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

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

BMC cancer (2008-07-01)
Anxun Wang, Bin Zhang, Hongzhang Huang, Leitao Zhang, Donglin Zeng, Qian Tao, Jianguang Wang, Chaobin Pan
ABSTRACT

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. 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. 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. 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.

MATERIALS
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Brand
Product Description

Sigma-Aldrich
MMP-2 human, recombinant, expressed in E. coli, ≥98% (SDS-PAGE), ≥98% (HPLC), suitable for cell culture