Modulation of the epidermal growth factor receptor by basic fibroblast growth factor

J Cell Physiol. 1993 Feb;154(2):350-8. doi: 10.1002/jcp.1041540219.


Treatment of Swiss 3T3 fibroblasts with basic fibroblast growth factor (bFGF) lead to a rapid reduction in epidermal growth factor (EGF) binding and a slower inhibition of EGF receptor autophosphorylation. The reduction in binding was due to a complete loss of the highest affinity EGF binding sites and a reduction in the lower affinity binding sites. Neither the inhibition of EGF binding nor the inhibition of EGF receptor autophosphorylation required protein kinase C. Treatment of cells with bFGF stimulated the phosphorylation of the EGF receptor, which persisted for several hours. The inhibition of EGF receptor autophosphorylation by bFGF was reduced in the presence of cycloheximide. However, cycloheximide had no effect on the reduction of EGF binding by bFGF. In contrast to these results with Swiss 3T3 fibroblasts, treatment of PC12 cells with bFGF lead to a reduction in EGF binding but no inhibition of EGF receptor autophosphorylation. Thus inhibition of EGF receptor autophosphorylation and inhibition of EGF binding can be uncoupled.

Publication types

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

MeSH terms

  • 3T3 Cells
  • Animals
  • Down-Regulation
  • Epidermal Growth Factor / antagonists & inhibitors
  • Epidermal Growth Factor / metabolism
  • ErbB Receptors / metabolism*
  • Fibroblast Growth Factor 2 / metabolism*
  • Immunoblotting
  • Kinetics
  • Mice
  • PC12 Cells
  • Phosphorylation
  • Precipitin Tests
  • Protein Kinase C / metabolism


  • Fibroblast Growth Factor 2
  • Epidermal Growth Factor
  • ErbB Receptors
  • Protein Kinase C