Figure 2
Figure 2. Variation in sialic acid expression on VWF and susceptibility to ADAMTS13 proteolysis. (A) To investigate whether sialic acid expression on VWF influences susceptibility to ADAMTS13 proteolysis, wild-type plasma–derived VWF (pd-VWF) α2-3,6,8,9 neuraminidase–treated VWF (Neu-VWF), and PNGase F–treated VWF (PNG-VWF) preparations were incubated with 3nM human rADAMTS13 in the presence of 1.5M urea. Rate of VWF cleavage was assessed by determining the rate of VWF:CB decrease over time. Results are expressed as residual VWF:CB (mean ± SEM). (B) VWF proteolysis was also studied by nonreducing 1% agarose gel electrophoresis. (C) To determine whether α2-3–linked sialic acid on VWF influenced ADAMTS13 proteolysis, pd-VWF and α2-3 neuraminidase–treated VWF (α2-3 Neu-VWF) were incubated with recombinant ADAMTS13 in the presence of 1.5M urea as before. Rate of proteolysis for α2-3Neu-VWF was compared with pd-VWF by determining residual collagen binding activity.

Variation in sialic acid expression on VWF and susceptibility to ADAMTS13 proteolysis. (A) To investigate whether sialic acid expression on VWF influences susceptibility to ADAMTS13 proteolysis, wild-type plasma–derived VWF (pd-VWF) α2-3,6,8,9 neuraminidase–treated VWF (Neu-VWF), and PNGase F–treated VWF (PNG-VWF) preparations were incubated with 3nM human rADAMTS13 in the presence of 1.5M urea. Rate of VWF cleavage was assessed by determining the rate of VWF:CB decrease over time. Results are expressed as residual VWF:CB (mean ± SEM). (B) VWF proteolysis was also studied by nonreducing 1% agarose gel electrophoresis. (C) To determine whether α2-3–linked sialic acid on VWF influenced ADAMTS13 proteolysis, pd-VWF and α2-3 neuraminidase–treated VWF (α2-3 Neu-VWF) were incubated with recombinant ADAMTS13 in the presence of 1.5M urea as before. Rate of proteolysis for α2-3Neu-VWF was compared with pd-VWF by determining residual collagen binding activity.

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