Studies on the molecular basis of insulin actions

与伦敦的M.Waterfield教授合作，我们发现与IRS-1相关的磷酸肌醇3-激酶介导胰岛素对葡萄糖转运（葡萄糖转运蛋白的易位）和膜皱褶的刺激作用。我们还发现一个与IRS-1结合的接头蛋白Nck在体外可与116 kDa和130 kDa两种蛋白结合。我们与巴斯的G.Holman教授合作，发现磷酸肌醇3-激酶的抑制剂渥曼青霉素（wortmannin）抑制胰岛素对3 T3-L1脂肪细胞中葡萄糖转运（GLUT 4从细胞质转移到质膜）的刺激作用。此外，我们分析了在渥曼青霉素和胰岛素存在下GLUT 4的动力学，并得出结论，渥曼青霉素抑制胰岛素对3 T3-L1脂肪细胞中GLUT 4的胞吐的刺激作用，但不抑制胞吞。

In collaboration with Professor M.Waterfield in London, we found phosphoinositide 3-kinases associated with IRS-1 mediate the stimulatory effect of insulin on the glucose transport (translocation of glucose transporters) and membrane ruffling. We also found that an adaptor protein Nck, which binds to IRS-1, associates two proteins of 116kDa and 130kDa in vitro. The amino acid sequence of these proteins was analyzed in Professor Waterfield's laboratory and we cloned the cDNA of these two proteins.In collaboration with Professor G.Holman in Bath, we found that wortmannin, an inhibitor of phosphoinositide 3-kinase, inhibits the stimulatory effect of insulin on glucose transport (translocation of GLUT4 from cytosols to plasma membranes) in 3T3-L1 adipocytes. Furthermore, we analyzed the kinetics of GLUT4 in the presence of wortmannin and insulin and concluded that wortmannin inhibited the stimulatory effect of insulin on the exocytosis, but not the endocytosis, of GULT4 in 3T3-L1 adipocytes.