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. Author manuscript; available in PMC: 2017 Nov 23.
Published in final edited form as: Cancer Res. 2016 Dec 6;77(4):982–995. doi: 10.1158/0008-5472.CAN-16-1589

Figure 7.

Figure 7

RHAMM signaling via Rho-associated protein kinase impacts the prometastatic phenotype. A, Coimmunoprecipitation of RHAMM and immunoblotting of RHAMM, F-actin, and loading control GAPDH in control and RB-deficient PC3 cells. B, Immunofluorescence confocal images of pRB and F-actin in RB-proficient and -deficient PC3 cells (left) and confocal images of RHAMM in control and RHAMM-overexpressing PC3 cells (right). C, Western blot analysis of ROCK II, p-Cofilin, cofilin, and lamin B in control, RHAMM-overexpressing, and RB-deficient PC3 cells. D, Immunoflourescence confocal images of localized F-actin, pRb, p-Cofilin, and RHAMM in control, RHAMM-overexpressing, and RB-deficient PC3 cells. E, Immunoblotting analysis of ROCK II, p-Cofilin, cofilin, and lamin B in RHAMM-overexpressing and RB-deficient PC3 cells treated with DMSO or Rho kinase inhibitor (Y27632). F, Quantitative cell migration and invasion kinetics in RB-deficient and RHAMM-overexpressing PC3 cells in response to DMSO or Y27632. G, Immunoblotting analysis of RHAMM, F-actin, and lamin B in PC3-ML–induced lung metastases treated with control or PD 0332991. H, Schematic illustration of the proposed working model. Each data point is a mean ± SD from three or more independent experiments. **, P < 0.05 was considered as statistically significant. Scale bar, 50 μm.