We found a marked (50%) inhibition in MMP-2 gelatinolytic activity in human breast cancer MDA-MB-435 cells pretreated with as little as 50 ng/ml of halofuginone, a concentration that markedly inhibited their invasive and proliferative capacities.
Finally, RT-quantitative PCR analysis of human breast cancer specimens showed a significant correlation between S100A14 mRNA expression and MMP2 mRNA expression in cases with wild-type p53 but not in cases with mutant p53.
This collagen-embedded spheroid system therefore offers a valuable screening model for TGF-β/Smad- and MMP2- and MMP9-dependent breast cancer invasion.
Our recent work has shown that breast cancer cell adhesion to vascular endothelial cells activates endothelial MMP-2, promoting tumor cell transendothelial migration (TEM(E)).
We studied the effect of EGCG on matrixmetalloproteinases-2 (MMP-2), the factors involved in activation, secretion and signaling molecules that might be involved in the regulation of MMP-2 in human breast cancer cell line, MCF-7.
The data suggest that MMP-2 -1306C>T polymorphism strongly contributes to the development of BC in the population studied, especially among women 50 years old and younger.
Matrix metalloproteinase-2 (MMP-2) is a key enzyme in the degradation of extracellular matrices and its expression has been dysregulated in breast cancer invasion and metastasis.
Therefore, in this study, we examined the effects of [6]-gingerol on adhesion, invasion, motility, activity and the amount of MMP-2 or -9 in the MDA-MB-231 human breast cancer cell line.
Analysis of ALCAM expression in relation to other molecular biomarkers revealed that ALCAM expression and the ALCAM/MMP-2 ratio are more promising indicators of breast cancer progression than MMP-2, E-cadherin, and alpha-catenin.
We found that PMVs 1) transferred PLT-derived integrin CD41 to the surface of breast cancer cells and enhanced their adhesion to endothelial cells; 2) increased CXCR4 expression and chemotaxis toward a stromal-derived factor-1 gradient in invasive MDA-231 and BT-549 cells; 3) increased phosphorylation of the mitogen-activated protein kinase p42/44 and AKT signaling pathways; 4) stimulated the production of MMPs in invasive MDA-231 and BT-549 cells and their chemoinvasion across the reconstituted basement membrane Matrigel; and 5) induced the secretion of MMP-9 by marrow fibroblasts and stimulated the secretion of both MMP-2 and MMP-9 in cocultures of fibroblasts with MDA-MB-231 cells.
In the present study, we show by gelatin zymography that, when exposed to ethanol, MCF-7 human breast cancer cells display a higher amount of active metalloproteinases (MMP) 2 and 9 in their culture medium.
Our results also suggest major roles of the MMP2, NRG1 and CGB genes (which encode type I gelatinase, heregulin and human chorionic gonadotropin beta subunit, respectively) in the PEA3 pathway dysregulation observed in breast cancer.
These findings suggest that the presence of the variant allele in the promoter of MMP2 or TIMP2 may be a protective factor for the development of breast cancer.
The correlation of MMPs-2 and -3 expression in peritumoural stromal cells with tumour type, shown for the first time, suggests that transcriptional regulation of these MMPs in stromal cells is important for the growth pattern of breast cancer.
We previously reported the induction of both mitogenesis and prostaglandin E2 (PGE2) production and the increased activities of matrix metalloproteinases (MMPs) MMP-2 and MMP-9 in normal human mammary epithelial cells and breast cancer cell lines, treated with HA.
We have analyzed Gelatinase A (MMP-2) and Gelatinase B (MMP-9) gene expression in a panel of six breast cancer cell lines and six primary cultures of stromal cells deriving from breast cancer biopsies.