Almira E C, Reddy W J
Endocrinology. 1979 Jan;104(1):205-11. doi: 10.1210/endo-104-1-205.
Binding of [125I]iodoinsulin to isolated hepatocytes from fed and fasted rats was measured. Hepatocytes from fed rats bound significanlty more [125I]iodoinsulin at insulin concentrations ranging from 0.15--100 nM. Scatchard and average affinity profile data analyses showed no significant difference in the affinities of the binding sites but indicated a decrease in the receptor concentration of the hepatocytes from fasted rats. In contrast to hepatocytes, liver plasma membranes of fasted rats showed increased insulin binding at all insulin concentrations, except the highest level of 100 nM. Analysis of the data indicated a significant increase in the affinity of the receptors but no change in the receptor concentration. Evidence is presented that the differences in the results obtained with hepatocytes and membranes were not due to the differences in the recovery of the plasma membranes. The results suggest that insulin binding by intact hepatocytes does not necessarily reflect the receptor protein content of the cell membrane and that the liver cell modulates its response to insulin by changes in the architecture of the plasma membrane.
测定了[125I]碘胰岛素与喂食及禁食大鼠分离的肝细胞的结合情况。在0.15至100 nM的胰岛素浓度范围内,喂食大鼠的肝细胞结合的[125I]碘胰岛素显著更多。Scatchard分析和平均亲和力图谱数据分析表明,结合位点的亲和力无显著差异,但显示禁食大鼠肝细胞的受体浓度降低。与肝细胞相反,禁食大鼠的肝细胞膜在所有胰岛素浓度下(除了最高的100 nM水平)均显示胰岛素结合增加。数据分析表明受体亲和力显著增加,但受体浓度无变化。有证据表明,肝细胞和细胞膜所获结果的差异并非由于质膜回收率的差异。结果表明,完整肝细胞对胰岛素的结合不一定反映细胞膜的受体蛋白含量,并且肝细胞通过质膜结构的变化来调节其对胰岛素的反应。