Catalytically inactive human cathepsin D triggers fibroblast invasive growth

J Cell Biol. 2005 Jan 31;168(3):489-99. doi: 10.1083/jcb.200403078. Epub 2005 Jan 24.

Abstract

The aspartyl-protease cathepsin D (cath-D) is overexpressed and hypersecreted by epithelial breast cancer cells and stimulates their proliferation. As tumor epithelial-fibroblast cell interactions are important events in cancer progression, we investigated whether cath-D overexpression affects also fibroblast behavior. We demonstrate a requirement of cath-D for fibroblast invasive growth using a three-dimensional (3D) coculture assay with cancer cells secreting or not pro-cath-D. Ectopic expression of cath-D in cath-D-deficient fibroblasts stimulates 3D outgrowth that is associated with a significant increase in fibroblast proliferation, survival, motility, and invasive capacity, accompanied by activation of the ras-MAPK pathway. Interestingly, all these stimulatory effects on fibroblasts are independent of cath-D proteolytic activity. Finally, we show that pro-cath-D secreted by cancer cells is captured by fibroblasts and partially mimics effects of transfected cath-D. We conclude that cath-D is crucial for fibroblast invasive outgrowth and could act as a key paracrine communicator between cancer and stromal cells, independently of its catalytic activity.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Apoptosis / physiology
  • Butadienes / pharmacology
  • Cathepsin D / genetics
  • Cathepsin D / metabolism
  • Cathepsin D / physiology*
  • Cell Enlargement / drug effects
  • Cell Growth Processes / drug effects
  • Cell Growth Processes / physiology
  • Cell Line
  • Cell Line, Tumor
  • Cell Movement / drug effects
  • Cell Movement / physiology*
  • Cell Proliferation / drug effects
  • Cell Survival / physiology
  • Coculture Techniques
  • Culture Media, Conditioned / pharmacology
  • Endocytosis / drug effects
  • Enzyme Inhibitors / pharmacology
  • Enzyme Precursors / metabolism
  • Enzyme Precursors / physiology
  • Fibroblasts / cytology*
  • Fibroblasts / drug effects
  • Fibroblasts / ultrastructure
  • Humans
  • Mannosephosphates / pharmacology
  • Mice
  • Microscopy, Electron
  • Mitogen-Activated Protein Kinase 1 / metabolism
  • Mitogen-Activated Protein Kinase 3 / metabolism
  • Neoplasm Invasiveness
  • Neoplasms, Glandular and Epithelial / enzymology
  • Neoplasms, Glandular and Epithelial / metabolism
  • Neoplasms, Glandular and Epithelial / pathology
  • Nitriles / pharmacology
  • Paracrine Communication / physiology
  • Phosphorylation / drug effects
  • RNA, Small Interfering / genetics
  • Transfection
  • Wound Healing

Substances

  • Butadienes
  • Culture Media, Conditioned
  • Enzyme Inhibitors
  • Enzyme Precursors
  • Mannosephosphates
  • Nitriles
  • RNA, Small Interfering
  • U 0126
  • mannose-6-phosphate
  • Mitogen-Activated Protein Kinase 1
  • Mitogen-Activated Protein Kinase 3
  • procathepsin D
  • Cathepsin D