Regulation by EGF is maintained in an overexpressed chimeric EGFR/neu receptor tyrosine kinase

H. Lehvaslaiho, L. Sistonen, F. DiRenzo, J. Partanen, P. Comoglio, E. Holtta, K. Alitalo

Research output: Contribution to journalArticlepeer-review

Abstract

The effects of a ligand regulated neu tyrosine kinase were examined in NIH 3T3 cells. A chimeric construct encoding the human EGF receptor extracellular domain fused to the tyrosine kinase domain of the rat neu cDNA was expressed under the transcriptional control of the Moloney murine leukemia virus LTR promoter. This resulted in higher levels of expression of the chimeric receptor than were previously obtained from the SV40 virus early promoter in the same cells. The chimeric receptor showed strict ligand-dependent tyrosine kinase and signal transducing activities for the induction of growth-regulated biochemical activities and DNA synthesis in resting cells. The ligand-activated cells became morphologically transformed and grew in agar in the presence of EGF and TGFβ as efficiently as did the ligand-independent neu oncogene-transformed cells. Our results establish similarities between the signal pathways of the EGF receptor and the neu tyrosine kinase.

Original languageEnglish
Pages (from-to)123-133
Number of pages11
JournalJournal of Cellular Biochemistry
Volume42
Issue number3
Publication statusPublished - 1990

Keywords

  • Glucose transport
  • Ligand-dependent transformation
  • Ornithine decarboxylase
  • Signal transduction
  • TGF-beta

ASJC Scopus subject areas

  • Biochemistry
  • Cell Biology

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