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Matrix metalloproteinase 2 (MMP2) can associate with integrin αv β3 on the surface of endothelial cells, thereby promoting vascular invasion. Here, we describe an organic molecule (TSRI265) selected for its ability to bind to integrin αv β3 and block αv β3 interaction with MMP2. Although disrupting αv β3 /MMP2 complex formation, TSRI265 has no effect on αv β3 binding 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 growthin vivo . These findings suggest that activated MMP2 does not facilitate vascular invasion during angiogenesis unless it forms a complex with αv β3 on 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.

proceedings of the national academy of sciences of the united states of america

Disruption of matrix metalloproteinase 2 binding to integrin α v β 3 by an organic molecule inhibits angiogenesis and tumor growth in vivo