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. 1997 Jan 6;185(1):153–164. doi: 10.1084/jem.185.1.153

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Effect of EC activation upon ATPDase antigen expression. (a) Western blotting. The polyclonal antibody recognized ATPDase in human EC preparations purified from quiescent- and TNFαstimulated cells by Western blotting. We did not observe significant diminution of ATPDase antigen expression, nor evidence for proteolytic degradation, despite the documented reduction in enzyme activity at this time point. (b) Immunocytofluorometric analysis. These plots demonstrate high levels of surface expression of CD39 on quiescent HUVEC (bold line, anti-CD39; faint line, isotype control mAb) (A). The expression of CD39 epitopes on the EC surface was largely unaltered after TNFα stimulation (10 ng/ml; B) or direct oxidative stress with H₂O₂ (100 μM; C). Cells were analyzed by flow cytometry as described in Materials and Methods.

Effect of EC activation upon ATPDase antigen expression. (a) Western blotting. The polyclonal antibody recognized ATPDase in human EC preparations purified from quiescent- and TNFαstimulated cells by Western blotting. We did not observe significant diminution of ATPDase antigen expression, nor evidence for proteolytic degradation, despite the documented reduction in enzyme activity at this time point. (b) Immunocytofluorometric analysis. These plots demonstrate high levels of surface expression of CD39 on quiescent HUVEC (bold line, anti-CD39; faint line, isotype control mAb) (A). The expression of CD39 epitopes on the EC surface was largely unaltered after TNFα stimulation (10 ng/ml; B) or direct oxidative stress with H₂O₂ (100 μM; C). Cells were analyzed by flow cytometry as described in Materials and Methods.