Göransson O, Wijkander J, Manganiello V, Degerman E
Department of Cell and Molecular Biology, Lund University, Sweden.
Biochem Biophys Res Commun. 1998 May 8;246(1):249-54. doi: 10.1006/bbrc.1998.8602.
Protein kinase B (PKB) has previously been shown to be activated in response to insulin and growth factor stimulation. The activation mechanism has been suggested to involve translocation of PKB to membranes, where it is phosphorylated and activated. Insulin-induced translocation of PKB has not been demonstrated in a physiological target cell. Therefore we have used the primary rat adipocyte to investigate insulin-induced translocation of PKB. In the presence of 1 nM insulin translocation of PKB was detected within 30 seconds and was blocked by wortmannin, a selective phosphatidylinositol 3-kinase inhibitor. This translocation was potentiated by the tyrosine phosphatase inhibitor vanadate. Subcellular localization studies revealed that PKB translocated to the plasma membrane.
蛋白激酶B（PKB）先前已被证明可响应胰岛素和生长因子刺激而被激活。其激活机制被认为涉及PKB向细胞膜的转位，在细胞膜上它被磷酸化并激活。胰岛素诱导的PKB转位尚未在生理靶细胞中得到证实。因此，我们使用原代大鼠脂肪细胞来研究胰岛素诱导的PKB转位。在存在1 nM胰岛素的情况下，30秒内即可检测到PKB的转位，并且被选择性磷脂酰肌醇3激酶抑制剂渥曼青霉素所阻断。酪氨酸磷酸酶抑制剂钒酸盐可增强这种转位。亚细胞定位研究表明，PKB转位至质膜。
