3.4.21.38: coagulation factor XIIa
This is an abbreviated version!
For detailed information about coagulation factor XIIa, go to the full flat file.
Word Map on EC 3.4.21.38
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3.4.21.38
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kininogen
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clot
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platelet
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thrombin
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thrombosis
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plasminogen
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bradykinin
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anticoagulant
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bleeding
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thromboplastin
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fibrinolysis
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fibrinogen
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prothrombin
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hereditary
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heparin
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fibrin
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antithrombin
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plasmin
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kinin
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procoagulant
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angioedema
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hemostasis
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viii
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kallikrein-kinin
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amidolytic
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autoactivation
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zymogen
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willebrand
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kaolin
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thromboembolic
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antithrombotic
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c1-inhibitor
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fxia
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d-dimers
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c1-inh
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hypercoagulability
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antiphospholipid
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thrombin-antithrombin
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c1s
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fletcher
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2-antiplasmin
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fibrinopeptide
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euglobulins
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c1-esterase
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thrombophilia
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synthesis
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drug development
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medicine
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recalcification
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recalcified
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blood-contacting
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bradykinin-mediated
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icatibant
- 3.4.21.38
- kininogen
- clot
- platelet
- thrombin
- thrombosis
- plasminogen
- bradykinin
-
anticoagulant
-
bleeding
- thromboplastin
-
fibrinolysis
- fibrinogen
- prothrombin
- hereditary
- heparin
- fibrin
- antithrombin
- plasmin
- kinin
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procoagulant
- angioedema
-
hemostasis
- viii
-
kallikrein-kinin
-
amidolytic
-
autoactivation
- zymogen
- willebrand
- kaolin
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thromboembolic
-
antithrombotic
- c1-inhibitor
- fxia
-
d-dimers
-
c1-inh
- hypercoagulability
-
antiphospholipid
-
thrombin-antithrombin
- c1s
-
fletcher
-
2-antiplasmin
-
fibrinopeptide
-
euglobulins
- c1-esterase
- thrombophilia
- synthesis
- drug development
- medicine
-
recalcification
-
recalcified
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blood-contacting
-
bradykinin-mediated
- icatibant
Reaction
selective cleavage of Arg-/-Ile bonds in factor VII to form factor VIIa and factor XI to form factor XIa =
Synonyms
activated coagulation factor XII, activated factor XII, alpha-FXIIa, alphaFXIIa, beta-factor XIIa, beta-FXIIa, blood coagulation factor XII, blood-coagulation factor XII, activated beta, blood-coagulation factor XIIabeta, blood-coagulation factor XIIf, coagulation beta-factor XIIa, coagulation factor XII, coagulation factor XIIa, F12, factor XII, factor XII Osaka, factor XIIa, FXII, FXIIa, HAF, Hageman factor, Hageman factor beta-fragment, Hageman factor fragment HFf, Hagemann factor, kallikreinogen, activator, prealbumin activator, prekallikrein activator, single-chain FXII
ECTree
3.4.21.38 coagulation factor XIIaAdvanced search results
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results (Activating Compound
Activating Compound on EC 3.4.21.38 - coagulation factor XIIa
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ACTIVATING COMPOUND 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
ellagic acid
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activation of factor XII by negatively charged agents, e.g. ellagic acid, is not necessarily accompanied by molecular scission
streptokinase SK
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enzyme activity in plasma increases 2fold over 60 min in patients treated with fibrinolytic agents, tissue plasminogen activator t-PA or with streptokinase SK
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TGFbeta
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treatment of human lung fibroblasts with TGF-beta1 results in a time-dependent increase in FXII production, activation of p44/42, p38, JNK, and Akt, and phosphorylation and translocation into the nucleus of Smad3
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tissue plasminogen activator t-PA
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enzyme activity in plasma increases 2fold over 60 min in patients treated with fibrinolytic agents, tissue plasminogen activator t-PA or with streptokinase SK
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plasma kallikrein
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factor XII is activated by plasma kallikrein in the presence of kaolin and high molecular weight kininogen stimulates the activation 4fold to 5fold. Factor XII is also activated by plasma kallikrein in the presence of vesicles of acidic lipids, such as sulfatides, ganglioside, stearic acid, and cholesterol sulfate
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additional information
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factor XIIa undergoes large changes in secondary structures when exposed to low pH in the presence of dextran sulfate 500. The reaction of factor XII with dextran sulfate 500 at pH 5.3 results in loss of alpha-helical structure while at pH 8.3, in its formation. At pH 5.3 autoactivation is inhibitited. This may indicate that alpha-helical structure in factor XII plays an important role in the autoactivation mechanism
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additional information
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conformational change ion factor XII is a key event in the activation process of this molecule. This conformational change can be induced by binding of factor XII to a surface as well as by proteolytic cleavage. Monoclonal antibody F1 can also induce the conformational change, this antibody may provide a unique tool in studies of the activation of factor XII
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additional information
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a sulfated galactan with the repeated structure -4-alpha-D-Gal-p-1->3-beta-D-Gal-p-1-> from Botryocladia accidentalis induces factor XII activation, dextran sulfates with molecular size above 8 kDa also activate factor XII
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additional information
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extracellular RNA, but not DNA, augments (auto)activation of FXII and thereby acts as a potent trigger of coagulation in vivo
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additional information
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Factor XII autoactivation is also initiated by misfolded or amorphous protein aggregates of transthyretin, Bence-Jones protein, glycated albumin, glycated hemoglobin, or endostatin
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additional information
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platelet- and erythrocyte-derived microparticles initiate the formation of thrombin via the activation of factor XII
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additional information
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exposure of blood to foreign surfaces induces reciprocal conversion of factor XII to the active protease alpha-fXIIa. These so-called contact activation is initiated through activity intrinsic to single-chain factor XII. Pre-existing alpha-fXIIa is not required for induction of contact activation
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additional information
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the enzyme gets activated by contact when exposed to artificial surfaces and biological substances
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additional information
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the enzyme is activated when blood is exposed to negatively-charged foreign surfaces or molecules such as RNA, DNA, misfolded proteins, and polyphosphates
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additional information
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extracellular RNA, but not DNA, augments (auto)activation of FXII and thereby acts as a potent trigger of coagulation in vivo
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additional information
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as with heparin, sulfated galactan from Gelidium crinale does not activate factor XII, while the polysaccharide from Botryocladia accidentalis activates factor XII in high concentrations
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