STAT6 mediates interleukin-4 growth inhibition in human breast cancer cells

Neoplasia. 2002 Jul-Aug;4(4):324-31. doi: 10.1038/sj.neo.7900248.

Abstract

In addition to acting as a hematopoietic growth factor, interleukin-4 (IL-4) inhibits growth of some transformed cells in vitro and in vivo. In this study, we show that insulin receptor substrate (IRS)-1, IRS-2, and signal transducer and activator of transcription 6 (STAT6) are phosphorylated following IL-4 treatment in MCF-7 breast cancer cells. STAT6 DNA binding is enhanced by IL-4 treatment. STAT6 activation occurs even after IRS-1 depletion, suggesting the two pathways are independent. To examine the role of STAT6 in IL-4-mediated growth inhibition and apoptosis, a full-length STAT6 cDNA was transfected into MCF-7 cells. Transient overexpression of STAT6 resulted in both cytoplasmic and nuclear expression of the protein, increased DNA binding in response to IL-4, and increased transactivation of an IL-4 responsive promoter. In STAT6-transfected cells, basal proliferation was reduced whereas apoptosis was increased. Finally, stable expression of STAT6 resulted in reduced foci formation compared to vector-transfected cells alone. These results suggest STAT6 is required for IL-4-mediated growth inhibition and induction of apoptosis in human breast cancer cells.

Publication types

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

MeSH terms

  • Adenocarcinoma / metabolism
  • Adenocarcinoma / pathology*
  • Apoptosis / drug effects
  • Apoptosis / physiology
  • Breast Neoplasms / metabolism
  • Breast Neoplasms / pathology*
  • Cell Division / drug effects
  • Cell Division / physiology
  • DNA, Complementary / genetics
  • Female
  • Growth Inhibitors / pharmacology*
  • Humans
  • Insulin Receptor Substrate Proteins
  • Interleukin-4 / pharmacology*
  • Intracellular Signaling Peptides and Proteins
  • Neoplasm Proteins / physiology*
  • Phosphoproteins / metabolism
  • Phosphorylation
  • Protein Processing, Post-Translational / drug effects
  • Recombinant Fusion Proteins / physiology
  • STAT6 Transcription Factor
  • Signal Transduction
  • Trans-Activators / genetics
  • Trans-Activators / physiology*
  • Transcriptional Activation
  • Transfection
  • Tumor Cells, Cultured / drug effects
  • Tumor Cells, Cultured / pathology

Substances

  • DNA, Complementary
  • Growth Inhibitors
  • IRS1 protein, human
  • IRS2 protein, human
  • Insulin Receptor Substrate Proteins
  • Intracellular Signaling Peptides and Proteins
  • Neoplasm Proteins
  • Phosphoproteins
  • Recombinant Fusion Proteins
  • STAT6 Transcription Factor
  • STAT6 protein, human
  • Trans-Activators
  • Interleukin-4