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Protein tyrosine phosphatase controls breast cancer invasion through the expression of matrix metalloproteinase-9

Author(s): Bo-Mi Hwang | Hee Suk Chae | Young-Ju Jeong | Young-Rae Lee | Eun-Mi Noh | Hyun Zo Youn | Sung Hoo Jung | Hong-Nu Yu | Eun Yong Chung | Jong-Suk Kim

Journal: BMB Reports
ISSN 1976-6696

Volume: 46;
Issue: 11;
Start page: 533;
Date: 2013;
Original page

Keywords: MCF-7 | Metastasis | MMP | NF-κB | PTP

The expression of matrix metalloproteinases (MMPs) produced bycancer cells has been associated with the high potential ofmetastasis in several human carcinomas, including breast cancer.Several pieces of evidence demonstrate that protein tyrosinephosphatases (PTP) have functions that promote cell migrationand metastasis in breast cancer. We analyzed whether PTPinhibitor might control breast cancer invasion through MMPexpression. Herein, we investigate the effect of 4-hydroxy-3,3-dimethyl-2H benzo[g]indole-2,5(3H)-dione (BVT948), anovel PTP inhibitor, on 12-O-tetradecanoyl phorbol-13-acetate(TPA)-induced MMP-9 expression and cell invasion in MCF-7cells. The expression of MMP-9 and cell invasion increased afterTPA treatment, whereas TPA-induced MMP-9 expression and cellinvasion were decreased by BVT948 pretreatment. Also, BVT948suppressed NF-κB activation in TPA-treated MCF-7 cells.However, BVT948 didn’t block TPA-induced AP-1 activation inMCF-7 cells. Our results suggest that the PTP inhibitor blocksbreast cancer invasion via suppression of the expression ofMMP-9. [BMB Reports 2013; 46(11): 533-538]

Tango Jona
Tangokurs Rapperswil-Jona

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