Abstract
Sulfoquynovosyl acylpropanediol (SQAP) is a novel and promising anticancer agent that was obtained by structural modifications from a natural compound. SQAP has the ability to trigger antiangiogenesis in vivo with very few side effects. In this study, the mechanism by which SQAP modifies the tumor microenvironment was revealed through the application of a T7 phage display screening. We could identify five SQAP-binding proteins including among them the FAT domain of focal adhesion kinase (FAK). Two independent experiments were used to verify the interactions. SQAP decreased FAK phosphorylation and cell migration in human umbilical vein endothelial cells and A549 cancer cells. The obtained data suggest that SQAP antiangiogenic activity may be due the modulation of FAK phosphorylation. Additionally, we hypothesized that SQAP radiosensitizing activity might be at least partly due to ROS generation. Indeed, we observed that SQAP romotes ROS formation on HeLa cancer cells.
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