Increased expression of matrix metalloproteinase-2 in oral cells after short-term stimulation and long-term usage of areca quid

J Formos Med Assoc. 2005 Jun;104(6):390-7.

Abstract

Background and purpose: Arecoline, an areca quid (AQ) component, has been shown to inhibit the secretion and activity of matrix metalloproteinase-2 (MMP-2) in fibroblast cultures. This study assessed whether MMP-2 expression was inhibited in the saliva samples and tumor specimens of oral tumor patients with a long-term history of AQ consumption. The net effect of crude AQ extract (AQE) on MMP-2 expression by oral cells was also investigated.

Methods: Western blot analysis, zymography, and reverse transcriptase-polymerase chain reaction were used to detect MMP-2 protein and mRNA in saliva and tumor samples, as well as in the conditioned media (CM) of oral cell cultures.

Results: The level of MMP-2 protein was significantly higher in the saliva samples of 12 oral tumor patients who had a minimum 10-year AQ-consuming history than in those of 12 non-AQ-using healthy controls (p < 0.05). MMP-2 mRNA was expressed in 26 of 28 oral squamous cell carcinoma (OSCC) specimens. MMP-2 protein was also detectable in the tested OSCC homogenates. Short-term stimulation with 10% AQE increased the secretion of MMP-2 protein in the CM of oral epidermoid carcinoma cell Meng-1 (an OSCC cell line) and oral fibroblasts.

Conclusions: MMP-2 expression is elevated rather than inhibited in most oral tumor patients with long-term AQ usage. Short-term AQE stimulation also increases the secretion of MMP-2 by oral epithelial cells and fibroblasts. Our results suggest that AQ consumption may promote oral tumor progression through the induction of MMP-2 secretion.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Areca*
  • Carcinoma, Squamous Cell / enzymology*
  • Carcinoma, Squamous Cell / etiology
  • Gene Expression
  • Humans
  • Matrix Metalloproteinase 2 / analysis
  • Matrix Metalloproteinase 2 / biosynthesis
  • Matrix Metalloproteinase 2 / genetics*
  • Mouth Neoplasms / enzymology*
  • Mouth Neoplasms / etiology
  • Reverse Transcriptase Polymerase Chain Reaction
  • Saliva / enzymology*

Substances

  • Matrix Metalloproteinase 2