BMC Cancer
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Research articleSuppression of local invasion of ameloblastoma by inhibition of matrix metalloproteinase-2 in vitroAnxun Wang1* , Bin Zhang2* , Hongzhang Huang3 , Leitao Zhang2 , Donglin Zeng3 , Qian Tao3 , Jianguang Wang2 and Chaobin Pan2  1
Department of Oral and Maxillofacial Surgery, The First Affiliated Hospital, Sun Yat-sen University, Guangzhou, Guangdong, 510080, PR China 2
Department of Oral and Maxillofacial Surgery, The Second Affiliated Hospital, Sun Yat-sen University, 107 Yan-jiang Road West, Guangzhou, Guangdong, 510120, PR China 3
Department of Oral and Maxillofacial Surgery, Guanghua College of Stomatology, Sun Yat-sen University, Guangzhou, Guangdong, 510055, PR China author email corresponding author email* Contributed equally
BMC Cancer 2008,
8:182doi:10.1186/1471-2407-8-182 Abstract
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. |