Deregulated matriptase causes ras-independent multistage carcinogenesis and promotes ras-mediated malignant transformation

Genes Dev. 2005 Aug 15;19(16):1934-50. doi: 10.1101/gad.1300705.

Abstract

Overexpression of the type II transmembrane serine protease matriptase is a highly consistent feature of human epithelial tumors. Here we show that matriptase possesses a strong oncogenic potential when unopposed by its endogenous inhibitor, HAI-1. Modest orthotopic overexpression of matriptase in the skin of transgenic mice caused spontaneous squamous cell carcinoma and dramatically potentiated carcinogen-induced tumor formation. Matriptase-induced malignant conversion was preceded by progressive interfollicular hyperplasia, dysplasia, follicular transdifferentiation, fibrosis, and dermal inflammation. Furthermore, matriptase induced activation of the pro-tumorigenic PI3K-Akt signaling pathway. This activation was frequently accompanied by H-ras or K-ras mutations in carcinogen-induced tumors, whereas matriptase-induced spontaneous carcinoma formation occurred independently of ras activation. Increasing epidermal HAI-1 expression completely negated the oncogenic effects of matriptase. The data implicate dysregulated matriptase expression in malignant epithelial transformation.

MeSH terms

  • 9,10-Dimethyl-1,2-benzanthracene / pharmacology
  • Animals
  • Carcinogens / pharmacology
  • Carcinoma, Squamous Cell / pathology
  • Carcinoma, Squamous Cell / secondary
  • Cell Transformation, Neoplastic / chemically induced
  • Cell Transformation, Neoplastic / genetics
  • Cell Transformation, Neoplastic / metabolism*
  • Epidermis / metabolism*
  • Humans
  • Lymph Nodes / pathology
  • Membrane Glycoproteins / genetics
  • Membrane Glycoproteins / physiology
  • Mice
  • Mice, Transgenic
  • Phosphatidylinositol 3-Kinases / metabolism
  • Protein Kinase C / metabolism
  • Proteinase Inhibitory Proteins, Secretory
  • Serine Endopeptidases / genetics
  • Serine Endopeptidases / metabolism
  • Serine Endopeptidases / physiology*
  • Serine Proteinase Inhibitors / genetics
  • Serine Proteinase Inhibitors / physiology
  • ras Proteins / physiology*

Substances

  • Carcinogens
  • Membrane Glycoproteins
  • Proteinase Inhibitory Proteins, Secretory
  • SPINT1 protein, human
  • Serine Proteinase Inhibitors
  • Spint1 protein, mouse
  • 9,10-Dimethyl-1,2-benzanthracene
  • Phosphatidylinositol 3-Kinases
  • Protein Kinase C
  • Serine Endopeptidases
  • matriptase
  • ras Proteins