DDR1 signaling is essential to sustain Stat5 function during lactogenesis

J Cell Biochem. 2006 Jan 1;97(1):109-21. doi: 10.1002/jcb.20618.

Abstract

Postnatal development of the mammary gland is achieved by an interplay of endocrine and extracellular matrix-derived signals. Despite intense research, a comprehensive understanding of the temporal and spatial coordination of these hormonal and basement membrane stimuli is still lacking. Here, we address the role of the collagen-receptor DDR1 in integrating extracellular matrix-derived signaling with the lactogenic pathway initiated by the prolactin receptor. We found that stimulation of DDR1-overexpressing mammary epithelial HC11 cells with collagen and prolactin resulted in stronger and more sustained induction of Stat5 phosphorylation as compared to control cells. Enhanced Stat5 activity in HC11-DDR1 cells correlated with increased beta-casein gene expression. In contrast, cells derived from DDR1-null mice showed reduced Stat5 activation upon lactogenic stimulation and completely failed to induce beta-casein expression. The cell-autonomous role of DDR1 in controlling ductal branching and alveologenesis prior to the onset of lactogenesis was corroborated by mammary tissue transplantation experiments. Our results show that aside from hormone- and cytokine receptors, DDR1 signaling establishes a third matrix-derived pathway vital to maintain mammary gland function.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Base Sequence
  • Blotting, Western
  • DNA Primers
  • Discoidin Domain Receptor 1
  • Electrophoretic Mobility Shift Assay
  • Immunoprecipitation
  • Lactation*
  • Mammary Glands, Animal / metabolism*
  • Membrane Proteins / metabolism*
  • Mice
  • Receptor Protein-Tyrosine Kinases / metabolism*
  • STAT5 Transcription Factor / physiology*

Substances

  • DNA Primers
  • Membrane Proteins
  • STAT5 Transcription Factor
  • Ddr1 protein, mouse
  • Discoidin Domain Receptor 1
  • Receptor Protein-Tyrosine Kinases