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Silletti, Steve; Kessler, Torsten; Goldberg, Joel; Boger, Dale L.; Cheresh, David A.
Proceedings of the National Academy of Sciences - PNAS, 01/2001, Letnik: 98, Številka: 1Journal Article
Matrix metalloproteinase 2 (MMP2) can associate with integrin αvβ3on the surface of endothelial cells, thereby promoting vascular invasion. Here, we describe an organic molecule (TSRI265) selected for its ability to bind to integrin αvβ3and block αvβ3interaction with MMP2. Although disrupting αvβ3/MMP2 complex formation, TSRI265 has no effect on αvβ3binding to its extracellular matrix ligand vitronectin and does not influence MMP2 activation or catalytic activity directly. However, TSRI265 acts as a potent antiangiogenic agent and thereby blocks tumor growth in vivo. These findings suggest that activated MMP2 does not facilitate vascular invasion during angiogenesis unless it forms a complex with αvβ3on the endothelial cell surface. By disrupting endothelial cell invasion without broadly suppressing cell adhesion or MMP function, the use of compounds such as TSRI265 may provide a novel therapeutic approach for diseases associated with uncontrolled angiogenesis.
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JCR | SNIP | JCR | SNIP | JCR | SNIP | JCR | SNIP |
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in: SICRIS
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