Possible Mechanism of Betel-quid-extract-induced Expression of Matrix Metalloproteinase-2

doi:10.1016/S0929-6646(10)60129-5

CNU IR > Pharmacy and Science > Dept. of Biotechnology (including master's program) > Periodical Articles > Item 310902800/25161

Please use this identifier to cite or link to this item: https://ir.cnu.edu.tw/handle/310902800/25161

Title:	Possible Mechanism of Betel-quid-extract-induced Expression of Matrix Metalloproteinase-2
Authors:	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
Contributors:	生物科技系
Keywords:	betel quid matrix metalloproteinase-2
Date:	2010-11
Issue Date:	2012-03-30 15:17:52 (UTC+8)
Abstract:	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.
Relation:	Journal of the Formosan Medical Association 109(11)：p.838-847
Appears in Collections:	[Dept. of Biotechnology (including master's program)] Periodical Articles

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