BMC Cancer · 2008 · 39 citations · 23 references
MedicineCell BiologyOncologyMolecular OncologyNeoplasiaTumor ProgressionAmeloblast BiologyTumor InvasionMatrix Metalloproteinase InhibitorsMatrix MetalloproteinasesProtein Expression Levels
BACKGROUND: Ameloblastomas are odontogenic neoplasms characterized by local invasiveness. This study was conducted to address the role of matrix metalloproteinase-2 (MMP-2) in the invasiveness of ameloblastomas. METHODS: Plasmids containing either MMP-2 siRNA or tissue inhibitor of metalloproteinase-2 (TIMP-2) cDNA were created and subsequently transfected into primary ameloblastoma cells. Zymography, RT-PCR, and Western blots were used to assess MMP-2 activity and expression of MMP-2 and TIMP-2, as well as protein levels. RESULTS: Primary cultures of ameloblastoma cells expressed cytokeratin (CK) 14 and 16, and MMP-2, but only weakly expressed CK18 and vimentin. MMP-2 mRNA and protein levels were significantly inhibited by RNA interference (P < 0.05). Both MMP-2 siRNA and TIMP-2 overexpression inhibited MMP-2 activity and the in vitro invasiveness of ameloblastoma. CONCLUSION: These results indicate that inhibition of MMP-2 activity suppresses the local invasiveness of ameloblastoma cells. This mechanism may serve as a novel therapeutic target in ameloblastomas pursuant to additional research.
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Activation mechanisms of matrix metalloproteinases.
Hideaki Nagase · PubMed · 1997 · 1.1K citations
Analysis of gene function in somatic mammalian cells using small interfering RNAs
Sayda M. Elbashir · Methods · 2002 · 1.1K citations · Full text
Metalloproteinases and cancer invasion.
Lance A. Liotta, William G. Stetler‐Stevenson · PubMed · 1990 · 397 citations
Medicine, Cancer Biology, Oncology +12