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. Author manuscript; available in PMC: 2008 Jan 26.
Published in final edited form as: Cell. 2007 Jan 26;128(2):341–355. doi: 10.1016/j.cell.2006.11.048

Figure 6.

Figure 6

Role of GC-A in PDGF-induced cell migration. A, Western blot with anti-GC-A antibody showing the reduction of GC-A protein levels in GC-A siRNA cells compared to cells treated with a control siRNA. Bottom panels: Western blots with anti-tubulin, anti-Rac1, or anti-PAK1 antibodies show no changes in control and GC-A siRNA cells. B, ANP-induced accumulation of cellular cGMP was reduced in GC-A siRNA cells compared to cells transfected with a control siRNA. C, GC-A siRNA treatment reduced the cGMP levels induced by PDGF, compared to cells treated with a control siRNA. D, GC-A siRNA treatment, expression of dominant-negative Rac1(T17N) or PAK1-(83–149) reduced the cell migration induced by PDGF in a wound healing assay. E, GC-A siRNA treatment and expression of dominant-negative Rac1 or PAK1 mutant proteins reduced the cell migration induced by PDGF in a Boyden chamber assay. F, Re-expression of human GC-A in MEF cells treated with mouse GC-A siRNA rescued the cell migration induced by PDGF. G, GC-A siRNA treatment and expression of dominant-negative PAK1 mutant proteins reduced Rac1(G12V) induced cell migration. H, Expression of constitutively active Rac1(G12V) or PAK1-(165–544) increased the endogenous cGMP levels in MEF cells and HeLa cells. I, Time-lapse recordings of MEF cells treated with a control siRNA or GC-A siRNA. The position of cells at 0 min (before PDGF addition) was marked as red. The position of cells at ~3 hours was marked as green. Data are representative of three to four similar experiments. **, P < 0.001; *, P < 0.005; ++, P < 0.01 (Student’s t-test).