Erikson E, Shealy D J, Erikson R L
J Biol Chem. 1981 Nov 25;256(22):11381-4.
Treatment of A-431 human epidermoid carcinoma cells with epidermal growth factor (EGF) was shown to enhance the phosphorylation of a Mr = 34,000 protein. Because the phosphorylation of an analogous protein is enhanced in various cell lines transformed by Rous sarcoma virus (RSV) (Erikson, E., and Erikson, R. L. (1980) Cell 21, 829-836), we characterized the phosphorylation of the A-431 Mr = 34,000 protein under these two conditions in order to determine whether there are common pathways between viral transformation and EGF stimulation. The results of tryptic phosphopeptide mapping and phosphoamino acid analysis showed that the Mr = 34,000 protein was phosphorylated in an identical manner by the EGF-stimulated protein kinase activity and by the protein kinase activity of the RSV transformation-specific protein or of its normal cell homolog. Although the specific protein kinase that phosphorylates the Mr = 34,000 protein under conditions of EGF-stimulation is not yet identified, these studies demonstrate that at least one consequence of EGF stimulation is identical with one of the consequences of viral transformation.
用表皮生长因子(EGF)处理A - 431人表皮样癌细胞,结果显示可增强一种分子量为34,000的蛋白质的磷酸化作用。由于在劳斯肉瘤病毒(RSV)转化的各种细胞系中,类似蛋白质的磷酸化作用增强(埃里克森,E.,和埃里克森,R. L.(1980年)《细胞》21卷,829 - 836页),我们对在这两种条件下A - 431细胞中分子量为34,000的蛋白质的磷酸化作用进行了表征,以确定病毒转化和EGF刺激之间是否存在共同途径。胰蛋白酶磷酸肽图谱分析和磷酸氨基酸分析结果表明,分子量为34,000的蛋白质在EGF刺激的蛋白激酶活性作用下,以及在RSV转化特异性蛋白或其正常细胞同源物的蛋白激酶活性作用下,以相同方式发生磷酸化。尽管在EGF刺激条件下使分子量为34,000的蛋白质发生磷酸化的特异性蛋白激酶尚未确定,但这些研究表明,EGF刺激的至少一个结果与病毒转化的一个结果相同。