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J. Biol. Chem., Vol. 261, Issue 27, 12490-12497, 09, 1986
E Livneh, R Prywes, O Kashles, N Reiss, I Sasson, Y Mory, A Ullrich and J Schlessinger
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: it exhibits typical high affinity (10%; Kd = 3 X
10(-10) M) and low affinity (90%; Kd = 3 X 10(-9) M) binding sites for
125I-EGF; 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; 125I-EGF is rapidly internalized into the CHO cells by
receptor mediated endocytosis and; 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.
Reconstitution of human epidermal growth factor receptors and its deletion mutants in cultured hamster cells
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