Tartare S, Ballotti R, Van Obberghen E
Institut National de la Santé et de la Recherche Médicale, INSERM U145, Faculté de Médecine, Nice, France.
FEBS Lett. 1991 Dec 16;295(1-3):219-22. doi: 10.1016/0014-5793(91)81422-5.
To determine whether heterologous receptor tyrosine kinases interact with each other we have investigated the ability of insulin receptors to transphosphorylate and transactivate IGF-I receptors. Using partially purified receptors we show that hormone-stimulated insulin receptors induced a 40% increase in IGF-I receptor phosphorylation. Remarkably, this transphosphorylation of IGF-I receptors by insulin receptors resulted in a 2.5-fold augmentation of the IGF-I receptor tyrosine kinase activity for substrates. Our findings demonstrate that transphosphorylation with transactivation can occur between insulin and IGF-I receptors. We would like to propose that such a phenomenon participates in the insulin-induced pleiotropic program by mediating the growth promoting effects of the hormone.
为了确定异源受体酪氨酸激酶是否相互作用，我们研究了胰岛素受体对胰岛素样生长因子-I（IGF-I）受体进行转磷酸化和转激活的能力。使用部分纯化的受体，我们发现激素刺激的胰岛素受体可使IGF-I受体的磷酸化增加40%。值得注意的是，胰岛素受体对IGF-I受体的这种转磷酸化导致IGF-I受体对底物的酪氨酸激酶活性增强了2.5倍。我们的研究结果表明，胰岛素和IGF-I受体之间可发生伴有转激活的转磷酸化。我们推测，这种现象通过介导激素的生长促进作用参与胰岛素诱导的多效性程序。
