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1,10-phenanthroline
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activity can be restored by Ca2+
Ca2+
enzyme catalytic activity in blood plasma is tuned by varying buffer calcium, with lower divalent ion concentrations enhancing cleavage
Cl-
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Chloride ions inhibit von Willebrand factor hydrolysis by ADAMTS-13 of the A1-A2-A3 and A1-A2 domains in the presence of either urea or high shear stress, whereas this effect is either absent or negligible when using A2 and A2-A3 domains
CoCl2
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an increasing concentration of CoCl2 inhibits ADAMTS13 activity
H2O2
treatment with 25 nM myeloperoxidase plus 50 microM H2O2 reduces ADAMTS13 activity by >85%. Residues Met249, Met331, and Met496 in important functional domains of ADAMTS13 are oxidized to methionine sulfoxide in an HOCl concentration-dependent manner
heparin
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inhibits ADAMTS13 activity through inhibition of enzyme binding to endothelial cell surfaces, overview
HOCl
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HOCl can oxidize methionine to methionine sulfoxide and tyrosine to chlorotyrosine, oxidation of VWF A2 peptide, at Met1606 and Tyr1605, markedly impairs ADAMTS13 cleavage. Oxidative modification by myeloperoxidase/H2O2 is similar to that produced by HOCl
Mn2+
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ADAMTS13 activity is decreased in the presence of 0.9 mM Ni2+
MnSO4
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an increasing concentration of MnSO4 inhibits ADAMTS13 activity
N-ethylmaleimide
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slow and weak inhibition
Ni2+
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ADAMTS13 activity is markedly decreased in the presence of 0.9 mM Ni2+
NiSO4
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an increasing concentration of NiSO4 inhibits ADAMTS13 activity
peroxynitrite
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formation of methionine sulfoxide by peroxynitrite at position 1606 of von Willebrand factor inhibits its cleavage by ADAMTS-13 a prothrombotic mechanism in diseases associated with oxidative stress, overview. Oxidation by peroxynitrite of purified VWF multimers inhibits ADAMTS-13 hydrolysis, but does not alter their electrophoretic pattern nor their ability to induce platelet agglutination by ristocetin. In vitro treatment of ADAMTS-13 with peroxynitrite over a concentration ranging from 0.050 to 0.250 mM causes a complete inhibition of the protease activity of the enzyme
plasma from patients with thrombotic thrombocytopenic purpurea
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Pro-1645-Lys-1668 fragment of von Willebrand factor 73
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Trypsin
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inhibits ADAMTS13 activity through inhibition of enzyme binding to endothelial cell surfaces, overview
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VWFA2 domain
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a C-terminal 32 kDa fragment of VWF, soluble VWFA2 domain effectively inhibits the binding of ADAMTS13 to immobilized VWFA2, and completely inhibits the interaction between ADAMTS13 and immobilized 64 kDa VWFA1A2A3 fragment
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W688X6-1
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the monoclonal antibody W688X6-1 shows dose-dependent inhibitory activity toward ADAMTS13-mediated hydrolysis
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WH2-22-1A
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the monoclonal antibody WH2-22-1A shows dose-dependent inhibitory activity toward ADAMTS13-mediated hydrolysis
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Z-Phe-Phe-CHN2
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best peptidyl diazomethyl ketone inhibitor
EDTA
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activity can be restored by Ca2+, complete inhibition
EDTA
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complete inhibition
EDTA
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no activity in the presence of EDTA
EDTA
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complete inhibition at 10 mM
EDTA
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potent inhibitor of the metalloprotease ADAMTS13
EDTA
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complete inhibition at 10 mM
EGTA
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activity can be restored by Ca2+, complete inhibition
EGTA
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complete inhibition
Zn2+
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ADAMTS13 activity is undetectable at concentrations of zinc ions above 3 mM Zn2+
Zn2+
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ADAMTS13 activity is markedly decreased in the presence of 0.9 mM Zn2+
additional information
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no inhibition by iodoacetamide, leupeptin, and serine protease inhibitors DFP, PMSF, aprotinin
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additional information
enzyme is inhibited by plasma from an individuum with acquired thrombotic thrombocytopenic pupura
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additional information
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enzyme is inhibited by plasma from an individuum with acquired thrombotic thrombocytopenic pupura
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additional information
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inhibitory autoantibodies from plasma of 3 patients with acquired thrombotic thrombocytopenic purpura, epitope mapping
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additional information
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inhibition by autoantibodies from patients with acquired thrombotic thrombocytopenic purpura
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additional information
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no inhibition by iodoacetamide, leupeptin, and serine protease inhibitorsDFP, PMSF, aprotinin
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additional information
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inhibition of the enzyme by IgG from a patient with idiopathic thrombotic thrombocytopenic pupura
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additional information
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increasing concentrations of BaCl2 (up to 5 mM) have little effect on the activity of ADAMTS13 at pH 7.4, Mg(SO4) and Cu(SO4) have little effect on the activity of ADAMTS13 at pH 7.4
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additional information
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proteolysis of ADAMTS-13 by thrombin leads to a 8fold reduction in affinity for von Willebrand factor
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additional information
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malaria patients possess high ADAMTS13 autoantibodies levels as well as endogenous ADAMTS13 inhibitors compared to healthy controls
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additional information
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construction and screening of an epitope peptide library, e.g. of epitope-A, i.e. a C-terminus of spacer domain from Arg670 to Gln684, and epitope-B, i.e. Pro618 to Glu641 in the middle of spacer domain. Synthetic epitope-B peptide inhibits the cleavage of VWF by ADAMTS13, while the synthetic epitope-A peptide does inhibit not as efficiently as epitope-B. Elimination of four amino acids from either sides of epitope-B terminus markedly reduces the inhibitory effect
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additional information
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inhibitory anti-ADAMTS 13 antibodies, measurement and clinical application, overview
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additional information
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C-terminal VWF fragments, as well as an antibody specifically directed toward the VWF D4 domain, inhibit VWF proteolysis by ADAMTS13 under shear conditions
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additional information
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specific blockade of von Willebrand factor string cleavage by antibody to ADAMTS-13, overview
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additional information
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substrate modified by treatment with PNGase F to remove complex N-linked glycan structures results in increased ADAMTS13 activity
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additional information
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auto-antibodies against ADAMTS13 lead to ADAMTS13 deficiency, which causes e.g. thrombotic thrombocytopenic purpurea, overview
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additional information
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influenza A infection is sufficient to trigger thrombotic thrombocytopenic purpura by producing the anti-ADAMTS13 IgG inhibitor, overview
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additional information
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an endogenous ADAMTS13 inhibitor can cause enzyme deficiency
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additional information
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infection with Plasmodium falciparum inhibits ADAMTS13. ADAMTS13 activity in normal plasma is reduced by approximately 60% after pooled normal plasma is incubated in a 3:1 mix with malarial plasma for 30 min
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additional information
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protease activity of ADAMTS13 is controlled not by natural inhibitors but by conformational changes in its substrate, which are induced when von Willebrand factor is subject to elevated rheologic shear forces
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additional information
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monoclonal antibody SZ34 inhibits proteolytic cleavage of VWF by ADAMTS13 in a concentration-dependent manner under fluid shear stress, but not under static/denaturing conditions (IC50 0.05 mg/ml). Thrombospondin-1 decreases the rate of von Willebrand factor proteolysis by ADAMTS13 by competing with ADAMTS13 for the A3 domain of von Willebrand factor
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additional information
exposure of ADAMTS13 to activated human neutrophils results in oxidation of residues Met249, Met331, and Met496 in important functional domains of ADAMTS13. ADAMTS13 treated with either neutrophil elastase or plasmin is inhibited to a lesser extent, especially in the presence of plasma.
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additional information
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exposure of ADAMTS13 to activated human neutrophils results in oxidation of residues Met249, Met331, and Met496 in important functional domains of ADAMTS13. ADAMTS13 treated with either neutrophil elastase or plasmin is inhibited to a lesser extent, especially in the presence of plasma.
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additional information
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ADAMTS-13 activity is evaluated in a model of sepsis induced by cecum ligature and puncture in wild-type and Vwf-/- mice. In wild-type mice, cecum ligature and puncture-induced sepsis elicits a significant ADAMTS-13 decrease, and a strong negative correlation exists between von Willebrand factor, VWF, and ADAMTS-13. In Vwf-/- mice, cecum ligature and puncture also induces severe sepsis, but ADAMTS-13 is not significantly diminished
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additional information
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CCl4 at concentration of 6.5 mM does not directly inhibit the activity of ADAMTS-13
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