Trypsin-2 enhances carcinoma invasion by processing tight junctions and activating ProMT1-MMP

Cancer Invest. 2012 Oct;30(8):583-92. doi: 10.3109/07357907.2012.716467. Epub 2012 Aug 21.

Abstract

Enhanced proteolysis and altered tight junction (TJ) proteins associate with carcinoma invasion. We hypothesized that trypsin-2, a tumor-associated serine proteinase, induces tongue carcinoma invasion by activating pro-membrane type-1 matrix metalloproteinase (MT1-MMP) and disturbing the TJs. The effects of invasion were analyzed using trypsin-2 over-expressing human tongue squamous cell carcinoma cells (Try2-HSC-3) in vitro and in vivo. The invasion of Try2-HSC-3 cells was increased in mouse xenografts and human organotypic model. Trypsin-2 activated proMT1-MMP, as well as altered the expression of TJ protein claudin-7. In conclusion, trypsin-2 over-expression enhanced tongue carcinoma cell invasion by various genetic and proteolytic mechanisms.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Carcinoma, Squamous Cell / genetics
  • Carcinoma, Squamous Cell / metabolism*
  • Carcinoma, Squamous Cell / pathology*
  • Cell Line, Tumor
  • Cell Movement / genetics
  • Claudins / genetics
  • Claudins / metabolism
  • Enzyme Activation
  • Female
  • Gene Expression
  • Gene Expression Profiling
  • Humans
  • Matrix Metalloproteinase 14 / metabolism*
  • Mice
  • Mice, Nude
  • Neoplasm Invasiveness
  • Protein Precursors / genetics
  • Protein Precursors / metabolism*
  • Tight Junctions / metabolism*
  • Tongue Neoplasms / genetics
  • Tongue Neoplasms / metabolism*
  • Tongue Neoplasms / pathology*
  • Trypsin / genetics
  • Trypsin / metabolism*
  • Trypsinogen / genetics
  • Trypsinogen / metabolism*
  • Tumor Burden / genetics
  • Xenograft Model Antitumor Assays

Substances

  • Claudins
  • Protein Precursors
  • PRSS2 protein, human
  • Trypsinogen
  • Trypsin
  • MMP14 protein, human
  • Matrix Metalloproteinase 14