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Figure 6


Fig. 6. Cell adhesion to epimorphin is mediated by {alpha}v-integrins. (A) Quantification of HMEC adhesion to recombinant epimorphin in the presence of anti-integrin antibodies. Adhesion to r-Epm is inhibited by antibodies that block {alpha}v- and β1-integrins (left). In the presence of function-stimulating antibody for β1-integrin (st) most of the cells bound to epimorphin within 2 hours (right). {alpha}v; clone P3G8, {alpha}v'; clone AV1. Data are the mean ± s.d., n=6, *P<0.05 vs r-Epm only. (B) Epimorphin adhesion-induced FAK phosphorylation is inhibited by antibodies against {alpha}v- and β1-integrins. (C) Immobilized epimorphin specifically binds to {alpha}v- and β1-integrins from HMECs lysates. Epimorphin beads selectively pull down 120-kDa to 140-kDa proteins (non-reduced condition) from HMEC-surface components labeled with membrane-impermeant biotinylation reagents. HRP-labeled streptavidin was used to visualize the proteins (left blot). Immunoblot of the proteins bound to r-Epm beads under the reduced condition. The cell surface proteins that bound to Epm beads appeared to include {alpha}v- and β1-integrins. FN, fibronectin (right blot). (D) Function-blocking antibodies against {alpha}v- and β1-integrins block adhesion of HSC-5 and HUVECs, whereas inhibition of {alpha}v- and {alpha}vβ5 integrins blocks adhesion of A549 and MCF7 cells. Data are the mean ± s.d., n=6, *P<0.05 vs control. (E) The transient silencing of {alpha}v-integrin results in a dramatic attenuation of epimorphin association of HMECs. The cells infected with lentivirus without (NT) or with the knockdown construct HE4 or HE5 were assessed for the expression of {alpha}v- and β1-integrins and cellular adhesion to r-Epm at day 3. Data are the mean ± s.d., n=4, *P<0.05 vs NT. (F) Epimorphin beads pull down purified {alpha}vβ5-integrin but not {alpha}1β1-integrin, and this integrin-epimorphin association is not affected by addition of RGDS or RGES peptide. {alpha}v- or {alpha}1β1-integrin bound to the beads was detected with antibodies against {alpha}v-integrin or β1-integrin, respectively.





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