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. 2018 Aug 21;9(65):32435–32447. doi: 10.18632/oncotarget.25945

Figure 4. α2β1 integrin suppresses cell growth and promotes migration and invasion by increasing the phosphorylation of p38 MAPK.

Figure 4

(A) Representative western blot indicating that α2 integrin expression on DU145 prostate cancer cells increased phosphorylation of FAK, ERK and p38 MAPK proteins when cells were plated on collagen I coated surface. The quantification of the phosphorylated FAK/ total FAK and phosphorylated ERK/ total ERK is shown; phosphorylation of p38 MAPK is shown as % of β-actin (a loading control). Box plot shows data from 4 or 5 independent experiments (dots) and the mean from all experiments ±SEM. ** = P < 0.01. Student’s t-test. (B) p38 MAPK inhibitor SB203580 treatment (10 μg/ml) increased proliferation of DU145 cells. Proliferation of DU145KO+α2 and DU145KO+vector cells was assessed based on the change in DNA amount in 3D spheroids. Mean (n = 3) ±SEM. * = P < 0.05. Student’s t test. (C) Inhibition of p38 MAPK with SB203580 (10μg/ml) results significantly decreased migration of DU145KO+α2 cells on collagen I. Mean (n = 3) ±SEM. ** = P < 0.01, *** = P < 0.001. One way ANOVA and Tukey HSD post hoc test. (D) Invasion capability of DU145KO+α2 cells into collagen gel decreased significantly when cells were treated with p38 MAPK inhibitor SB203580 (10μg/ml). Mean (n = 3) ±SEM. *** = P < 0.001. One way ANOVA and Tukey HSD post hoc test.