3.4.21.5: thrombin
This is an abbreviated version!
For detailed information about thrombin, go to the full flat file.
Word Map on EC 3.4.21.5
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3.4.21.5
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platelet
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anticoagulant
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heparin
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thrombosis
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bleeding
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endothelial
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artery
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thromboplastin
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collagen
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agonist
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thromboembolism
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coronary
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procoagulant
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adp
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antithrombotic
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venous
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fibrinolysis
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thrombus
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hemorrhage
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hemostatic
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hirudin
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plasminogen
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antiplatelet
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thrombomodulin
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protease-activated
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arachidonic
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plasmin
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thromboxane
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intravascular
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viii
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d-dimers
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atrial
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thrombocytopenia
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aspirin
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aptamer
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hypercoagulability
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willebrand
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warfarin
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percutaneous
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p-selectin
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rivaroxaban
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platelet-rich
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unfractionated
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coagulopathy
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prothrombotic
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embolism
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haemostasis
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diagnostics
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analysis
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hemophilia
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biotechnology
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thrombolytic
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nutrition
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synthesis
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clopidogrel
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medicine
- 3.4.21.5
- platelet
-
anticoagulant
- heparin
- thrombosis
- bleeding
- endothelial
- artery
- thromboplastin
- collagen
- agonist
- thromboembolism
- coronary
-
procoagulant
- adp
-
antithrombotic
- venous
-
fibrinolysis
- thrombus
- hemorrhage
-
hemostatic
- hirudin
- plasminogen
-
antiplatelet
- thrombomodulin
-
protease-activated
-
arachidonic
- plasmin
-
thromboxane
-
intravascular
- viii
-
d-dimers
- atrial
- thrombocytopenia
- aspirin
- aptamer
- hypercoagulability
- willebrand
- warfarin
-
percutaneous
-
p-selectin
- rivaroxaban
-
platelet-rich
-
unfractionated
- coagulopathy
-
prothrombotic
- embolism
-
haemostasis
- diagnostics
- analysis
- hemophilia
- biotechnology
-
thrombolytic
- nutrition
- synthesis
- clopidogrel
- medicine
Reaction
selective cleavage of Arg-/-Gly bonds in fibrinogen to form fibrin and release fibrinopeptides A and B =
Synonyms
activated factor II, alpha-thrombin, alphaTh, beta-thrombin, blood-coagulation factor II, activated, blood-coagulation factor IIa, clotting factor IIa, EC 3.4.4.13, factor IIa, fibrinogenase, thrombase, thrombin, E, thrombin-C, thrombofort, TLE2, topical, tropostasin
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Natural Substrates Products
Natural Substrates Products on EC 3.4.21.5 - thrombin
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REACTION DIAGRAM
ADAMTS-13 + H2O
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proteolysis of ADAMTS-13 by thrombin causes an 8fold reduction in its affinity for von Willebrand factor VWF that contributes to its loss of VWF-cleaving function, physiologic function, overview
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factor VIII + H2O
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activation by cleavage of Arg372, Arg74, and Arg1689, plays a fundamental role in the amplification of the coagulation cascade
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?
factor XII + H2O
activated factor XII + ?
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activated factor XII cross-links fibrin molecules and stabilizes the fibrin clot
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?
factor XIII + H2O
activated factor XIII + ?
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the enzyme is involved in the coagulation cascade, overview
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galectin-8 + H2O
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although intact isoform G8L stimulates neutrophil adhesion to substrate more efficiently than isoform G8M, the activity of isoform G8L but not that of isoform G8M decreases on thrombin digestion, overview
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galectin-9 + H2O
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thrombin treatment almost completely abolishes eosinophil chemoattractant activity of isoform G9L, overview
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pro-factor XIII + H2O
factor XIII
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activation by cleavage at Arg37 leading to blood coagulation
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?
protease-activated receptor 1 + H2O
activated protease-activated receptor 1 + ?
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activation
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?
protease-activated receptor-1 + H2O
activated PAR-1
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i.e. PAR-1, activation, major thrombin receptor
product induces connective tissue growth factor production, a fibroblast mitogen, which promotes extracellular matrix protein production
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proteinase-activated receptor 1 + H2O
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alpha-thrombin may not effectively catalyze proteinase-activated receptor 1-(1-41) generation
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proteinase-activated receptor 4 + H2O
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alpha-thrombin may not effectively catalyze proteinase-activated receptor 4-(1-47) generation
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?
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cleavage of four Arg-Gly peptide bonds, the enzyme is involved in the final step in the coagulation of mammalian blood
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Fibrinogen + H2O
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the fully reversible interaction of alpha-thrombin with glycoprotein Ibalpha supports the association with platelets of a proteolytically active enzyme that may contribute to activation
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Fibrinogen + H2O
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in intact human erythrocyte leucemia cells thrombin activates adenylate cyclase
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fibrin + ?
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the enzyme mediates the conversion of fibrinogen to fibrin
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fibrin + fibrinopeptide A + fibrinopeptide B
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fibrinogen + H2O
fibrin + fibrinopeptide A + fibrinopeptide B
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704797, 707320, 707506, 707511, 707652, 707672, 707944, 707960, 708032, 708154, 708178, 708248, 708363, 708811, 708816, 709043, 709050, 709074, 709109, 709161, 709242, 709437, 709468, 709588, 710103, 710224, 710402, 710594, 710604, 710610, 710634, 717085, 717199, 717789
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?
fibrinogen + H2O
fibrin + fibrinopeptide A + fibrinopeptide B
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proteolytic activation
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?
fibrinogen + H2O
fibrin + fibrinopeptide A + fibrinopeptide B
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oxidation impairs the capacity of isolated fibrinogen to form a fibrin clot under the effect of thrombin
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fibrin 1 + fibrinopeptide A + fibrinopeptide B
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fibrinogen 1 + H2O
fibrin 1 + fibrinopeptide A + fibrinopeptide B
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?
fibrin 2 + fibrinopeptide A + fibrinopeptide B
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fibrinogen 2 + H2O
fibrin 2 + fibrinopeptide A + fibrinopeptide B
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protease-activated receptor 1 + H2O
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endothelial protein C receptor-dependent cleavage of PAR-1 on vascular endothelial cells, the enzyme exhibts anti-inflammatory activity
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protease-activated receptor 1 + H2O
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thrombin inhibits the tumor necrosis factor-alpha-mediated expression of secretory group IIA phospholipase A2-IIA through the cleavage of protease-activated receptor 1, the EPCR-dependent cleavage of protease-activated receptor 1by thrombin increases the phosphorylation of extracellular signalregulated kinase 1/2
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protease-activated receptor-1 + H2O
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PAR-1 is the major mediator of thrombin signalling and is involved in platelet activation, smooth muscle cells migration and proliferation, PAR-1 activation also regulates many aspects of endothelial cell biology and has been involved in vascular development
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activated protein C + propeptide
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activated protein C has a regulatory function in inhibiting thrombin activation, overview
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protein C zymogen + H2O
activated protein C + propeptide
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on vascular endothelial cells
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?
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enzyme stimulates a marked increase in inositol phosphate accumulation, which is fully mimicked by a selective PAR1 activating peptide. Mitogenic effect of enzyme involves activation of PDGF or EGF receptors and a Gi/o-dependent activation of phosphoinositide 3-kinase. Enzyme stimulates phosphatidylinositol-3,4,5-triphosphate mass accumulation
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additional information
?
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thrombin is a multifunctional trypsin-like protease that plays a role in the blood coagulation system, stimulates platelet aggregation, and promotes its own generation through the activation of factor XI and cofactors V and VII
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additional information
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enzyme deficienxy leads to umbilical cord bleeding at birth, development of hematoma, diminished vitamin K-dependent clotting factor, thrombocytopenia, and at least to lethal retroperitoneal bleeding
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additional information
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enzyme exerts pro-inflammatory and profibrotic effects via proteolytic activation of the major thrombin receptor
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additional information
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enzyme is important in blood coagulation
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?
additional information
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enzyme plays a pivotal role in hemostasis, thrombosis, cell differentiation, and is involved in the activation of many cell types and platelets
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additional information
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enzyme stimulates platelets and exposure of phosphatidylserine on the external surface
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?
additional information
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a hirudin-like pentapeptide from the COOH terminus of factor Va heavy chain regulates the rate and pathway for prothrombin activation, prothrombinase complex regultion, overview
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additional information
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Na+ binding to thrombin is an interaction at the basis of the procoagulant and prothrombotic roles of the enzyme in the blood
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additional information
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the ligand occupancy of endothelial protein C receptor by caveolin-1 switches the protease-activated receptor 1-dependent signaling specificity of thrombin from a permeability-enhancing to a barrier-protective response in endothelial cells, overview
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additional information
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thrombin is initially implicated in hemostasis and fibrin clot formation, and is also involved in cell biology since the discovery of its major receptor, the protease-activated receptor-1, PAR-1, fibrin-adsorbed thrombin interacts with endothelial progenitor cells via the thrombin receptor PAR-1, overview
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additional information
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both thrombin and thrombin receptor agonist peptide enhance the permeability barrier of HPAEC cells, both exhibit a potent barrier protective effect when cells are treated with inactive mutant S195A of protein C prior to stimulation. Thrombin exhibits a potent cytoprotective activity in the lipopolysaccharide-induced permeability and tumor necrosis factor alpha-induced apoptosis and adhesion assays in the protein C mutant S195A treated cells. Treatment with the cholesterol depleting molecule methyl-beta-cyclodextrin eliminates the protective effect
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additional information
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both thrombin and thrombin receptor agonist peptides initiate proinflammatory responses in cells. The occupancy of endothelial protein C receptor by the inactive protein C mutant S195A switches the receptor PAR-1-dependent signaling specificity of thrombin leading to thrombin inhibition of the expression of cell surface adhesion molecules CCAM-I, ICAM-I and E-selectin as well as the binding of neutrophils to tumor necrosis factor alpha-activated endothelial cells. Both thrombin and thrombin receptor agonist peptides activate Rac I and inhibit the activation of RhoA and nuclear factor kappaB pathways in response to tumor necrosis factor alpha in cells pretreated with protein C mutant S195A
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additional information
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in cell cultures of HUVEC and HPAEC cells, low concentrations of thrombin or of receptor PAR-1 agonist peptide induce significant anti-inflammatory activities. Relatively high concentration of thrombin or of PAR-1 agonist peptide show pro-inflammatory activities. The direct anti-inflammatory effects of low concentrations of thrombin are dependent on the activation of PAR-1 and PI3 kinase
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additional information
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treatment of platelets with thrombin or ADP induces activation and mitochondrial association of active proapoptotic proteins Bid, Bax, and Bak. Thrombin evokes mitochondrial membrane depolarization, which is attenuated by catalase
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additional information
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thrombin is generated by proteolysis of its precursor prothrombin at sites of injury
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additional information
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nestin gene expression is regulated by the thrombin-mediated transactivation of EGFR in serum-deprived primary cultures of vascular smooth muscle cells. Upon binding of thrombin, regulator PAR-1 induces c-Src resulting in direct intracellular phosphorylation of EGFR and in the extracellular activation of the matrix metalloprotease MMP-2-mediated shedding of HB-epidermal growth factor
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additional information
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the presence of thrombin induces a significant increase in matrix metalloprotease-9 activity and also increases its mRNA expression in primary astrocytes. Thrombin-induced matrix metalloprotease-9 production is inhibited by the selective inhibitor of protease-activated receptor PAR-1, SCH 79797 and by PDS98059
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additional information
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enzyme stimulates platelets and exposure of phosphatidylserine on the external surface
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additional information
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following activation of platelets by thrombin, 26 proteins exhibit statistically significant differences. Deregulated proteins include proteins of the coagulation system and integrin signalling
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