Matić G, Trajković D, Damjanović S, Petrović J
Department of Molecular Biology and Biochemistry, Sinisa Stanković Institute for Biological Research, Belgrade, Yugoslavia.
Biochim Biophys Acta. 1990 Feb 19;1051(2):192-8. doi: 10.1016/0167-4889(90)90193-h.
Stability-, equilibrium- and kinetic binding parameters, transformation rate and sedimentation properties of liver cytosol glucocorticoid receptor from insulin-treated rats were studied. 40% elevation of cytosolic glucocorticoid binding and a lower affinity of the receptor for ligand were observed in hypoglycemic rats as compared to the controls. A small but significant decrease of [3H]triamcinolone acetonide-receptor complexes association rate and an increase of dissociation rate were also found. The rate and the extent of activation of the complexes from insulin-treated rats were somewhat higher compared to the controls, and the complexes from both groups showed higher affinity for the nuclei isolated from insulin-treated animals. Mixing experiments suggested that insulin treatment lead to alterations at the level of both the receptor protein and the nuclear binding sites. Sedimentation properties of transformed and untransformed receptor remained unchanged upon insulin treatment. The physiological relevance of the data was confirmed by hypoglycemia-related stimulation of tyrosine aminotransferase induction by dexamethasone.
研究了胰岛素处理大鼠肝脏胞质溶胶糖皮质激素受体的稳定性、平衡和动力学结合参数、转化率及沉降特性。与对照组相比，低血糖大鼠的胞质糖皮质激素结合增加了40%，且受体对配体的亲和力降低。还发现[3H]曲安奈德 - 受体复合物的缔合速率略有但显著下降，解离速率增加。与对照组相比，胰岛素处理大鼠的复合物活化速率和程度略高，且两组的复合物对从胰岛素处理动物分离的细胞核显示出更高的亲和力。混合实验表明，胰岛素处理导致受体蛋白和核结合位点水平均发生改变。胰岛素处理后，转化和未转化受体的沉降特性保持不变。地塞米松诱导酪氨酸转氨酶的低血糖相关刺激证实了这些数据的生理相关性。
