Abstract:
:The metalloprotease ADAMTS13 is assumed to regulate the functional levels of von Willebrand factor (VWF) appropriate for normal hemostasis in vivo by reducing VWF multimer size, which directly represents the thrombogenic activity of this factor. Using an in vitro perfusion chamber system, we studied the mechanisms of ADAMTS13 action during platelet thrombus formation on a collagen surface under whole blood flow conditions. Inhibition studies with a function-blocking anti-ADAMTS13 antibody, combined with immunostaining of thrombi with an anti-VWF monoclonal antibody that specifically reflects the VWF-cleaving activity of ADAMTS13, provided visual evidence for a shear rate-dependent action of ADAMTS13 that limits thrombus growth directly at the site of the ongoing thrombus generation process. Our results identify an exquisitely specific regulatory mechanism that prevents arterial occlusion under high shear rate conditions during mural thrombogenesis.
journal_name
Bloodjournal_title
Bloodauthors
Shida Y,Nishio K,Sugimoto M,Mizuno T,Hamada M,Kato S,Matsumoto M,Okuchi K,Fujimura Y,Yoshioka Adoi
10.1182/blood-2007-09-110700subject
Has Abstractpub_date
2008-02-01 00:00:00pages
1295-8issue
3eissn
0006-4971issn
1528-0020pii
blood-2007-09-110700journal_volume
111pub_type
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