Possible mechanism of betel-quid-extract-induced expression of matrix metalloproteinase-2

Yu Chi Liu, Mei Huei Lin, Shyun Yeu Liu, Wei Fan Chiang, Li Lin Chen, Tai Chi Chen, Yon Chi Cheng, Kai Chen Hsu, Pse Chou Cheng, Chin Hai Lee, Young Chau Liu

Research output: Contribution to journalArticlepeer-review

4 Citations (Scopus)


Background/Purpose: Betel quid extract (BQE) has been demonstrated to induce matrix metalloproteinase (MMP)-2 expression. This study aimed to establish the possible mechanism involved in this event. Methods: Western blotting, reverse-transcription polymerase chain reaction, and gelatin zymography were used to study the expression level of MMP-2. LY294002, PD98059, U0126, N-acetyl-L-cysteine, SB203580, SP600125, and Bay 11-7082 were used to pretreat OECM-1 cells before BQE treatment and MMP-2 detection. Results: OECM-1 cells were subjected to short-term (10 minutes) or long-term (24 hours) BQE treatment (designated as SBT and LBT, respectively), and we found that both treatments increased MMP-2 protein and extracellular signal-regulated kinase (ERK) phosphorylation levels in a concentration- and time-dependent manner. LBT also increased MMP-2 mRNA level. LBT-induced MMP-2 secretion was not inhibited by PD98059 (up to 50 μM) when ERK was effectively blocked, but was attenuated by LY294002 (0-10 μM) in a concentrationdependent manner. This LBT effect was inhibited strongly by SB203580 (10 μM), SP600125 (10 μM), and Bay 11-7082 (10 μM) and mildly by N-acetyl-L-cysteine (5 mM), but not by U0126 (10 μM). Conclusion: Both SBT and LBT upregulate MMP-2 expression, and LBT-induced MMP-2 expression might be mediated by phosphoinositide 3-kinase, p38 mitogen-activated protein kinase, c-Jun N-terminal kinase, and nuclear factor-κB, and to a lesser extent, by reactive oxygen species, rather than by ERK.

Original languageEnglish
Pages (from-to)838-847
Number of pages10
JournalJournal of the Formosan Medical Association
Issue number11
Publication statusPublished - Nov 2010


  • Betel quid
  • Matrix metalloproteinase-2

ASJC Scopus subject areas

  • Medicine(all)


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