ArticleJournal of thrombosis and haemostasis : JTH2009
Multi-step binding of ADAMTS-13 to von Willebrand factor.
Article in Journal of thrombosis and haemostasis : JTH, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
37 citing papers in PubMed, 89 citations in OpenAlex.
- Trp1250, Lys1252, and Arg1367 of ADAMTS13 comprise a hot spot for anti-CUB domain antibodies in patients with iTTP.Blood advances · 2025Article
- Open or closed? Understanding the molecular mechanisms and clinical implications of ADAMTS13's conformation.HemaSphere · 2025Review
- Unraveling antibody-induced structural dynamics in the ADAMTS13 CUB1-2 domains via HDX-MS.Blood advances · 2025Article
- Mechanisms of ADAMTS13 regulation.Journal of thrombosis and haemostasis : JTH · 2022Review
- Causal relationship among obesity and body fat distribution and epilepsy subtypes.Frontiers in neurology · 2022Review
- Predicting pathological von Willebrand factor unraveling in elongational flow.Biophysical journal · 2021Article
- Pathologic Shear and Elongation Rates Do Not Cause Cleavage of Von Willebrand Factor by ADAMTS13 in a Purified System.Cellular and molecular bioengineering · 2020Article
- Identification of cysteine thiol-based linkages in ADAMTS13 in support of a non-proteolytic regulation of von Willebrand factor.Journal of thrombosis and haemostasis : JTH · 2019Article
- Domain-specific mechanical modulation of VWF-ADAMTS13 interaction.Molecular biology of the cell · 2019Article
- Article
- Exploring the "minimal" structure of a functional ADAMTS13 by mutagenesis and small-angle X-ray scattering.Blood · 2019Article
- A Review of Integrin-Mediated Endothelial Cell Phenotype in the Design of Cardiovascular Devices.Annals of biomedical engineering · 2019Review
- ADAMTS-13 and von Willebrand factor: a dynamic duo.Journal of thrombosis and haemostasis : JTH · 2018Review
- A model for the conformational activation of the structurally quiescent metalloprotease ADAMTS13 by von Willebrand factor.The Journal of biological chemistry · 2017Article
- Conformational quiescence of ADAMTS-13 prevents proteolytic promiscuity.Journal of thrombosis and haemostasis : JTH · 2016Article
- Article
- Generation of Anti-Murine ADAMTS13 Antibodies and Their Application in a Mouse Model for Acquired Thrombotic Thrombocytopenic Purpura.PloS one · 2016Article
- Linker regions and flexibility around the metalloprotease domain account for conformational activation of ADAMTS-13.Journal of thrombosis and haemostasis : JTH · 2015Article
- ADAMTS13 and von Willebrand factor interactions.Current opinion in hematology · 2015Article
- Allosteric activation of ADAMTS13 by von Willebrand factor.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
backgroundADAMTS-13 proteolytic activity is controlled by the conformation of its substrate, von Willebrand factor (VWF), and changes in the secondary structure of VWF are essential for efficient cleavage. Substrate recognition is mediated through several non-catalytic domains in ADAMTS-13 distant from the active site.
objectivesWe hypothesized that not all binding sites for ADAMTS-13 in VWF are cryptic and analyzed binding of native VWF to ADAMTS-13.
methodsImmunoprecipiation of VWF-ADAMTS-13 complexes using anti-VWF antibodies and magnetic beads was used. Binding was assessed by Western blotting and immunosorbent assays.
resultsCo-immunoprecipitation demonstrated that ADAMTS-13 binds to native multimeric VWF (K(d) of 79 +/- 11 nmol L(-1)) with no measurable proteolysis. Upon shear-induced unfolding of VWF, binding increased 3-fold and VWF was cleaved. Binding to native VWF was saturable, time dependent, reversible and did not vary with ionic strength (I of 50-200). Moreover, results with ADAMTS-13 deletion mutants indicated that binding to native VWF is mediated through domains distal to the ADAMTS-13 spacer, probably thrombospondin-1 repeats. Interestingly, this interaction occurs in normal human plasma with an ADAMTS-13 to VWF stoichiometry of 0.0040 +/- 0.0004 (mean +/- SEM, n = 10).
conclusionsADAMTS-13 binds to circulating VWF and may therefore be incorporated into a platelet-rich thrombus, where it can immediately cleave VWF that is unfolded by fluid shear stress.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.