Growth factor-independent proliferation of rat mammary carcinoma cells by autocrine secretion of neu-differentiation factor/heregulin and transforming growth factor-alpha

Mol Carcinog. 1996 Feb;15(2):134-43. doi: 10.1002/(SICI)1098-2744(199602)15:2<134::AID-MC6>3.0.CO;2-J.

Abstract

Serially transplantable rat mammary tumor (RMT) cells are not dependent on exogenous epidermal growth factor (EGF) and insulin-like growth factor-I for continuous growth in serum-free medium. Previously, we found that conditioned medium obtained from these cells contained EGF-like mitogenic activity and stimulated tyrosine phosphorylation of a 185-kDa protein in EGF-dependent mammary epithelial cells. This protein is distinct from the EGF receptor and resembles a 185-kDa tyrosine-phosphorylated protein present in RMT cells themselves. The results of the studies reported here indicate that the tyrosine-phosphorylated p185 detected in growth factor-independent RMT cells and in human mammary epithelial cells exposed to RMT-conditioned medium was activated erbB-2 protein. Partial purification of the activating factor present in RMT-conditioned medium yielded a heparin-binding growth factor with biochemical properties similar to those of neu differentiation factor/heregulin (NDF/HRG). RNA-polymerase chain reaction analysis demonstrated that RMT cells expressed mRNA for NDF/HRG, and western-blot analysis confirmed the presence of the 45-kDa secreted form of NDF/HRG in conditioned medium from the growth factor-independent RMT cells. The biological activity of partially purified rat NDF/HRG was examined and found to be the same as that of the pure growth factor. In addition, we found that RMT-conditioned medium, fractionated on an anion-exchange column and by reverse-phase high-pressure liquid chromatography, contained a potent EGF-like growth factor that was distinct from NDF/HRG. This factor competes with 125I-EGF for binding to EGF receptors and has an apparent molecular mass of 6600 Da. This factor copurifies by high-pressure liquid chromatography with pure transforming growth factor-alpha (TGF-alpha), and the cells are positive for TGF-alpha mRNA. Thus, growth factor-independent RMT cells also synthesize and secrete TGF-alpha. These results indicate that growth factor-independent cells secrete two growth factors with overlapping biological activities and suggest that autocrine loops mediated by these factors are important in the growth factor-independent proliferation of the RMT cells.

Publication types

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

MeSH terms

  • Animals
  • Base Sequence
  • Blotting, Western
  • Breast
  • Cell Division / drug effects
  • Cell Line
  • Chromatography, Affinity
  • Chromatography, High Pressure Liquid
  • Chromatography, Ion Exchange
  • Culture Media, Conditioned
  • DNA Primers
  • Epidermal Growth Factor / biosynthesis
  • Epidermal Growth Factor / pharmacology*
  • Female
  • Glycoproteins / biosynthesis*
  • Glycoproteins / isolation & purification
  • Growth Substances / pharmacology*
  • Humans
  • Mammary Neoplasms, Experimental / pathology*
  • Molecular Sequence Data
  • Neuregulins
  • Phosphorylation
  • Phosphotyrosine / analysis
  • Polymerase Chain Reaction
  • Rats
  • Receptor, ErbB-2 / biosynthesis
  • Transforming Growth Factor alpha / biosynthesis
  • Tumor Cells, Cultured

Substances

  • Culture Media, Conditioned
  • DNA Primers
  • Glycoproteins
  • Growth Substances
  • Neuregulins
  • Transforming Growth Factor alpha
  • Phosphotyrosine
  • Epidermal Growth Factor
  • Receptor, ErbB-2