ArticleJournal of thrombosis and haemostasis : JTH2021
A human monoclonal antibody against the distal carboxyl terminus of ADAMTS-13 modulates its susceptibility to an inhibitor in thrombotic thrombocytopenic purpura.
Article in Journal of thrombosis and haemostasis : JTH, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 15 citations in OpenAlex.
- Human monoclonal and polyclonal anti-ADAMTS13 antibodies in immune thrombotic thrombocytopenic purpura: variable mechanisms of inhibition.Journal of thrombosis and haemostasis : JTH · 2026Article
- Pathological Allostery in ADAMTS13: Autoantibody-Induced Modulation and Its Role in Immune Thrombotic Thrombocytopenic Purpura (iTTP).Pharmaceuticals (Basel, Switzerland) · 2026Review
- ADAMTS-13 R1206K variant exhibits an open conformation and an enhanced proteolytic activity toward von Willebrand factor.Journal of thrombosis and haemostasis : JTH · 2026Article
- Hydrogen Exchange Mass Spectrometry (HX-MS) for Mapping Antibody Binding Sites and Conformational Dynamics of ADAMTS13.Methods in molecular biology (Clifton, N.J.) · 2026Article
- The landscape of ADAMTS13-related tests in thrombotic thrombocytopenic purpura: a review.Frontiers in medicine · 2026Review
- Method for Assessing Inhibition Kinetics of Autoantibodies Against ADAMTS13 in Immune-Mediated Thrombotic Thrombocytopenic Purpura.Methods in molecular biology (Clifton, N.J.) · 2026Article
- 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
- Arginine Methylation by PRMT1 Affects ADAMTS13 Secretion and Enzymatic Activity.Arteriosclerosis, thrombosis, and vascular biology · 2025Article
- Anti-ADAMTS13 Autoantibodies in Immune-Mediated Thrombotic Thrombocytopenic Purpura.Antibodies (Basel, Switzerland) · 2025Review
- Mechanistic insight into multiple antibody binding to ADAMTS13 in immune thrombotic thrombocytopenic purpura.Research and practice in thrombosis and haemostasis · 2024Article
- ADAMTS13 in the New Era of TTP.International journal of molecular sciences · 2024Review
- Mechanism underlying severe deficiency of plasma ADAMTS-13 activity in immune thrombotic thrombocytopenic purpura.Journal of thrombosis and haemostasis : JTH · 2024Article
- Immune thrombotic thrombocytopenic purpura: pathogenesis and novel therapies: a narrative review.Annals of blood · 2023Article
- ADAMTS13 Biomarkers in Management of Immune Thrombotic Thrombocytopenic Purpura.Archives of pathology & laboratory medicine · 2023Review
- Mechanisms of inhibition of human monoclonal antibodies in immune thrombotic thrombocytopenic purpura.Blood · 2023Article
- Immune and Hereditary Thrombotic Thrombocytopenic Purpura: Can ADAMTS13 Deficiency Alone Explain the Different Clinical Phenotypes?Journal of clinical medicine · 2023Review
- ADAMTS13 conformations and mechanism of inhibition in immune thrombotic thrombocytopenic purpura.Journal of thrombosis and haemostasis : JTH · 2022Review
- The standard of care for immune thrombotic thrombocytopenic purpura today.Journal of thrombosis and haemostasis : JTH · 2021Review
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
backgroundImmune thrombotic thrombocytopenic purpura (iTTP) is a potentially fatal thrombotic microangiopathy, resulting from a severe deficiency of plasma ADAMTS-13 (A Disintegrin And Metalloproteinase with ThromboSpondin type 1 motif, member 13) activity. IgG-type autoantibodies are primarily responsible for the inhibition of plasma ADAMTS-13 activity. However, the mechanism underlying autoantibody-mediated inhibition is not fully understood.
objectiveThe purpose of the present study is to determine the role of IgG autoantibodies against various carboxyl-terminal domains of ADAMTS-13 in regulating ADAMTS-13 activity and its inhibition.
methodVarious human monoclonal antibodies isolated by phage display, recombinant protein expression and purification, and biochemical analyses were employed for the study.
resultsOur results demonstrate for the first time that a human monoclonal antibody fragment, the single chain fragment of the variable region (scFv) isolated from a patient with acute iTTP that binds the distal carboxyl-terminus of ADAMTS-13, is able to activate ADAMTS-13 and increase the proteolytic cleavage of a FRETS-VWF73 substrate; moreover, binding of such a human monoclonal antibody against the carboxyl-terminus of ADAMTS-13 to plasma ADAMTS-13 appears to modulate inhibition by another human monoclonal antibody (i.e., scFv4-20), also isolated from an iTTP patient, that targets the spacer domain of ADAMTS-13. These results provide new insights into our understanding of the pathogenesis of iTTP.
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Registered trials
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.