Expression of epidermal-growth-factor receptor in the K562 cell line by transfection. Altered receptor biochemistry

H. Allen, J. Hsuan, S. Clark, R. Maziarz, M. D. Waterfield, R. A. Flavell, J. Haley

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6 Scopus citations


The epidermal-growth-factor (EGF) receptor was expressed in the human erythroleukaemic cell line K562 by transfection of the receptor cDNA. EGF-receptor biochemistry appears altered in the K562 transfectants. Autophosphorylation of the K562 receptor is not stimulated substantially by EGF. Tyrosine kinase activity of the receptor is high in the absence of EGF, whereas receptor affinity for EGF is low. K562 cells are shown to lack mRNA for transforming growth factor α (TGF(α)). Therefore autocrine stimulation of the K562 receptor, at least by TGF(α), does not explain the observed receptor biochemistry. The K562 receptor is phosphorylated at a single major site in intact cells, a threonine residue that may be Thr-669. Possible mechanisms of regulation of the EGF receptor in the K562 transfectants are discussed.

Original languageEnglish (US)
Pages (from-to)785-790
Number of pages6
JournalBiochemical Journal
Issue number3
StatePublished - Jan 1 1990


ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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