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ADAMTS13 Antibody and Inhibitor Assays

2023
A finding of an ADAMTS13 (a disintegrin-like and metalloprotease with thrombospondin type 1 motif, member 13) activity level of
Gary W, Moore   +2 more
openaire   +2 more sources

ADAMTS13 in Health and Disease

Acta Haematologica, 2009
We raised a set of monoclonal antibodies (mAb) against recombinant human ADAMTS13, constructed the first antigen test fully based on mAbs and compared ADAMTS13 antigen and enzymatic activity levels in a large set of plasma samples collected from different patients and healthy controls.
Hendrik B, Feys   +2 more
openaire   +2 more sources

ADAMTS13: origins, applications, and prospects

Transfusion, 2018
ADAMTS13 is an enzyme that acts by cleaving prothrombotic von Willebrand factor (VWF) multimers from the vasculature in a highly regulated manner. In pathologic states such as thrombotic thrombocytopenic purpura (TTP) and other thrombotic microangiopathies (TMAs), VWF can bind to the endothelium and form large multimers. As the anchored VWF chains grow,
William E. Plautz   +5 more
openaire   +2 more sources

Improving on nature: redesigning ADAMTS13

Blood, 2012
In this issue of Blood , Jian and coworkers report on a gain-of function variant of ADAMTS13 that is resistant to the autoantibodies responsible for acquired thrombotic thrombocytopenic purpura (TTP).[1][1] Auto-antibodies directed toward ADAMTS13 prohibit cleavage of von Willebrand factor (VWF)
Hovinga, Johanna A. Kremer   +1 more
openaire   +2 more sources

The emerging concept of residual ADAMTS13 activity in ADAMTS13-deficient thrombotic thrombocytopenic purpura

Blood Reviews, 2013
Thrombotic thrombocytopenic purpura (TTP) is a rare, life-threatening disease characterized by acute episodes of widespread microvascular thrombosis. The discovery that the plasmatic activity of the von Willebrand factor cleaving protease, ADAMTS13, is severely deficient in patients with TTP partially clarified the pathophysiology of the disease ...
L. A. Lotta   +3 more
openaire   +3 more sources

Variants in ADAMTS13 and Smoking Contribute to Plasma ADAMTS13 Level Variation

Blood, 2014
Abstract Homeostatic processing of von Willebrand factor (VWF) in the circulation relies on proteolysis of ultra-large VWF (ULVWF) multimers by the metalloprotease ADAMTS13. Deficiency in ADAMTS13 results in Thrombotic Thrombocytopenic Purpura (TTP) due to the accumulation of thrombogenic ULVWF.
Karl C. Desch   +6 more
openaire   +1 more source

Hemoglobin versus ADAMTS13

Blood, 2005
Comment on Studt et al, page [542][1] Free hemoglobin inhibits ADAMTS13 activity in vitro, demonstrating a potential source of artifact affecting ADAMTS13 activity assays and inhibitor screens. Deficiency of the ADAMTS13 metalloprotease causes thrombotic thrombocytopenic purpura (TTP).
openaire   +1 more source

ADAMTS13 and Angiogenesis

2015
ADAMTS13 has been identified as the von Willebrand factor-cleaving protease and is deficient in the disorder thrombotic thrombocytopenic purpura. The identification of vascular endothelium as a site of synthesis and secretion of ADAMTS13 has led to studies of the role of ADAMTS13 in angiogenesis.
Manfai Lee, George M. Rodgers
openaire   +1 more source

ADAMTS13

Archives of Surgery, 2012
Delawir Kahn, Jake E. Krige
openaire   +1 more source

ADAMTS13: Structure and Function

2015
ADAMTS13, a plasma metalloprotease that cleaves von Willebrand factor (VWF), has been shown to have both antithrombotic and anti-inflammatory activities. Severe deficiency of plasma ADAMTS13 activity is a primary cause of thrombotic thrombocytopenic purpura (TTP), a potentially fatal syndrome, but mild to moderate deficiency of plasma ADAMTS13 activity
openaire   +1 more source

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