PURIFIED EGF RECEPTOR-KINASE INTERACTS SPECIFICALLY WITH ANTIBODIES TO ROUS-SARCOMA VIRUS TRANSFORMING PROTEIN
PURIFIED EGF RECEPTOR-KINASE INTERACTS SPECIFICALLY WITH ANTIBODIES TO ROUS-SARCOMA VIRUS TRANSFORMING PROTEIN
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DOI：
10.1038/290516a0
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发表时间：
1981-01-01
期刊：
影响因子：
64.8
通讯作者：
COHEN, S
中科院分区：
文献类型：
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作者：
CHINKERS, M;COHEN, S
几种RNA肿瘤病毒的转化似乎是由特异性磷酸化酪氨酸的病毒编码蛋白激酶介导的。酪氨酸特异性蛋白激酶似乎也参与表皮生长因子（EGF）的促有丝分裂作用。这种表皮生长因子刺激的激酶活性与表皮生长因子受体密切相关，在表皮生长因子亲和层析过程中与表皮生长因子受体共同纯化。由于病毒和EGF刺激的酪氨酸激酶可能参与刺激细胞生长，并且病毒激酶可能与正常细胞蛋白抗原相关，因此检查了病毒酪氨酸激酶抗体与亲和纯化的EGF受体激酶制剂的相互作用。受体激酶特异性磷酸化针对劳斯肉瘤病毒的转化蛋白激酶pp60src的抗体。然而，这些抗体，包括与pp60src的正常细胞同源物（pp60sarc）交叉反应的抗体，都不能沉淀受体激酶。EGF受体激酶可能与pp60sarc相关，但可能不相同。
Transformation by several RNA tumor viruses seems to be mediated by virally-coded protein kinases which specifically phosphorylate tyrosine. A tyrosine-specific protein kinase also seems to be involved in the mitogenic action of epidermal growth factor (EGF). This EGF-stimulated kinase activity is closely associated with the EGF receptor with which it co-purifies during EGF-affinity chromatography. Because both the virus- and EGF-stimulated tyrosine kinases may be involved in stimulation of cell growth, and the viral kinases may be antigenically related to normal cell proteins, the interaction of antibodies to viral tyrosine kinases with the affinity-purified EGF receptor-kinase preparation was examined. The receptor-kinase specifically phosphorylates antibodies directed against the transforming protein kinase pp60src of Rous sarcoma virus. However, none of these antibodies, including those which cross-react with the normal cellular homolog of pp60src (pp60sarc), precipitate the receptor-kinase. The EGF receptor-kinase may be related to, but is probably not identical with, pp60sarc.