1. Tricetin suppresses human oral cancer cell migration by reducing matrix metalloproteinase-9 expression through the mitogen-activated protein kinase signaling pathway
- Author
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Ying-Hock Teng, Tsung-Te Chung, Ji-Ching Lai, Yi-Ting Chuang, Mu-Kuan Chen, Shun-Fa Yang, Chun-Yi Chuang, and Ming-Ju Hsieh
- Subjects
0301 basic medicine ,MAP Kinase Signaling System ,Health, Toxicology and Mutagenesis ,p38 mitogen-activated protein kinases ,Cell ,Down-Regulation ,Management, Monitoring, Policy and Law ,Biology ,Matrix metalloproteinase ,Toxicology ,p38 Mitogen-Activated Protein Kinases ,03 medical and health sciences ,chemistry.chemical_compound ,0302 clinical medicine ,Cell Movement ,Cell Line, Tumor ,medicine ,Humans ,Neoplasm Invasiveness ,Phosphorylation ,Tricetin ,Mitogen-Activated Protein Kinase 1 ,Mitogen-Activated Protein Kinase 3 ,Kinase ,JNK Mitogen-Activated Protein Kinases ,Cell migration ,General Medicine ,Antineoplastic Agents, Phytogenic ,Molecular biology ,030104 developmental biology ,medicine.anatomical_structure ,Matrix Metalloproteinase 9 ,chemistry ,Chromones ,030220 oncology & carcinogenesis ,Mitogen-activated protein kinase ,Cancer research ,biology.protein ,Mouth Neoplasms ,Signal transduction - Abstract
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.
- Published
- 2017