IRS-1 is a common element in insulin and insulin-like growth factor-I signaling to the phosphatidylinositol 3'-kinase.
IRS-1 is a common element in insulin and insulin-like growth factor-I signaling to the phosphatidylinositol 3'-kinase.
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DOI：
10.1210/endo.132.4.8384986
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发表时间：
1993-04
期刊：
影响因子：
4.8
通讯作者：
M. G. Myers;X. Sun;B. Cheatham;BOZENA R. Jachna;Erin Glasheen;J. Backer;M. White
中科院分区：
文献类型：
--
作者：
M. G. Myers;X. Sun;B. Cheatham;BOZENA R. Jachna;Erin Glasheen;J. Backer;M. White
IRS-1 是一种独特的胞质蛋白，在胰岛素刺激完整细胞的过程中，酪氨酸会被磷酸化，并立即与磷脂酰肌醇 3'-激酶 (PtdIns 3'-激酶) 结合。胰岛素样生长因子-I (IGF-I) 受体还介导 IRS-1 的酪氨酸磷酸化，并增加中国仓鼠卵巢细胞中与 IRS-1 结合的 PtdIns 3'-激酶活性的量。纯化的胰岛素受体和IGF-I受体在体外相似位点上磷酸化重组杆状病毒产生的IRS-1，并且磷酸化杆状病毒产生的IRS-1结合来自静止细胞裂解物的PtdIns 3'-激酶活性。用IGF-I处理细胞激活PtdIns 3'-激酶，表明IGF-I以类似于胰岛素的方式通过IRS-1与p85结合来激活PtdIns 3'-激酶。过表达 IRS-1 的中国仓鼠卵巢细胞显示 IRS-1 的酪氨酸磷酸化增加，并且这些细胞中与 IRS-1 相关的 PtdIns 3'-激酶活性更高。这些数据表明 IRS-1 是 IGF-I 和胰岛素受体信号传输的常见元件。
IRS-1 is a unique cytosolic protein that becomes tyrosine phosphorylated during insulin stimulation of intact cells and immediately associates with the phosphatidylinositol 3'-kinase (PtdIns 3'-kinase). The insulin-like growth factor-I (IGF-I) receptor also mediated the tyrosine phosphorylation of IRS-1 and increased the amount of PtdIns 3'-kinase activity bound to IRS-1 in Chinese hamster ovary cells. Purified insulin receptor and IGF-I receptor phosphorylated recombinant baculovirus-produced IRS-1 on similar sites in vitro, and phosphorylated baculovirus-produced IRS-1 bound PtdIns 3'-kinase activity from lysates of quiescent cells. Treatment of cells with IGF-I activated the PtdIns 3'-kinase, suggesting that IGF-I activates the PtdIns 3'-kinase through IRS-1 binding to p85 in a manner similar to insulin. Chinese hamster ovary cells overexpressing IRS-1 demonstrated increased tyrosine phosphorylation of IRS-1, and more PtdIns 3'-kinase activity associated with IRS-1 in these cells. These data demonstrate that IRS-1 is a common element for signal transmission by the IGF-I and insulin receptors.