␤ig-h3 is an extracellular matrix protein that mediates adhesion and migration of several cell types through interaction with integrins. In the present study, we tested whether ␤ig-h3 mediates endothelial cell adhesion and migration, thereby regulating angiogenesis. In this study, we demonstrate that not only ␤ig-h3 itself but also all four fas-1 domains of ␤ig-h3 mediate endothelial cell adhesion and migration through interaction with the ␣ v ␤ 3 integrin. We found that the ␣ v ␤ 3

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... eracting motif of the four fas-1 domains of ␤ig-h3 is the same YH motif that we reported previously to interact with ␣ v ␤ 5 integrin. The YH peptide inhibited endothelial cell adhesion and migration in a dose-dependent manner. We demonstrate that the YH peptide has anti-angiogenic activity in vitro and in vivo using an endothelial cell tube formation assay and a Matrigel plug assay, respectively. Our results reveal that ␤ig-h3 bears ␣ v ␤ 3 integrin-interacting motifs that mediate endothelial cell adhesion and migration and, therefore, may regulate angiogenesis.