Tricetin suppresses human oral cancer cell migration by reducing matrix metalloproteinase‐9 expression through the mitogen‐activated protein kinase signaling pathway

<jats:title>Abstract</jats:title><jats:p>Tricetin is a flavonoid derivative and a potent anti‐inflammatory and anticancer agent. However, the molecular mechanism underlying the effects of tricetin on human oral cancer cell migration remains unclear. The cell migration and invasion abilities of three oral cancer cell lines (SCC‐9, HSC‐3, and OECM‐1) were analyzed using Boyden chamber migration assays. Our results demonstrated that tricetin attenuates 12‐O‐tetradecanoylphorbol‐13‐acetate‐induced SCC‐9, HSC‐3, and OECM‐1 cell invasiveness and migration by reducing matrix metalloproteinase (MMP)‐9 enzyme activity. The reverse transcription polymerase chain reaction and luciferase reporter assay revealed that tricetin downregulates the mRNA expression and promoter activity of MMP‐9. In addition, Western blot analysis revealed that tricetin significantly reduced the levels of phosphorylated c‐Jun N‐terminal kinase (JNK) 1/2 and p38 levels but not those of extracellular signal‐regulated kinase 1/2. In conclusion, this study demonstrated that tricetin suppresses MMP‐9 enzymatic activity by downregulating the p38/JNK1/2 pathway and might be a beneficial chemopreventive agent.</jats:p>