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Figure 1. Sema 3C stimulates MGEC adhesion and induces ß₁ integrin phosphorylation. Adhesion of MGEC to fibronectin (A), collagen (B), and gelatin (C), at each substrate concentration of 1 µg/ml, were assessed in the absence (control) or in the presence of sema 3C (180 ng/ml) or VEGF (30 ng/ml). D) Dose response to sema 3C (180 to 480 ng/ml) showing that sema 3C regulates MGEC adhesion to fibronectin, *P < 0.05 control vs. sema 3C, **P < 0.05 sema 3C 480 vs. 180 ng/ml; E) MGEC adhesion to fibronectin (1 µg/ml) in the absence (control=gray bars) or in the presence of sema 3C (360 ng/ml; red bars) with or without antibodies blocking ₅ ß₁, _V ß₃, or both ₅ ß₁ and _V ß₃ integrins. Data are mean ± SE of 3 separate experiments, carried out in quadruplicate, *P < 0.05 control vs. ₅ ß₁ or _V ß₃ blocking antibodies, #P < 0.05 sema 3C vs. ₅ ß₁ or _V ß₃ blocking antibodies. F) Western blot showing a 2-fold increase in phosphorylated Ser-785ß₁ integrin at 30 min, reprobed with an anti-actin Ab to document equal loading. G) Western blot showing that NP1 and NP2 neutralizing antibodies prevent sema 3C-induced Ser-785ß₁ integrin phosphorylation, whereas VEGF and VEGFR2 neutralizing antibodies do not. H) Western blot showing phosphorylated Y³⁹⁷ FAK and total FAK showing that sema 3C did not alter FAK tyrosine phosphorylation. Western blots are representative of 3 separate experiments.

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