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- W3193020 abstract "Accumulating evidence suggests a dual role of tissue inhibitor of metalloproteinase-2 (TIMP-2) in regulating the activity of matrix metalloproteinase-2 (MMP-2), which has long been associated with tumor angiogenesis and metastasis. By forming a complex with pro-MMP-2 and its cell surface activator MMP-14, TIMP-2 can either induce or restrain MMP-2 activation. Our recent work has shown that breast cancer cell adhesion to vascular endothelial cells activates endothelial MMP-2. The purpose of this study was to explore the underlying mechanism and its potential impact on endothelial barrier function and transendothelial migration. We found that MMP-14 was expressed in both breast cancer cells (MDA-231) and lung microvascular endothelial cells (HBMVEC-L), whereas TIMP-2 was exclusively expressed in cancer cells. Importantly, the tumor cell-derived TIMP-2 was identified as a major determinant of MMP-2 activation during tumor cell transmigration in the presence of MMP-14. This response was associated with endothelial barrier dysfunction, as evidenced by a significant decrease in transendothelial electric resistance and endothelial cell-cell junction disruption. These findings suggest a cooperative mechanism between metastatic breast cancer cells and microvascular endothelial cells in promoting MMP-2 activation and tumor cell transmigration. NIH grants HL61507, HL70753, HL73324, HL84852" @default.
- W3193020 created "2016-06-24" @default.
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- W3193020 date "2010-04-01" @default.
- W3193020 modified "2023-10-18" @default.
- W3193020 title "Tumor‐derived TIMP‐2 mediates endothelial barrier dysfunction and breast cancer cell transmigration by activating endothelial MMP‐2" @default.
- W3193020 doi "https://doi.org/10.1096/fasebj.24.1_supplement.592.2" @default.
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