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Fig. 3 | Journal of Experimental & Clinical Cancer Research

Fig. 3

From: Focal adhesion kinase (FAK) activation by estrogens involves GPER in triple-negative breast cancer cells

Fig. 3

Transduction signaling mediating FAK Y397 phosphorylation. Immunoblots showing FAK phosphorylation in MDA-MB 231 cells treated for 30 min with 100 nM E2 (a) and 100 nM G1 (b) alone or in combination with 1 μM FAK kinase inhibitor VS-4718. Side panels show densitometric analysis of the immunoblots normalized to the loading control. Immunoblots showing ERK1/2 and AKT phosphorylation in MDA-MB 231 cells treated for 30 min with 100 nM E2 (c) and 100 nM G1 (d) alone or in combination with 1 μM FAK kinase inhibitor VS-4718. Side panels show densitometric analysis of the immunoblots normalized to the loading control. Immunoblots showing FAK phosphorylation in MDA-MB 231 cells treated for 30 min with 100 nM E2 (e) and 100 nM G1 (f) alone or in combination with 1 μM c-Src inhibitor PP2. Side panels show densitometric analysis of the immunoblots normalized to the loading control. Immunoblots showing FAK phosphorylation in MDA-MB 231 cells treated for 30 min with 100 nM E2 (g) and 100 nM G1 (h) alone or in combination with 10 μM MEK inhibitor PD98059 (PD). Side panels show densitometric analysis of the immunoblots normalized to the loading control. Immunoblots showing FAK phosphorylation in MDA-MB 231 cells treated for 30 min with 100 nM E2 (i) and 100 nM G1 (j) alone or in combination with 10 μM PI3K inhibitor Wortmannin. Side panels show densitometric analysis of the immunoblots normalized to the loading control. FAK, ERK-2 and AKT expression were used as loading controls for pFAK, pERK and pAKT, respectively. Results shown are representative of at least three independent experiments. (*) indicates p < 0.05

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