Figure 2
Figure 2. KSHV infection increases VE-cadherin and β-catenin phosphorylation. (A) VE-cadherin was immunoprecipitated with anti–VE-cadherin antibody from lysates of HUVEC and KSHV-HUVEC and analyzed by Western blot using anti-phosphotyrosine antibody (clone 4G10). (B) HUVEC and KSHV-HUVEC lysates were analyzed by Western blot for phosphorylated forms of VE-cadherin using antibodies that specifically recognize VE-cadherin phosphorylated at Tyr-658 (Y658) and Tyr-731 (Y731). Total VE-cadherin was used as a loading control. (C) β-catenin was immunoprecipitated with anti–β-catenin antibody from lysates of HUVEC and KSHV-HUVEC, and analyzed by Western blot using anti-phosphotyrosine antibody (clone 4G10). (D) HUVEC and KSHV-HUVEC lysates were analyzed by Western blot for phosphorylated forms of β-catenin using antibodies that specifically recognize β-catenin phosphorylated at Tyr-654 (Y654). Total β-catenin was used as a loading control.

KSHV infection increases VE-cadherin and β-catenin phosphorylation. (A) VE-cadherin was immunoprecipitated with anti–VE-cadherin antibody from lysates of HUVEC and KSHV-HUVEC and analyzed by Western blot using anti-phosphotyrosine antibody (clone 4G10). (B) HUVEC and KSHV-HUVEC lysates were analyzed by Western blot for phosphorylated forms of VE-cadherin using antibodies that specifically recognize VE-cadherin phosphorylated at Tyr-658 (Y658) and Tyr-731 (Y731). Total VE-cadherin was used as a loading control. (C) β-catenin was immunoprecipitated with anti–β-catenin antibody from lysates of HUVEC and KSHV-HUVEC, and analyzed by Western blot using anti-phosphotyrosine antibody (clone 4G10). (D) HUVEC and KSHV-HUVEC lysates were analyzed by Western blot for phosphorylated forms of β-catenin using antibodies that specifically recognize β-catenin phosphorylated at Tyr-654 (Y654). Total β-catenin was used as a loading control.

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