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. 2011 Oct 3;21(7):1176–1186. doi: 10.1089/scd.2011.0293

FIG. 2.

FIG. 2.

BMP stimulates RhoA signaling. (A) Western blot (upper panels) and quantification plot (lower panel) showed active RhoA in serum-starved hMSCs at 3,000 cells/cm2 with BMP-2 (100 ng/mL) treatment at different time points. (B) Western blot and quantification plot showed active RhoA in serum-starved hMSCs plated at 3,000 or 20,000 cells/cm2 with or without BMP-2 (100 ng/mL) treatment. (*P<0.05 vs. paired control; #P<0.05 vs. BMP treatment at 3,000 cells/cm2). (C) Western blot and quantification plot showed levels of recombined p-mypt after in vitro ROCK kinase assay in serum-starved hMSCs plated at 3,000 or 20,000 cells/cm2 with or without BMP-2 (100 ng/mL) treatment. (*P<0.05 vs. paired control; #P<0.05 vs. BMP treatment at 3,000 cells/cm2). (D) Western blot ppMLC/MLC and quantification plot showed activation of ppMLC in serum-starved hMSCs plated at 3,000 or 20,000 cells/cm2 with or without BMP-2 (100 ng/mL) treatment (*P<0.05 vs. paired control; #P<0.05 vs. BMP treatment at 3,000 cells/cm2). All western blot results were presented as a representative experiment of at least 3 independent experiments. ppMLC, phosphorylated myosin light chain. ROCK, Rho-associated protein kinase.