Identity of human epidermal growth factor (EGF) receptor with glycoprotein SA-7: evidence for differential phosphorylation of the two components of the EGF receptor from A431 cells.
Identity of human epidermal growth factor (EGF) receptor with glycoprotein SA-7: evidence for differential phosphorylation of the two components of the EGF receptor from A431 cells.
复制标题
人表皮生长因子 (EGF) 受体与糖蛋白 SA-7 的同一性:A431 细胞 EGF 受体两种成分差异磷酸化的证据。
DOI:
10.1073/pnas.79.16.5026
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发表时间:
1982
影响因子:
11.1
通讯作者:
Knowles,BB
中科院分区:
文献类型:
--
作者:
Carlin,CR;Knowles,BB
A 165-kilodalton (kDal) surface glycoprotein encoded by human chromosome 7 (SA-7) had been characterized by using antisera raised against human chromosome 7-containing somatic cell hybrids. We now present evidence that SA-7 is the human receptor for epidermal growth factor (EGF) and that these antisera recognize human-specific determinants. The gene coding for the human EGF receptor is localized to the p12 to p22 region of chromosome 7. We have characterized the 145-kDal/165-kDal EGF receptor doublet of A431 cells after immunoprecipitation of radiolabeled cell extracts with these antisera. We find that a protein with endogenous kinase activity copurifies with the A431 receptor doublet and that both components of the doublet contain phosphotyrosine and phosphothreonine and the 165-kDal component contains phosphoserine as well. Further, although each component of the receptor doublet has an average pI of 7, both display charge heterogeneity and appear to have unique charge isomers. The relationship between the two components of the A431 EGF receptor is discussed.