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. 2008 Apr 15;29(7):1319–1326. doi: 10.1093/carcin/bgn091

Fig. 4.

Fig. 4.

GPC3 enhances the IGF-II-triggered IGF-1R phosphorylation. (A) IGF-1R phosphorylation in GPC3-expressing NIH3T3 stable lines. Cells were serum starved and 600 μg of cell extracts were immunoprecipitated with anti-IGF-1Rβ, followed by western blot with PY20. IGF-1R was phosphorylated. Twenty micrograms of total cell extracts were analyzed with anti-tubulin as an equal loading control. (B) IGF-1R phosphorylation in HuH-7 cells. Cells were transfected with control or gpc3 shRNA and serum starved. Whole-cell extracts were then subjected to immunoblot with anti-phospho-IGF-1R and then reblotted with anti-IGF-1Rβ. Phosphorylated IGF-IR was decreased by gpc3 shRNA in HuH-7 cells. (C) IGF-II-triggered IGF-1R phosphorylation in HEK293 cells. Either wild-type GPC3 (WT-GPC3), RR → AA or P25-29A was expressed in HEK293 cells. Transiently transfected cells were serum starved and then treated with IGF-II (20 ng/ml) for 5, 15, 30 or 60 min at 37°C, followed by western blot probed with anti-phospho-IGF-1Rβ and reprobed with anti-IGF-1R. GPC3 expression was shown in parallel.