Reconstitution of human epidermal growth factor receptors and the deletion mutants in cultured hamster cells

E. Livneh, R. Prywes, O. Kashles, N. Reiss, I. Sasson, Y. Mory, A. Ullrich, J. Schlessinger

Research output: Contribution to journalArticlepeer-review

127 Scopus citations


DNA sequences encoding the human epidermal growth factor (EGF) receptor and various EGF-receptor deletion mutants were transfected into Chinese hamster ovary (CHO) cells devoid of endogenous EGF receptors. A functional human EGF-receptor is expressed on the surface of heterologous CHO cells with the following properties: 1) it exhibits typical high affinity (10%; K(d) = 3 x 10-10 M) and low affinity (90%; K(d) = 3 x 10-9 M) binding sites for 125I-EGF; 2) it is expressed as a polypeptide of 170,000 molecular weight with intrinsic protein tyrosine kinase activity. EGF stimulates the kinase activity leading to self-phosphorylation and to phosphorylation of exogenous substrate; 3) 125I-EGF is rapidly internalized into the CHO cells by receptor mediated endocytosis and 4) EGF stimulates DNA synthesis in the cells expressing the human EGF-receptor. Deletion of 63 amino acids from the C-terminal end of EGF-receptor, which removes two autophosphorylation sites, abolishes the high affinity state of the receptor. Nevertheless, this receptor mutant is able to undergo endocytosis and to respond mitogenically to EGF to a similar extent as the 'wild type' receptor. Further deletions from the cytoplasmic domain give rise to low affinity endocytosis-defective receptor mutants. Finally, deletion of the transmembrane domain of the human receptor yields an EGF-receptor ligand binding domain which is secreted from the cells.

Original languageEnglish
Pages (from-to)12490-12497
Number of pages8
JournalJournal of Biological Chemistry
Issue number27
StatePublished - 1 Dec 1986
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology


Dive into the research topics of 'Reconstitution of human epidermal growth factor receptors and the deletion mutants in cultured hamster cells'. Together they form a unique fingerprint.

Cite this