Figure 3. α2β1 integrin is the receptor for HDFC and is a potent inducer of invadopodia. (A) Effect of specific integrin inhibition on invadopodia formation in MDA-MB-231 cells invading HDFC in serum-containing medium. Means ± SEM from 100–150 cells for each condition with three independent repeats. N/S, nonspecific. (B) Effect of integrin inhibition by mAbs on invadopodia formation in MDA-MB-231 cells invading HDFC in serum-free medium. Means ± SEM of 100 cells/condition with three repeats. (C) Effect of specific integrin inhibition on invadopodia formation in MDA-MB-231 cells invading 2D gelatin in the presence of serum. The values are mean number of cells with ECM-degrading invadopodia ± SEM of 100–150 cells/condition, with three independent repeats. (D) Representative images for integrin inhibitory experiments of MDA-MB-231 cells invading HDFC in the presence of serum in A. (E) Representative images for integrin inhibitory studies in C. (F) Immunostaining of fibronectin (green) bound to the gelatin matrix with or without serum in the medium. (G) Effect of fibronectin-coated gelatin matrix on invadopodia induction in c-Src–expressing MDA-MB-231 cells. Serum-starved cells were plated on the fibronectin-coated gelatin in the presence or absence of serum or with 5 nM EGF. Means ± SEM of 90–100 cells per condition with three independent experiments. (H) Percentage of MDA-MB-231 cells with invadopodia after adhesion to antibody-coated substrates targeting individual integrin subunits. Means ± SEM of ∼100 cells per condition with three experiments each, comparing antibodies at 10 µg (dark bar) or 200 µg (light bar) per 14-mm-diameter coverslip. (I) Representative micrographs of invadopodia formation by MDA-MB-231 carcinoma cells induced by adhesion to antibody-coated substrates targeting individual integrin subunits as in H. Invadopodia are yellow dots of colocalized actin and cortactin immunostaining. *, P < 0.05; **, P < 0.001; ***, P < 0.0001. Bars, 10 µm.
Figure 3.

α2β1 integrin is the receptor for HDFC and is a potent inducer of invadopodia. (A) Effect of specific integrin inhibition on invadopodia formation in MDA-MB-231 cells invading HDFC in serum-containing medium. Means ± SEM from 100–150 cells for each condition with three independent repeats. N/S, nonspecific. (B) Effect of integrin inhibition by mAbs on invadopodia formation in MDA-MB-231 cells invading HDFC in serum-free medium. Means ± SEM of 100 cells/condition with three repeats. (C) Effect of specific integrin inhibition on invadopodia formation in MDA-MB-231 cells invading 2D gelatin in the presence of serum. The values are mean number of cells with ECM-degrading invadopodia ± SEM of 100–150 cells/condition, with three independent repeats. (D) Representative images for integrin inhibitory experiments of MDA-MB-231 cells invading HDFC in the presence of serum in A. (E) Representative images for integrin inhibitory studies in C. (F) Immunostaining of fibronectin (green) bound to the gelatin matrix with or without serum in the medium. (G) Effect of fibronectin-coated gelatin matrix on invadopodia induction in c-Src–expressing MDA-MB-231 cells. Serum-starved cells were plated on the fibronectin-coated gelatin in the presence or absence of serum or with 5 nM EGF. Means ± SEM of 90–100 cells per condition with three independent experiments. (H) Percentage of MDA-MB-231 cells with invadopodia after adhesion to antibody-coated substrates targeting individual integrin subunits. Means ± SEM of ∼100 cells per condition with three experiments each, comparing antibodies at 10 µg (dark bar) or 200 µg (light bar) per 14-mm-diameter coverslip. (I) Representative micrographs of invadopodia formation by MDA-MB-231 carcinoma cells induced by adhesion to antibody-coated substrates targeting individual integrin subunits as in H. Invadopodia are yellow dots of colocalized actin and cortactin immunostaining. *, P < 0.05; **, P < 0.001; ***, P < 0.0001. Bars, 10 µm.

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