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. 2020 Jul 21;42(4):560–572. doi: 10.1038/s41401-020-0458-7

Fig. 6. Lowering [Cl−]i impairs VEGFR2 phosphorylation by enhancing PTP1B activity and VEGFR2/PTP1B association.

Fig. 6

a Western blotting analysis of VEGFR2 phosphorylation at the Tyr951, Tyr1059, Tyr1175, and Tyr1214 sites in HUVECs treated with normal Cl− and low Cl− medium followed by VEGF (50 ng/mL) stimulation for 5 min. Densitometric analysis of the phosphorylated levels of VEGFR2 at the Tyr951 (b), Tyr1059 (c), Tyr1175 (d), and Tyr1214 (e) sites. **P < 0.01 vs. normal Cl−, ##P < 0.01 vs. normal Cl− + VEGF, n = 6. f HUVECs were incubated with normal Cl− and low Cl− medium for 48 h. PTP1B activity was measured. **P < 0.01 vs. normal Cl−, n = 6. VEGFR2 interacted with PTP1B. The HUVEC lysates were immunoprecipitated (IP) with VEGFR2 antibody (g) or PTP1B antibody (h) followed by immunoblotting with PTP1B antibody and VEGFR2 antibody. i The cells were treated with normal Cl− and low Cl− medium containing VEGF (50 ng/mL) for 48 h. Cell lysates were processed for immunoprecipitation with VEGFR2 antibody, and immunoprecipitated proteins were immunoblotted with PTP1B antibody. j Densitometric analysis of the amount of PTP1B in VEGFR2 immunoprecipitates. **P < 0.01 vs. normal Cl−, ##P < 0.01 vs. normal Cl− + VEGF, n = 5.