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We have previously shown that the angiogenic growth factor pleiotrophin (PTN) induces migration of endothelial cells through binding to its receptor protein tyrosine phosphatase β/ (RPTPβ/ ). In this study, we show that a monoclonal antibody against β 3 but not 5 β 1 integrin abolished PTN-induced human endothelial cell migration in a concentration-dependent manner. Integrin β 3 was found to directly interact with PTN in an RGD-independent manner, whereas a synthetic peptide corresponding to the specificity loop of the β 3 integrin extracellular domain ( 177 CYDMKTTC 184 ) inhibited PTN- β 3 interaction and totally abolished PTN-induced endothelial cell migration. Interestingly, β 3 was also found to directly interact with RPTPβ/ , and PTN-induced Y773 phosphorylation of β 3 integrin was dependent on both RPTPβ/ and the downstream c-src kinase activation. Midkine was found to interact with RPTPβ/ , but not with β 3 , and caused a small but statistically significant decrease in cell migration. In the same line, PTN decreased migration of different glioma cell lines that express RPTPβ/ but do not express β 3 , while it stimulated migration of U87MG cells that express β 3 on their cell membrane. Overexpression or down-regulation of β 3 stimulated or abolished, respectively, the effect of PTN on cell migration. Collectively, these data suggest that β 3 is a key molecule that determines the stimulatory or inhibitory effect of PTN on cell migration.—Mikelis, C., Sfaelou, E., Koutsioumpa, M., Kieffer, N., Papadimitriou, E. Integrin β 3 is a pleiotrophin receptor required for pleiotrophin-induced endothelial cell migration through receptor protein tyrosine phosphatase β/ .
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