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Vanillin Inhibits Matrix Metalloproteinase-9 Expression through Down-Regulation of Nuclear Factor-B Signaling Pathway in Human Hepatocellular Carcinoma Cells

Departments of Radiation Therapy and Oncology (J.-A.L.) and Nuclear Medicine (T.-Y.H.), China Medical University Hospital, Taichung, Taiwan; and Department of Biochemistry (S.-L.W.), Graduate Institute of Chinese Medical Science (H.-Y.L., T.-Y.H.), and Department of Microbiology (C.-Y.H.), China Medical University, Taichung, Taiwan

Vanillin has been reported to exhibit anti-invasive and antimetastatic activities by suppressing the enzymatic activity of matrix metalloproteinase-9 (MMP-9). However, the underlying mechanism of anti-invasive activity remains unclear so far. Herein we demonstrate that vanillin reduced 12-O-tetradecanoylphorbol-13-acetate (TPA)-induced MMP-9 gelatinolytic activity and suppressed cell invasion through the down-regulation of MMP-9 gene transcription in HepG2 cells. Vanillin significantly reduced the 6.6-fold invasive capacity of HepG2 cells in noncytotoxic concentrations, and this anti-invasive effect was concentration-dependent in the Matrigel invasion assay. Moreover, vanillin significantly suppressed the TPA-induced enzymatic activity of MMP-9 and decreased the induced mRNA level of MMP-9. Analysis of the transcriptional regulation indicated that vanillin suppressed MMP-9 transcription by inhibiting nuclear factor-B (NF-B) activity. Western blot further confirmed that vanillin inhibited NF-B activity through the inhibition of IB- phosphorylation and degradation. In conclusion, vanillin might be a potent antiinvasive agent that suppresses the MMP-9 enzymatic activity via NF-B signaling pathway.

Received for publication June 6, 2008.

Accepted for publication October 1, 2008.

Address correspondence to: Prof. Tin-Yun Ho, Molecular Biology Laboratory, Graduate Institute of Chinese Medical Science, China Medical University, 91 Hsueh-ShihRoad, Taichung 40402, Taiwan. E-mail:cyhsiang{at}mail.cmu.edu.tw

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