Figure 2.
Figure 2. Plasmin binds annexin A2 and S100A10 expressed on the monocyte surface. Monocytes (20 × 106) were exposed to plasmin cross-linker 0.143 CTA U/mL in the presence or absence of the inhibitor of plasmin binding, t-AMCA 2 mM, for 7 minutes. The cross-linker was activated by UV light, and after solubilization, the biotinylated proteins were precipitated using streptavidin beads. Precipitated proteins were analyzed by immunoblotting with mAbs against annexin A2 and S100A10. VPLCK-plasmin indicates catalytically inactivated plasmin generated by pretreatment with 25 μM VPLCK; a 35-fold molar excess of VPLCK-plasmin was used. Results of one of 3 independent experiments are shown.

Plasmin binds annexin A2 and S100A10 expressed on the monocyte surface. Monocytes (20 × 106) were exposed to plasmin cross-linker 0.143 CTA U/mL in the presence or absence of the inhibitor of plasmin binding, t-AMCA 2 mM, for 7 minutes. The cross-linker was activated by UV light, and after solubilization, the biotinylated proteins were precipitated using streptavidin beads. Precipitated proteins were analyzed by immunoblotting with mAbs against annexin A2 and S100A10. VPLCK-plasmin indicates catalytically inactivated plasmin generated by pretreatment with 25 μM VPLCK; a 35-fold molar excess of VPLCK-plasmin was used. Results of one of 3 independent experiments are shown.

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