Figure 5
N-linked glycans N1515 and N1574 modulate in vitro binding of VWF to macrophages. To examine the biological mechanisms mediating the enhanced clearance of A1A2A3-N1515Q/N1574Q, we assessed binding to THP-1 macrophages in vitro. The binding of A1A2A3 VWF and the glycan variants A1A2A3-N1515Q and A1A2A3-N1574Q to THP-1 macrophages was examined in the presence or absence of 1mg/ml ristocetin. Additionally, all the A1A2A3 variants were subjected to PNGase treatment to remove both N-linked glycans (black columns) and THP-1 macrophage binding was measured. Data are graphed as percentage binding relative to maximal binding (mean ± SEM).

N-linked glycans N1515 and N1574 modulate in vitro binding of VWF to macrophages. To examine the biological mechanisms mediating the enhanced clearance of A1A2A3-N1515Q/N1574Q, we assessed binding to THP-1 macrophages in vitro. The binding of A1A2A3 VWF and the glycan variants A1A2A3-N1515Q and A1A2A3-N1574Q to THP-1 macrophages was examined in the presence or absence of 1mg/ml ristocetin. Additionally, all the A1A2A3 variants were subjected to PNGase treatment to remove both N-linked glycans (black columns) and THP-1 macrophage binding was measured. Data are graphed as percentage binding relative to maximal binding (mean ± SEM).

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