Korherr C, Hofmeister R, Wesche H, Falk W
Department of Internal Medicine I, University of Regensburg, Germany.
Eur J Immunol. 1997 Jan;27(1):262-7. doi: 10.1002/eji.1830270139.
Interleukin-1 (IL-1) is a central molecule in inflammation and immune responses whose pleiotropic activities are mediated by the type I IL-1 receptor (IL-1RI). The IL-1RI alone on the cell surface is silent after binding of the ligand. We show that the recently identified IL-1RI accessory protein (IL-1RAcP) converts the silent into a fully functional IL-1RI complex. Although transfection of IL-1RAcP into IL-1RAcP-deficient EL4D6/76 cells did not alter the binding kinetics or dissociation constants of the 125I-labeled IL-1alpha/IL-1RI complex, a very early event, internalization of the activated receptor complex, and a late event, IL-1-stimulated IL-2 production, were successfully restored. Therefore, recruitment of IL-1RAcP is a critical early step in the signaling cascade mediated by the IL-1RI activation complex.
白细胞介素-1（IL-1）是炎症和免疫反应中的核心分子，其多效性活动由I型IL-1受体（IL-1RI）介导。细胞表面单独的IL-1RI在配体结合后处于沉默状态。我们发现，最近鉴定出的IL-1RI辅助蛋白（IL-1RAcP）可将沉默的IL-1RI转变为功能完全的IL-1RI复合物。虽然将IL-1RAcP转染到缺乏IL-1RAcP的EL4D6/76细胞中，并未改变125I标记的IL-1α/IL-1RI复合物的结合动力学或解离常数，但一个非常早期的事件，即活化受体复合物的内化，以及一个晚期事件，即IL-1刺激的IL-2产生，均成功恢复。因此，IL-1RAcP的募集是IL-1RI活化复合物介导的信号级联反应中的关键早期步骤。
