biology Group, National Institute of Diabetes and Digestive and Kidney Diseases, Bethesda, Maryland.
Horm Metab Res. 1990 Nov;22(11):557-60. doi: 10.1055/s-2007-1004972.
An insulin receptor was found on the surface of cloned mouse glomerular endothelial cells in vitro. Total specific binding was 2.5 +/- 0.3%/10(6) cells at 90 min and 22 degrees C. Analysis according to Scatchard resulted in a curvilinear plot, with a kd for the high and low affinity sites estimated at 1.41 x 10(-10) and 8.2 x 10(-8) respectively. Insulin binding decreased following 12 hour exposure to 50 ng/ml of insulin suggesting that down regulation of the receptor had occurred, an effect which was reversible. Covalent crosslinking of the receptor to 125I insulin revealed one band at Mr 125,000 by SDS-PAGE which disappeared following preincubation with excess unlabeled insulin. Insulin was also able to stimulate phosphorylation of the beta subunit. The characteristics of this insulin receptor appear very similar to that of endothelial cell types from other microvascular beds.
在体外培养的克隆小鼠肾小球内皮细胞表面发现了胰岛素受体。在90分钟和22摄氏度条件下,总特异性结合为2.5±0.3%/10(6)个细胞。根据Scatchard分析得到一条曲线,高亲和力位点和低亲和力位点的kd分别估计为1.41×10(-10)和8.2×10(-8)。暴露于50 ng/ml胰岛素12小时后,胰岛素结合减少,提示受体下调,且这种效应是可逆的。受体与125I胰岛素的共价交联在SDS-PAGE上显示出一条Mr为125,000的条带,在用过量未标记胰岛素预孵育后该条带消失。胰岛素还能够刺激β亚基的磷酸化。这种胰岛素受体的特性与其他微血管床内皮细胞类型的特性非常相似。