Results 11 to 20 of about 3,354,179 (197)

Improvement of recombinant ADAMTS13 production through a more optimal signal peptide or an N-terminal fusion protein

Journal of Thrombosis and Haemostasis, 2022
Recombinant human ADAMTS13 (rADAMTS13) is a key protein in fundamental research for investigating its mode of action and the pathophysiology of thrombotic thrombocytopenic purpura (TTP). However, the expression of rADAMTS13 is quite low in mammalian cells, which makes the production of the protein time-consuming and labor-intensive.We aimed at ...
Nuno Graça, Elien Roose, Kadri Kangro
exaly   +5 more sources

Generation and validation of small ADAMTS13 fragments for epitope mapping of anti‐ADAMTS13 autoantibodies in immune‐mediated thrombotic thrombocytopenic purpura

Research and Practice in Thrombosis and Haemostasis, 2020
Background In immune‐mediated thrombotic thrombocytopenic purpura (iTTP), patients develop an immune response against the multidomain enzyme ADAMTS13.
Kadri Kangro, Elien Roose, An‐Sofie Schelpe, Edwige Tellier, Gilles Kaplanski, Jan Voorberg, Simon F. De Meyer, Andres Männik, Karen Vanhoorelbeke   +8 more
doaj   +3 more sources

Inherited ADAMTS13 mutations associated with Thrombotic Thrombocytopenic Purpura: a short review and update [PDF]

Platelets, 2023
ADAMTS13 is a plasma metalloprotease with the primary function of cleaving VWF to maintain hemostasis. Circulating ADAMTS13 is in the closed conformation until blood vessel injury triggers a VWF-dependant activation to the open active form of the protein.
Zoe Markham-Lee, Neil V. Morgan, Jonas Emsley   +2 more
doaj   +2 more sources

Phenotypic expression of ADAMTS13 in glomerular endothelial cells. [PDF]

PLoS ONE, 2011
BackgroundADAMTS13 is the physiological von Willebrand factor (VWF)-cleaving protease. The aim of this study was to examine ADAMTS13 expression in kidneys from ADAMTS13 wild-type (Adamts13⁺/⁺) and deficient (Adamts13⁻/⁻) mice and to investigate the ...
Ramesh Tati, Ann-Charlotte Kristoffersson, Anne-Lie Ståhl, Matthias Mörgelin, David Motto, Simon Satchell, Peter Mathieson, Minola Manea-Hedström, Diana Karpman   +8 more
doaj   +3 more sources

Decreased protein C activity, lower ADAMTS13 antigen and free protein S levels accompanied by unchanged thrombin generation potential in hospitalized COVID-19 patients

Thrombosis Research, 2023
COVID-19 is associated with an increased thromboembolic risk. However, the mechanisms triggering clot formation in those patients remain unknown.In 118 adult Caucasian severe but non-critically ill COVID-19 patients (median age 58 years; 73 % men) and 46 controls, we analyzed in vitro plasma thrombin generation profile (calibrated automated thrombogram
Wójcik, Krzysztof, Bazan-Socha, Stanisława, Celejewska-Wójcik, Natalia, Górka, Karolina, Lichołai, Sabina, Polok, Kamil, Stachura, Tomasz, Zaręba, Lech, Dziedzic, Radosław, Gradzikiewicz, Ada, Sanak, Marek, Musiał, Jacek, Sładek, Krzysztof, Iwaniec, Teresa   +13 more
exaly   +4 more sources

Pathological Allostery in ADAMTS13: Autoantibody-Induced Modulation and Its Role in Immune Thrombotic Thrombocytopenic Purpura (iTTP) [PDF]

Pharmaceuticals
Background/Objectives: ADAMTS13 is a plasma metalloprotease that cleaves von Willebrand Factor (vWF), a multimeric glycoprotein involved in platelet recruitment during primary hemostasis.
Madison Gil, Konstantine Halkidis
doaj   +2 more sources

Local Elongation of Endothelial Cell-anchored von Willebrand Factor Strings Precedes ADAMTS13 Protein-mediated Proteolysis* [PDF]

Journal of Biological Chemistry, 2011
Platelet-decorated von Willebrand factor (VWF) strings anchored to the endothelial surface are rapidly cleaved by ADAMTS13. Individual VWF string characteristics such as number, location, and auxiliary features of the ADAMTS13 cleavage sites were explored here using imaging and computing software.
Hiroshi Uji-I, Simon F De Meyer, Johan Hofkens   +2 more
exaly   +4 more sources

An IAP retrotransposon in the mouse ADAMTS13 gene creates ADAMTS13 variant proteins that are less effective in cleaving von Willebrand factor multimers

Blood, 2007
AbstractSevere deficiency of ADAMTS13, a von Willebrand factor (VWF)–cleaving metalloprotease, causes thrombotic thrombocytopenic purpura. When analyzed with VWF multimers, but not with an abbreviated VWF peptide (VWF73) as the substrate, the plasma ADAMTS13 activity levels of mouse strains segregated into a high and a low group that differed by ...
Eric E Bouhassira, Han-Mou Tsai
exaly   +4 more sources

Probing ADAMTS13 substrate specificity using phage display. [PDF]

PLoS ONE, 2015
Von Willebrand factor (VWF) is a large, multimeric protein that regulates hemostasis by tethering platelets to the subendothelial matrix at sites of vascular damage.
Karl C Desch, Colin Kretz, Andrew Yee, Robert Gildersleeve, Kristin Metzger, Nidhi Agrawal, Jane Cheng, David Ginsburg   +7 more
doaj   +2 more sources

Optimization of plasma-based BioID identifies plasminogen as a ligand of ADAMTS13

Scientific Reports
ADAMTS13, a disintegrin and metalloprotease with a thrombospondin type 1 motif, member 13, regulates the length of Von Willebrand factor (VWF) multimers and their platelet-binding activity. ADAMTS13 is constitutively secreted as an active protease and is
Hasam Madarati, Veronica DeYoung, Kanwal Singh, Taylor Sparring, Andrew C. Kwong, James C. Fredenburgh, Cherie Teney, Marlys L. Koschinsky, Michael B. Boffa, Jeffrey I. Weitz, Colin A. Kretz   +10 more
doaj   +2 more sources