3.4.21.69: Protein C (activated)
This is an abbreviated version!
For detailed information about Protein C (activated), go to the full flat file.
Word Map on EC 3.4.21.69
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3.4.21.69
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thrombosis
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venous
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leiden
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sepsis
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endothelial
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antithrombin
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thromboembolism
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thrombophilia
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clot
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thrombomodulin
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platelet
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procoagulant
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heparin
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arterial
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vein
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bleeding
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plasminogen
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hypercoagulable
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thromboplastin
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lupus
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fibrinogen
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fibrinolysis
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hemostatic
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viiia
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epcr
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intravascular
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contraceptive
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antiphospholipid
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antithrombotic
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prothrombotic
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fibrin
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k-dependent
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anticardiolipin
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d-dimers
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coagulopathy
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embolism
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prothrombinase
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amidolytic
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thrombin-antithrombin
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haemostasis
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par1
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profibrinolytic
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pharmacology
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goal-directed
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diagnostics
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drug development
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gamma-carboxyglutamic
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deep-vein
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time-based
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tafi
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hypofibrinolysis
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thromboprophylaxis
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medicine
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protac
- 3.4.21.69
- thrombosis
- venous
- leiden
- sepsis
- endothelial
- antithrombin
- thromboembolism
- thrombophilia
- clot
- thrombomodulin
- platelet
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procoagulant
- heparin
- arterial
- vein
-
bleeding
- plasminogen
-
hypercoagulable
- thromboplastin
-
lupus
- fibrinogen
-
fibrinolysis
-
hemostatic
- viiia
- epcr
-
intravascular
-
contraceptive
-
antiphospholipid
-
antithrombotic
-
prothrombotic
- fibrin
-
k-dependent
-
anticardiolipin
-
d-dimers
- coagulopathy
- embolism
- prothrombinase
-
amidolytic
-
thrombin-antithrombin
-
haemostasis
- par1
-
profibrinolytic
- pharmacology
-
goal-directed
- diagnostics
- drug development
-
gamma-carboxyglutamic
-
deep-vein
-
time-based
- tafi
-
hypofibrinolysis
-
thromboprophylaxis
- medicine
- protac
Reaction
degradation of blood coagulation factors Va and VIIIa =
Synonyms
Activated blood coagulation factor XIV, Activated protein C, anticoagulant activated protein C, anticoagulant protein C/protein S system, anticoagulant serine protease-activated protein C, anticoagulant-activated protein C, APC, Autoprothrombin II-A, Autoprothrombin IIA, Blood coagulation factor XIV, Blood-coagulation factor XIV, activated, Blood-coagulation factor XIVa, ghrelin endopeptidase, GSAPC, hAPC, PROC, Protein Ca, rhAPC
ECTree
3.4.21.69 Protein C (activated)Advanced search results
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results (Activating Compound
Activating Compound on EC 3.4.21.69 - Protein C (activated)
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ACTIVATING COMPOUND 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
cholesterol
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in phosphatidylcholine/phosphatidylserine vesicles, cholesterol enhances Factor Va inactivation and the rate of cleavage by enzyme both at R506 and R306
endothelial cell protein C receptor
activation of protein C is potentiated by the presence of the endothelial cell protein C receptor (EPCR), which binds protein C with high affinity and increases the rate of protein C activation by about 20fold in vivo
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factor Xa
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stimulates factor Va cleavage at Arg306, but inhibits the cleavage at Arg506 20fold, overview, factor Xa and protein S interact with distinct sites on factor Va
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glycosaminoglycan
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enhances activity with factor V but not with factor Va as substrate
phosphatidylcholine
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as phospholipid vesicles with 80% phosphatidylcholine and 20% phosphatidylserine, specific binding to the enzyme of anionic phospholipid vesicles passed over the protein C surface, defective phospholipid binding of mutant variants also resulted in severely impaired anticoagulant activity in protein C-deficient plasma
phosphatidylserine
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as phospholipid vesicles with 80% phosphatidylcholine and 20% phosphatidylserine, specific binding to the enzyme of anionic phospholipid vesicles passed over the protein C surface, defective phospholipid binding of mutant variants also resulted in severely impaired anticoagulant activity in protein C-deficient plasma
polysulfated dermatan sulfate
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more active than dermatan sulfate-derived oligosaccharide on basis of comparable molecular weight. Most active polysulfated dermatan sulfate has a molecular weight of 2749 and increases enzyme activity by about 230%
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dermatan sulfate
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and oligosaccharide derivatives, all enhance enzyme activity. Most active dermatan sulfate-derived oligosaccharide increases enzyme activity by about 80%
Phospholipid
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accelerates cleavages at Arg506, Arg679 and Arg306 to a different extent
Phospholipid
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vesicles of 20% phosphatidylserine, 40% phosphatidylcholine, and 40% phosphatidylethanolamine
ProTac
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a protein C-activating agent isolated from snake venom, administration to mice enhances the production of octanoyl ghrelin(1-15) in circulation
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protein S
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the cofactor is active as free protein and in complex with C4b binding protein, the latter shows a less potent effect, activation up to 10fold, but the complex inhibits proteolysis at Arg506 by 3-4fold, overview
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protein S
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the cofactor function of protein S is weak in purified systems, only enhancing the rate of APC inactivation of factor Va twofold as compared with the inactivation of the cofactor by APC alone
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additional information
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the antiapoptotic effect of activated protein C requires its serine protease domain and is dependent on the endothelial cell protein C receptor and protease-activated receptor-1
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additional information
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activated protein C-protein C inhibitor complex is significantly higher in all abdominal aortic aneurysm cohorts compared with the control group
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additional information
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concentration of the APC-protein C inhibitor complex is increased in hypercoagulable states and is therefore a sensitive indicator of the degree of activation of blood coagulation
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additional information
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p38 MAPK activation is required for recombinant activated protein C-mediated up-regulation of interleukin-10. Endothelial protein C receptor and protease-activated receptor-1 are required for the upregulation of interleukin-10 by recombinant activated protein C, whereas JRK 1495, JRK 1535, or ATAP-2 have no effect
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additional information
the physiologic mechanism for protein C activation involves proteolysis at Arg169 in EPCR-bound protein C by thrombomodulin-bound thrombin
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additional information
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the physiologic mechanism for protein C activation involves proteolysis at Arg169 in EPCR-bound protein C by thrombomodulin-bound thrombin
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additional information
the physiologic mechanism for protein C activation involves proteolysis at Arg169 in EPCR-bound protein C by thrombomodulin-bound thrombin
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additional information
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the physiologic mechanism for protein C activation involves proteolysis at Arg169 in EPCR-bound protein C by thrombomodulin-bound thrombin
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