Insulin-dependent alterations of phorbol ester binding to adipocyte subcellular constituents. Evidence for the involvement of protein kinase C in insulin action.
Insulin-dependent alterations of phorbol ester binding to adipocyte subcellular constituents. Evidence for the involvement of protein kinase C in insulin action.
复制标题
佛波酯与脂肪细胞亚细胞成分结合的胰岛素依赖性改变。
DOI：
10.1016/0006-291x(87)91591-9
复制
发表时间：
1987
影响因子：
3.1
通讯作者：
McDonald,JM
中科院分区：
文献类型：
--
作者：
Pershadsingh,HA;Shade,DL;McDonald,JM
利用氚化磷酸- 12,13 -二丁酸（3H-PBu2）的结合来估计从未处理和胰岛素处理的脂肪细胞中分离的与质膜和细胞质相关的蛋白激酶C的质量。3h - pbu2与质膜和细胞质溶胶的结合速度很快，在几分钟内达到稳定状态。生理胰岛素浓度（0.67 mM）处理细胞后，胞浆和质膜上的磷酸酯含量分别增加42%（从0.92±0.08增加到1.30±0.12 pmol3H-PBu2/mg蛋白，p <0.0001）和27%（从0.41±0.07增加到0.30±0.05 pmol3H-PBu2/mg蛋白，p <0.020）。从对照和胰岛素处理的细胞中置换3h - pbu2到胞浆所需的未标记pbu2的半最大浓度分别为54 pM和13 pM。这些数据表明胰岛素改变脂肪细胞中的蛋白激酶C。
The binding of tritiated phorbol-12, 13-dibutyrate (3H-PBu2) was employed to estimate the mass of protein kinase C associated with plasma membranes and cytosol isolated from untreated and insulin-treated adipocytes. Binding of3H-PBu2to both plasma membranes and cytosol was rapid, achieving a steady state within minutes. Treatment of cells with physiological concentration of insulin (0.67 mM) caused a 42% increase (from 0.92 ± 0.08 to 1.30 ± 0.12 pmol3H-PBu2/mg protein, p <0.0001) and a 27% decrease (from 0.41 ± 0.07 to 0.30 ± 0.05 pmol3H-PBu2/mg protein, p <0.020) in phorbol ester bound to cytosol and plasma membranes, respectively. The half-maximal concentrations of unlabelled PBu2needed to displace 3H-PBu2bound to cytosol from control and insulin-treated cells were 54 and 13 pM, respectively. These data indicate that insulin modifies protein kinase C in adipocytes.