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为了探讨人类GMCSF受体(GMR)的功能特性,将编码人GMRα和βc亚单位的cDNA转染到无GMR表达的小鼠前B细胞系BaF3中。阳性转染子功能检测表明,表达GMRα的BaF3克隆能与配体低亲和力结合(Kd=3.4nmol/L),并仅在高浓度配体诱导后出现增殖反应;而共表达GM-Rα/β的BaF3克隆则能以高亲和力方式与配体结合(Kd=99pmol/L),并表现出配体依赖性细胞增殖;增殖信号的传导与配体通过诱导βc磷酸化而活化胞浆Jak2、Shc及Shc相关蛋白P145(SHIP)有关。提示这些信号分子可能在连结造血生长因子受体与细胞有丝分裂及其它反应的“激酶瀑布”中发挥着关键作用。
In order to investigate the functional properties of human GM-CSF receptor (GMR), cDNA encoding human GMRα and βc subunits was transfected into BaF3, a mouse pre-B cell line without GMR expression. The results of positive transfectant assay showed that BaF3 clone expressing GMRα could bind to the ligand with low affinity (Kd = 3.4nmol / L) and proliferate only after induction with high concentration of ligand. However, co-expression of GM- Rα / β BaF3 clones bind to the ligand in a high affinity manner (Kd = 99 pmol / L) and exhibit ligand-dependent cell proliferation; the signaling and signaling of proliferative signals activate cytoplasm by inducing βc phosphorylation Jak2, Shc and Shc-related protein P145 (SHIP). Suggesting that these signaling molecules may play key roles in “Kinase Falls”, which link hematopoietic growth factor receptors to cell mitosis and other responses.