Basic fibroblast growth factor confers growth inhibition and mitogen-activated protein kinase activation in human breast cancer cells

Eyal Fenig, Robert Wieder, Shoshana Paglin, Huisheng Wang, Roger Persaud, Adriana Haimovitz-Friedman, Zvi Fuks, Joachim Yahalom*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

58 Scopus citations

Abstract

The effect of basic fibroblast growth factor (bFGF) on human breast cancer cells was studied in vitro. Exposure to bFGF resulted in significant growth inhibition, decreased DNA synthesis, and accumulation of cells in G0-G1. The IC50 for growth inhibition in MCF-7 cells was 50 pg/ml, and it was abrogated by neutralizing antibodies against bFGF. Inhibition of growth by bFGF was predominant over the growth stimulatory effects of 17β-estradiol, insulin, or epidermal growth factor. Binding and cross-linking studies of 125I-labeled bFGF in intact MCF-7 cells demonstrated 5.2 x 103 saturable bFGF binding sites per cell, a dissociation constant of 57 pM, and a M(r) 142,000 125I-labeled bFGF cross-linked protein. Stimulation of MCF-7 cells with bFGF at concentrations which effected growth inhibition also resulted in activation of p42(mapk) (ERK2) and p44(mapk) (ERK1) mitogen-activated protein kinases. These data demonstrate that whereas bFGF inhibits the growth of several breast cancer cell lines, it concomitantly activates ERK1 and ERK2, generally considered to signal mitogenic rather than growth inhibitory responses. Whether there is association between these phenomena remains unknown.

Original languageEnglish
Pages (from-to)135-142
Number of pages8
JournalClinical Cancer Research
Volume3
Issue number1
StatePublished - 1997
Externally publishedYes

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