Characterization of a novel epidermal-growth-factor-receptor-related 200-kDa tyrosine kinase in tumor cells

Eur J Biochem. 1995 Jun 15;230(3):951-7. doi: 10.1111/j.1432-1033.1995.tb20641.x.


We have detected a tyrosine-phosphorylated 200-kDa protein in two human tumor cell lines, A1235 glioma and A172 glioblastoma. The protein is an integral plasma membrane sialoglycoprotein with tyrosine kinase activity. The interesting characteristic of this protein (gp200) is that it is recognized by a number of monoclonal and polyclonal antibodies to the 170-kDa epidermal-growth-factor (EGF) receptor; however, it lacks detectable EGF-binding activity. gp200 differs from three other EGF-receptor-related proteins, erb-B-2, erb-B-3 and erb-B-4 gene products, and hence appears to be yet another member of the EGF-receptor family of proteins. This is further strengthened by the fact that both gp200 and the EGF receptor contain a common epitope which is recognized by an anti-peptide IgG to the beta-type platelet-derived-growth-factor (PDGF) receptor. Our previous studies [Bishayee, S., Majumdar, S., Scher, C.D. & Khan, S. (1988) Mol. Cell. Biol. 8, 3696-3702] have demonstrated that this epitope in the PDGF receptor is highly susceptible to the phosphorylation state of the receptor and that such a conformational change appears to be important in biological message transmission. The expression of gp200, which appears to have tyrosine kinase activity and is immunologically related to the EGF receptor in tumor cells, suggests its possible involvement in cell growth.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • ErbB Receptors / analysis*
  • ErbB Receptors / immunology
  • Glioblastoma / chemistry
  • Glioma / chemistry
  • Humans
  • Molecular Sequence Data
  • Molecular Weight
  • Neoplasm Proteins / analysis*
  • Oligosaccharides / analysis
  • Phosphorylation
  • Protein-Tyrosine Kinases / analysis*
  • Sialoglycoproteins / analysis*
  • Tumor Cells, Cultured


  • Neoplasm Proteins
  • Oligosaccharides
  • Sialoglycoproteins
  • ErbB Receptors
  • Protein-Tyrosine Kinases