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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.
K Hicks, and
B Friedman, and
M R Rosner
January 1991,
Growth factors (Chur, Switzerland),
K Hicks, and
B Friedman, and
M R Rosner
February 1993,
Journal of cellular physiology,
K Hicks, and
B Friedman, and
M R Rosner
April 2004,
The Journal of biological chemistry,
K Hicks, and
B Friedman, and
M R Rosner
August 1995,
Endocrinology,
K Hicks, and
B Friedman, and
M R Rosner
November 1988,
Brain research,
K Hicks, and
B Friedman, and
M R Rosner
May 1999,
Diabetes,
K Hicks, and
B Friedman, and
M R Rosner
September 1995,
Cell growth & differentiation : the molecular biology journal of the American Association for Cancer Research,
K Hicks, and
B Friedman, and
M R Rosner
May 1996,
Carcinogenesis,
K Hicks, and
B Friedman, and
M R Rosner
July 1988,
The Journal of biological chemistry,
K Hicks, and
B Friedman, and
M R Rosner
March 1992,
Biochimica et biophysica acta,
