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.

Abstract

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

Substances

  • 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