Basic and acidic fibroblast growth factors modulate the epidermal growth factor receptor by a protein kinase C-independent pathway

Biochem Biophys Res Commun. 1989 Oct 31;164(2):796-803. doi: 10.1016/0006-291x(89)91529-5.


Human acidic and basic fibroblast growth factors (aFGF and bFGF) inhibit epidermal growth factor (EGF) receptor binding in mouse Swiss 3T3 cells. Scatchard analysis indicates that aFGF and bFGF cause a decrease in the high affinity EGF receptor population, similar to that observed for activators of protein kinase C such as phorbol esters, platelet-derived growth factor (PDGF) and bombesin. However, unlike phorbol esters, aFGF and bFGF inhibit EGF binding in protein kinase C-deficient cells. The time course and dose response of inhibition of EGF binding by both aFGF and bFGF are very similar, with an ID50 of approximately 0.10 ng/ml. In contrast to bombesin but like PDGF, neither aFGF nor bFGF act on the EGF receptor through a pertussis toxin-sensitive G protein. These results indicate that both acidic and basic FGF depress high affinity EGF binding in Swiss 3T3 cells with similar potency through a protein kinase C/Gi-independent pathway.

Publication types

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

MeSH terms

  • Animals
  • Bombesin / pharmacology
  • Cattle
  • Cells, Cultured
  • Epidermal Growth Factor / metabolism
  • ErbB Receptors / drug effects
  • ErbB Receptors / metabolism*
  • Fibroblast Growth Factors / pharmacology*
  • Humans
  • Kinetics
  • Mice
  • Pertussis Toxin
  • Phorbol 12,13-Dibutyrate / pharmacology
  • Platelet-Derived Growth Factor / pharmacology
  • Protein Kinase C / metabolism*
  • Virulence Factors, Bordetella / pharmacology


  • Platelet-Derived Growth Factor
  • Virulence Factors, Bordetella
  • Phorbol 12,13-Dibutyrate
  • Fibroblast Growth Factors
  • Epidermal Growth Factor
  • Pertussis Toxin
  • ErbB Receptors
  • Protein Kinase C
  • Bombesin