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Open AccessResearch article

Suppression of local invasion of ameloblastoma by inhibition of matrix metalloproteinase-2 in vitro

Anxun Wang1* email, Bin Zhang2* email, Hongzhang Huang3 email, Leitao Zhang2 email, Donglin Zeng3 email, Qian Tao3 email, Jianguang Wang2 email and Chaobin Pan2 email

Department of Oral and Maxillofacial Surgery, The First Affiliated Hospital, Sun Yat-sen University, Guangzhou, Guangdong, 510080, PR China

Department of Oral and Maxillofacial Surgery, The Second Affiliated Hospital, Sun Yat-sen University, 107 Yan-jiang Road West, Guangzhou, Guangdong, 510120, PR China

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

Published: 30 June 2008

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.


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