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. 2015 Jul 27;6(28):25660–25676. doi: 10.18632/oncotarget.4705

Figure 7. The binding between endoglin and the PP2A/B subunit is involved in the disruption of the PP2A complex in human hemangioma specimens.

Figure 7

A. Representative images of immunohistochemical staining of endoglin in human proliferating phase hemangioma specimens and involuting phase hemangioma specimens. Bar = 50 μm B. Quantitative analysis of the IOD value of endoglin staining. (n = 36, t test) *P < 0.05 C. Binding between endoglin and the PP2A/B subunit in HEC-P cells and HEC-I cells was determined by immunoprecipitation and immunoblot. D. Human HEC-P cells were transiently transfected with the PP2A/A and C plasmids and cell lysates were subjected to immunoprecipitation with endoglin and probed with anti-PP2A/A, B, C antibody. Competition assay results showed that ectopic expression of the PP2A/A, C subunits abolished the endoglin-PP2A/B binding. E. Human HEC-I cells were transiently transfected with the endoglin expression plasmids and cell lysates were subjected to immunoprecipitation with PP2A/A, C and probed with anti-PP2A/A, B, C antibody. Competition assay results showed that ectopic expression of endoglin abolished the PP2A/B -PP2A/A, C binding. F. Phosphatase activity assay results showed that increased PP2A activity was detected when the PP2A/A, C subunits were overexpressed in HEC-P cells. In contrast, PP2A activity was decreased when endoglin was overexpressed in HEC-I cells. (n = 3/group, t test) *P < 0.05 G. There was a significant difference in the tumor-free time between the control PyMT TG(+) mice and TG(+) mice treated with PP2A activator FTY720. (n = 7/group, one-way ANOVA) *P < 0.05