Upregulated expression and activation of membrane‑associated proteases in esophageal squamous cell carcinoma

Oncol Rep. 2014 Jun;31(6):2820-6. doi: 10.3892/or.2014.3162. Epub 2014 Apr 29.

Abstract

To better understand the role of membrane-associated proteolytic systems in the development of esophageal cancer, we studied the expression of two serine proteases, fibroblast activation protein-α (FAP-α) and dipeptidyl peptidase IV (DPPIV) and three metalloproteinases, matrix metalloproteinase (MMP)-2, MMP-9 and MT1-MMP in 24 primary esophageal squamous cell carcinoma (ESCC) tissues and paired non-cancer tissues. Using reverse-transcription PCR, western blotting and zymography, we showed that both serine proteases and all three metalloproteinases were highly altered in ESCC. A positive correlation between the expression of FAP-α and DPPIV and the activity of both gelatinases was found. This may indicate that these proteolytic systems are tightly linked to each other and collectively are involved in the process of ECM degradation that facilitates cancer cell invasion and metastasis.

MeSH terms

  • Aged
  • Carcinoma, Squamous Cell / genetics*
  • Carcinoma, Squamous Cell / pathology
  • Dipeptidyl Peptidase 4 / biosynthesis*
  • Esophageal Neoplasms / genetics*
  • Esophageal Neoplasms / pathology
  • Esophageal Squamous Cell Carcinoma
  • Female
  • Gene Expression Regulation, Neoplastic
  • Humans
  • Male
  • Matrix Metalloproteinase 14 / biosynthesis
  • Matrix Metalloproteinase 2 / biosynthesis
  • Matrix Metalloproteinase 9 / biosynthesis
  • Middle Aged
  • Protein Tyrosine Phosphatase, Non-Receptor Type 13 / biosynthesis*
  • Transcriptional Activation / genetics*

Substances

  • PTPN13 protein, human
  • Protein Tyrosine Phosphatase, Non-Receptor Type 13
  • Dipeptidyl Peptidase 4
  • MMP2 protein, human
  • Matrix Metalloproteinase 2
  • Matrix Metalloproteinase 9
  • MMP14 protein, human
  • Matrix Metalloproteinase 14