Insulin-activated tyrosine phosphorylation of a 15-kilodalton protein in intact 3T3-L1 adipocytes.
Insulin-activated tyrosine phosphorylation of a 15-kilodalton protein in intact 3T3-L1 adipocytes.
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完整 3T3-L1 脂肪细胞中 15 千道尔顿蛋白质的胰岛素激活酪氨酸磷酸化。
DOI：
10.1073/pnas.84.7.1844
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发表时间：
1987
影响因子：
11.1
通讯作者：
Lane,MD
中科院分区：
文献类型：
--
作者：
Bernier,M;Laird,DM;Lane,MD
胰岛素刺激15-kDa蛋白质（p15）上酪氨酸残基的磷酸化，并且胞质磷酸化蛋白质（pp 15）仅在用氧化苯胂处理3 T3-L1脂肪细胞时积累。先前已经表明，氧化苯胂，一种与邻位二硫醇络合的试剂，中断从胰岛素受体到葡萄糖转运系统的信号传递。这里提出的几条证据表明pp 15参与胰岛素受体启动的信号转导到葡萄糖转运系统。氧化苯胂对胰岛素激活的PP 15积累和胰岛素刺激的己糖摄取的相互作用被逆转的邻位二硫醇2，3-二巯基丙醇，但不是由单硫醇2-巯基乙醇。因此，细胞二硫醇似乎在pp 15下游的信号传递途径中起作用。与受体β亚基（酪氨酸上）的胰岛素激活自磷酸化一样，p15磷酸化的激活是特异性的，胰岛素样生长因子1和2、表皮生长因子和血小板衍生生长因子无活性。此外，这两个过程表现出相同的胰岛素浓度依赖性。胰岛素激活受体β亚基磷酸化的时间动力学关系，其次是磷酸化的p15，然后增加己糖摄取率，是一致的中介信号作用pp 15在胰岛素刺激的葡萄糖摄取。
Insulin stimulates phosphorylation of a tyrosine residue(s) on a 15-kDa protein (p15), and the cytosolic phosphorylated protein (pp15) accumulates only when 3T3-L1 adipocytes are treated with phenylarsine oxide. It has been shown previously that phenylarsine oxide, an agent that complexes vicinal dithiols, interrupts signal transmission from the insulin receptor to the glucose transport system. Several lines of evidence presented here indicate the involvement of pp15 in insulin receptor-initiated signal transduction to the glucose transport system. The reciprocal effects of phenylarsine oxide on the insulin-activated accumulation of pp15 and on insulin-stimulated hexose uptake are reversed by the vicinal dithiol 2,3-dimercaptopropanol but not by the monothiol 2-mercaptoethanol. Thus, a cellular dithiol appears to function in the signal transmission pathway downstream from pp15. Like the insulin-activated autophosphorylation of the receptor's beta subunit (on tyrosine), activation of phosphorylation of p15 is specific, with insulin-like growth factors 1 and 2, epidermal growth factor, and platelet-derived growth factor being inactive. Moreover, both processes exhibit identical insulin concentration dependence. The temporal kinetic relationship of insulin-activated receptor beta-subunit phosphorylation, followed by the phosphorylation of p15 and then increased hexose uptake rate, is consistent with an intermediary signaling role for pp15 in insulin-stimulated glucose uptake.