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
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fibrinolysis
- thrombus
- hemorrhage
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hemostatic
- hirudin
- plasminogen
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antiplatelet
- thrombomodulin
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protease-activated
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arachidonic
- plasmin
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thromboxane
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intravascular
- viii
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d-dimers
- atrial
- thrombocytopenia
- aspirin
- aptamer
- hypercoagulability
- willebrand
- warfarin
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percutaneous
-
p-selectin
- rivaroxaban
-
platelet-rich
-
unfractionated
- coagulopathy
-
prothrombotic
- embolism
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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
ECTree
3.4.21.5 thrombinAdvanced search results
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Application on EC 3.4.21.5 - thrombin
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APPLICATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
analysis
biotechnology
diagnostics
concentrations of active alpha-thrombin, tissue factor-factor VIIa-factor Xa ternary complex, and intrinsic tenase complex with factor X, at specific time windows, can be used to classify acute coronary syndromes to an accuracy of about 87.2%. Such a combination can be used to efficiently assay the coagulation system
medicine
nutrition
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comparison of anticoagulation response to thrombin inhibitors ximelagatran and warfarin in rats on a normal diet to those on a vitamin K deficient diet. Ximelagatran and warfarin increase prothrombin time, activated partial thromboplastin time and ecarin clotting time in rats on normal diet. Vitamin K deficient diet alone causes modest increases in prothrombin time, activated partial thromboplastin time and ecarin clotting time. The anticoagulant activity of both ximelagatran and warfarin is significantly greater in rats on vitamin K deficient diet compared to those on normal diet. Thrombin activity is reduced by both ximelagatran and warfarin to 58% and 44%, respectively, in rats on normal diet. Thrombin activity is virtually abolished by both drugs in rats on vitamin K deficient diet
synthesis
additional information
a modified in situ proteolysis approach is applied to specifically remove the His tag by thrombin cleavage during crystallization screening trials. This improves the morphology and diffraction quality of the crystals and allowes the acquisition of high-resolution diffraction data and structure solution
analysis
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detection of enzyme complexed with polyclonal anti-prothrombin antiserum. Enzyme retains enzymatic activity, and binding to antibody may enhance the efficiency of proenzyme activation
analysis
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affinity probe capillary electrophoresis/laser-induced fluorescence polarization assay for detection of human thrombin using a specific aptamer as probe. Monovalent and bivalent cations promoting the formation of a stable G quadruplex conformation in the aptamer may enhance the binding of the aptamer and thrombin, while cations like K+ and Mg2+ cannot stabilize the affinity complex. Without the use of typical cations, a highly sensitive assay of human thrombin was developed with the corresponding detection limits of 4.38×10?19 and 2.94×10?19 mol in mass for standard solution and human serum, respectively
analysis
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conjugation of angiomax to a 5'-amino oligonucleotide and assembly into a two-dimensional DNA lattice for observation of the binding of thrombins to the DNA lattice. Use of the functionalized DNA lattices as a platform for investigation of biomolecular interactions such as drug-protein, protein-protein, DNA-RNA, and DNA-protein interactions in the nano- and subnanoscales
analysis
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development of a biosensor for thrombin detection using surface-enhanced Raman spectroscopy. The method utilizes the electrostatic interaction between capture thrombin aptamer and probe crystal violet molecules. Procedure shows a highly specific selectivity and a linear detection of thrombin in the range from 0.1 nM to 10 nM with a detection limit of about 20 pM and realizes the thrombin detection in human blood serum solution directly
analysis
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development of a direct and an indirect competitive assay for thrombin by an electrochemical aptamer-based assay coupled to magnetic beads. With the direct competitive assay, when the aptamer is immobilised onto the magnetic beads, a detection limit of 430 nM for thrombin is achieved. A detection limit of 175 nM is obtained by detecting the product of the enzymatic reaction catalysed by thrombin. A sandwich assay reaches a detection limit of 0.45 nM of thrombin
analysis
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development of a modified electrochemical sandwich model for target protein detection using differential pulse voltammetry. With model target analyte thrombin, the sensor shows a linear response for thrombin in the range 1-60 nM with a detection limit of 0.5 nM
analysis
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development of an aptamer-based surface enhanced resonance Raman scattering sensor with high sensitivity, specificity, and stability for the detection of human alpha-thrombin. The sensor displays a limit of detection of 100 pM by monitoring the signal change upon the single-step of thrombin binding to immobilized thrombin binding aptamer and specifically discriminates thrombin from other proteins. The sensor can detect 1 nM thrombin in the presence of complex biofluids, such as 10% fetal calf serum, and is sufficiently robust for clinical diagnostic applications
analysis
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study on the effects of dilution on the thrombin generation process in assessing the clotting function. Anticoagulant pathways are far more affected by dilution than the procoagulant pathways. Plasma dilution causes a loss of sensitivity towards thrombomodulin and activated protein C. At dilutions above 1:12 a second wave of prothrombinase-activity is observed
analysis
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design of an aptamer-based suspension array detection platform for the sensitive, specific and rapid detection of human alpha-thrombin as a model. Thrombin is first recognized by a 29-mer biotinylated thrombin-binding aptamer in solution. Then 15-mer TBA modified magnetic beads capture the former aptamer-thrombin to form an aptamer-thrombin-aptamer sandwich complex. The median fluorescence intensity obtained via suspension array technology is positively correlated with the thrombin concentration. The dynamic quantitative working range of the aptamer-based suspension array is 18.37-554.31 nM, and the coefficients of determination R2 are greater than 0.9975. The lowest detection limit of thrombin is 5.4 nM. The method is highly specific for thrombin without being affected by other analogs and interfering proteins. The recoveries of thrombin spiked in diluted human serum are in the range 82.6-114.2%
biotechnology
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fibrin is a biopolymer that has been used in a variety of biomaterial, cell delivery and tissue engineering applications, the enzyme thrombin catalyzes the formation of fibrin microfibrils, which form a three-dimensional mesh in which cells can be directly embedded at the time of gel formation, method development, overview
biotechnology
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usage of human thrombin in a fibrin glue, method development, thrombin initiates clotting and cross-linking of fibrin from cryoprecipitate to produce an entirely autologous fibrin glue, overview
medicine
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the enzyme can be engineered to function in vivo as a potent anticoagulant that may possess a superior therapeutic profile with reduced potential for bleeding complications
medicine
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enzyme inhibitors are used in therapy and prevention of venous and arterial thrombosis, inhibition mode, efficiency and safety, overview
medicine
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enzyme is a target for development of inhibitors in antithrombotic therapy
medicine
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enzyme activation of factor VIII mutant R372H, occuring in patients with hemophilia A, is about 80fold decreased, resulting in generation of about 6.1 nM factor X4 per min compared to 13 nM for wild-type
medicine
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exposure to thrombin induces an increase in cytosolic calcium in both anterior and equatorial lens cells. Repeated exposure produces a significant increase in cell coverage in the capsular bag model and increased thymidine incorporation into FHL124 cells. In FHL124 cells, exposure to thrombin induces biphasic increases in the phosphorylation of p42/p44
medicine
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mechanism of high affinity fibrinogen binding and cleavage in Staphylococcus aureus mediated endocarditis
medicine
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affinity probe capillary electrophoresis/laser-induced fluorescence polarization assay for detection of human thrombin using a specific aptamer as probe. Monovalent and bivalent cations promoting the formation of a stable G quadruplex conformation in the aptamer may enhance the binding of the aptamer and thrombin, while cations like K+ and Mg2+ cannot stabilize the affinity complex. Without the use of typical cations, a highly sensitive assay of human thrombin was developed with the corresponding detection limits of 4.38×10?19 and 2.94×10?19 mol in mass for standard solution and human serum, respectively
medicine
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beta2-glycoprotein I may regulate thrombin inactivation by heparin cofactor II. The presence of anti-beta2-glycoprotein I antibodies potentiates the protective effect of beta2-glycoprotein I on thrombin and may explain the prothrombic tendency in patients with antiphospholipid syndrome
medicine
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comparison of anticoagulation response to thrombin inhibitors ximelagatran and warfarin in rats on a normal diet to those on a vitamin K deficient diet. Ximelagatran and warfarin increase prothrombin time, activated partial thromboplastin time and ecarin clotting time in rats on normal diet. Vitamin K deficient diet alone causes modest increases in prothrombin time, activated partial thromboplastin time and ecarin clotting time. The anticoagulant activity of both ximelagatran and warfarin is significantly greater in rats on vitamin K deficient diet compared to those on normal diet. Thrombin activity is reduced by both ximelagatran and warfarin to 58% and 44%, respectively, in rats on normal diet. Thrombin activity is virtually abolished by both drugs in rats on vitamin K deficient diet
medicine
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comparison of thrombin inhibitors dabigatran and enoxaparin in unilateral total knee arthroplasty patients after surgery. Dabigatran shows inferior efficacy to enoxaparin. Bleeding rates are similar, and no drug-related hepatic illness has been recognized
medicine
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comparison of thrombin inhibitors lepirudin and argatroban for treatment of heparin-induced thrombocytopenia. Adult subjects with a positive anti-heparin platelet factor 4 antibody test and more than 50% decrease in platelet count during the first 30 days of admission over a period of 2 years were included in the study. Subjects treated with a thrombin inhibitor are more likely to experience platelet count recovery, with 87.5% for the lepirudin group and 82.4% for the argatroban group, compared to those who do not receive antithrombin therapy. The thrombosis rate for subjects who do not receive antithrombin therapy after the diagnosis of heparin-induced thrombocytopenia is 26.8%, compared to 8.3% for the lepirudin group and 5.9% for the argatroban group
medicine
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development of a biosensor for thrombin detection using surface-enhanced Raman spectroscopy. The method utilizes the electrostatic interaction between capture thrombin aptamer and probe crystal violet molecules. Procedure shows a highly specific selectivity and a linear detection of thrombin in the range from 0.1 nM to 10 nM with a detection limit of about 20 pM and realizes the thrombin detection in human blood serum solution directly
medicine
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development of a modified electrochemical sandwich model for target protein detection using differential pulse voltammetry. With model target analyte thrombin, the sensor shows a linear response for thrombin in the range 1-60 nM with a detection limit of 0.5 nM
medicine
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development of an aptamer-based surface enhanced resonance Raman scattering sensor with high sensitivity, specificity, and stability for the detection of human alpha-thrombin. The sensor displays a limit of detection of 100 pM by monitoring the signal change upon the single-step of thrombin binding to immobilized thrombin binding aptamer and specifically discriminates thrombin from other proteins. The sensor can detect 1 nM thrombin in the presence of complex biofluids, such as 10% fetal calf serum, and is sufficiently robust for clinical diagnostic applications
medicine
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examination of the effect of thrombin on tumor cell cycle activation and spontaneous growth in synchronized serum-starved tumor cell lines and a model of spontaneous prostate cancer development in TRAMP mice expressing the SV40 Large T Antigen under the control of the prostate-specific probasin promoter, leading to the spontaneous development of prostate cancer and metastasis. Prostate LNCaP cells arrested in G0 and treated with thrombin or serum reveal a 48- and 29-fold increase in S phase cells, respectively, at 8 hours. Addition of thrombin, PAR-1 agonist TFLLRN, or serum down-regulates the inhibitory cell cycle regulator p27Kip1 with concomitant induction of Skp2, cyclin D1, and cyclin A with similar kinetics. LNCaP p27Kip1-transfected cells or Skp2 knockdown cells are refractory to thrombin-induced cell cycle activation. Repetitive thrombin injection enhances prostate tumor volume 6- to 8-fold. Repetitive hirudin injection, a specific potent antithrombin, decreases tumor volume 13- to 24fold
medicine
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exogenous oxidative stress, thrombin activation, progression of ageing and type 2 diabetes lead to protein carbonyls formation in platelets, and this modification can be attenuated by antioxidant enzymes
medicine
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exogenous oxidative stress, thrombin activation, progression of ageing and type 2 diabetes lead to protein carbonyls formation in platelets, and this modification can be attenuated by antioxidant enzymes
medicine
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exogenous oxidative stress, thrombin activation, progression of ageing and type 2 diabetes lead to protein carbonyls formation in platelets, and this modification can be attenuated by antioxidant enzymes
medicine
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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
medicine
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in patients with acute ST-segment elevation myocardial infarction who have received tenecteplase together with aspirin and heparin, thrombin-antithrombin complexes correlate with tissue factor activity associated with microparticles, and correlates with soluble platelet glycoprotein. Fibrinolysis failure in acute ST-segment elevation myocardial infarction is characterized by a higher procoagulant state associated with tissue factor activity associated with microparticles and lower plasmin generation
medicine
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in patients with first spontaneous venous thromboembolism, high endogenous thrombin potential confers an 1.6fold increased risk of recurrence, and risk of recurrence is 2.8fold higher among patients with both high endogenous thrombin potential and high fibrin D-dimer
medicine
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in patients with rheumatoid arthritis, citrullinated fibrin and fibrinogen are present in the synovium. Citrullinated fibrinogen is not a substrate for thrombin and may be associated with the pathophysiology of rheumatoid arthritis
medicine
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placentas from pregnancies complicated by preterm preeclampsia have a significantly higher frequency of strong receptor PAR-1 expression than placentas from women with spontaneous pre-term labour. Role for PAR-1 as a mediator of the effect of thrombin on coagulation and inflammation in preeclampsia. The effects of thrombin in preeclampsia are due to increased thrombin generation and higher expression of PAR-1
medicine
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rabbits receiving infusions with recombinant hirudin containing the RGD motif, which competitively inhibits the binding of fibrinogen to GP IIb/IIIa on platelets, have prolonged thrombin time, prothrombin time. and activated partial thromboplastin time which are similar to that of wild-type hirudin. In addition, recombinant RGD-hirudin is capable of inhibiting platelet aggregation and is two to three times more effective than wild-type hirudin in preventing thrombosis
medicine
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thrombin augments the contractility of uterine smooth muscle cell and immortalized myometrial smooth muscle cell collagen gels. The effect is inhibited by thrombin inhibitor hirudin. Thrombin-induced collagen contractility results in activation of thrombin receptor F2R
medicine
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thrombin inhibition by argatroban improves neurological outcomes and provides neuroprotection against acute events after subarachnoid hemorrhage such as blood-brain barrier disruption, brain edema, and cell death
medicine
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treatment of adults with one or more mild or moderate bleeding sites not manageable by conventional modalities during elective cardiovascular, neurologic, or general surgey procedures with human or bovine thrombin, applied topically with an absorbable gelatin sponge. The proportions of patients achieving hemostasis within 10 min, 6 min or 3 min were equivalent for human and bovine thrombin.12.7% of patients who received bovine thrombin demonstrated seroconversion compared with 3.3% of the patients who received human thrombin
medicine
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treatment of adults with one or more mild or moderate bleeding sites not manageable by conventional modalities during elective cardiovascular, neurologic, or general surgey procedures with human or bovine thrombin, applied topically with an absorbable gelatin sponge. The proportions of patients achieving hemostasis within 10 min, 6 min or 3 min were equivalent for human and bovine thrombin.12.7% of patients who received bovine thrombin demonstrated seroconversion compared with 3.3% of the patients who received human thrombin. None of the patients in the human thrombin group developed seroconversion for anti-human thrombin or anti-human factor V/Va antibodies
medicine
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treatment of iatrogenic pseudoaneurisms of the trunk by injection of 765 IU thrombin. Both percutaneous and endoluminal techniques are technically feasible and safe but the questioning of dosage and long-term results need further experiences
medicine
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treatment of pigs that underwent mid-left anterior descending coronary artery occlusion followed by reperfusion with saline vehicle or thrombin fragment TP508, i.e. chrysalin as a bolus into the ischemic period followed by continuous intravenous infusion. Endothelium-dependent coronary microvascular relaxation is greater in the TP508 group and associated with higher endothelial nitric oxide synthase phosphorylation. Both infarct size and TUNEL staining is decreased in the TP508 group compared with the saline control group. ession of cell survival proteins B-cell lymphoma and heat shock protein-73 is higher in the TB508 group. Expression of cell death-signaling proteins polyadenosine-diphosphate-ribose polymerase, cleaved polyadenosine-diphosphate-ribose polymerase, and B-cell lymphoma2/adenovirus E1B 19 kDa-interacting protein is significantly higher in the TB508 group in the ischemic territory
medicine
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when endothelial protein C receptor is ligated by protein C, the cleavage of receptor PAR-1 by thrombin initiates antiinflammatory responses, thus leading to activation of Rac I and inhibition of RhoA and nuclear factor kappaB signaling cascades
medicine
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thrombin activation is not related to the measured thrombus surface area or thrombus volume in patients with abdominal aortic aneurysms
medicine
because of the essential role of thrombin in the coagulation cascade, achieving the ability to specifically modulate thrombin activity represents a major goal in the development of anticoagulant strategies. Thrombin-binding aptamer (TBA), is a single-stranded 15-mer DNA with the sequence (5'-GGT TGG TGT GGT TGG-3') that binds thrombin with high specificity and affinity. TBA specifically inhibits clot-bound thrombin and reduces arterial thrombus formation. Native TBA consisting of only natural bases is susceptible to nuclease digestion and has a very short half-life in vivo of 108/s. Its binding affinity and selectivity need to be optimized. These optimization efforts are of critical importance in both diagnostic and therapeutic applications. Chemical modification of the DNA aptamer can be used to significantly improve its binding affinity
medicine
fibrinogenolytic properties make the enzyme applicable for biochemical research and drug development on thrombolytic therapy
synthesis
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production of recombinant human prethrombin-2 in mouse myeloma cells, activation by recombinant ecarin and purification by affinity chromatography. Yield is about 70%, product is indistinguishable from plasma-derived enzyme
synthesis
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preparation of thrombin from human plasma. Isolation of prothrombin is followed by activation to thrombin and further purification, process is suitable for large-scale production with a high degree of virus safety
synthesis
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use of thrombin as enhancer in polymerase chain reaction. Presence of bovine thrombin is exceptionally effective at preventing the formation of primer dimers and enhancing the formation of the desired polymerase chain reaction products. The PCR enhancement effects of thrombin apply to low-copy synthetic single-stranded DNAs, synthetic ssDNA pools, human genomic DNA, or hepatitis B virus genomic DNA. Thrombin is also able to effectively relieve PCR inhibition by nanomaterial inhibitors such as gold nanoparticles and graphene oxide. Compared with bovine serum albumin, thrombin is more effective and requires concentrations 18-178 times less than that of serum albumin to achieve a similar level of PCR enhancement
