Weber W, Gill G N, Spiess J
Science. 1984 Apr 20;224(4646):294-7. doi: 10.1126/science.6324343.
Human epidermoid carcinoma A431 cells in culture produce a soluble 105-kilodalton protein which, by the criteria of epidermal growth factor (EGF) binding, recognition by monoclonal and polyclonal antibodies to the EGF receptor, amino-terminal sequence analysis and carbohydrate content, is related to the cell surface domain of the EGF receptor. The high rate of production and the finding that with biosynthetic labeling the specific activity of this 105-kilodalton protein exceeds that of the intact receptor indicate that it is not derived from membrane-bound mature receptor but is separately produced by the cell. These cells thus separately synthesize an EGF receptor that is inserted into the membrane and an EGF receptor-related protein that is secreted.
培养的人表皮样癌A431细胞产生一种可溶性的105千道尔顿蛋白,根据表皮生长因子(EGF)结合、针对EGF受体的单克隆和多克隆抗体识别、氨基末端序列分析以及碳水化合物含量的标准,该蛋白与EGF受体的细胞表面结构域相关。该蛋白的高产量以及通过生物合成标记发现这种105千道尔顿蛋白的比活性超过完整受体这一现象表明,它并非源自膜结合的成熟受体,而是由细胞单独产生的。因此,这些细胞分别合成一种插入膜中的EGF受体和一种分泌型的EGF受体相关蛋白。