Carboxyl-terminus of ADAMTS13 directly inhibits platelet aggregation and ultra large VWF string formation under flow in a free thiol-dependent manner
2014
Objective
ADAMTS13 cleaves von Willebrand factor (VWF), thereby inhibiting thrombus formation. Proteolytic cleavage relies on the amino-terminal (MDTCS) domains, but the role of the more distal carboxyl-terminal domains of ADAMTS13 is not fully understood. A previous study demonstrated the presence of multiple surface- exposed free sulfhydryls on ADAMTS13 that appeared to interact with those on VWF under shear. Here, we determined the physiological relevance of such an interaction in antithrombotic responses under flow.
Keywords:
- Correction
- Source
- Cite
- Save
- Machine Reading By IdeaReader
0
References
0
Citations
NaN
KQI