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FXII deficiency impairs thrombosis in animal models without inducing abnormal excessive bleeding. Recent work has established the FXIIa-driven contact system as promising target for anticoagulant and anti-inflammatory drugs. This review focuses on the biochemistry of the contact system, its regulation by endogenous and exogenous inhibitors, and roles in disease states
Results demonstrated that the composition of the solution and the surface properties of the material all contribute to the observation of contact activation, and the activation of FXII is not specific to anionic surfaces as has been long believed.
Report an independent association between FXII levels and the risk of hemorrhagic stroke in Swedish population.
analysis of how FXII reacts to surface materials, which can be applied to the activities of FXII in its natural environment [review]
beta-amyloid interacts with fibrinogen and factor XII. These interactions can lead to increased clotting, abnormal clot (show TXNDC17 Proteins) formation, persistent fibrin deposition, and generation of proinflammatory molecules.
Abeta (show APP Proteins) activates FXII, resulting in FXI (show F11 Proteins) activation and thrombin (show F2 Proteins) generation in human plasma, thereby establishing Abeta (show APP Proteins) as a possible driver of prothrombotic states
results support a model for induction of contact activation in which activity intrinsic to single-chain FXII initiates alphaFXIIa and alpha-kallikrein (show KLK4 Proteins) formation on a surface. alphaFXIIa, with support from alpha-kallikrein (show KLK4 Proteins), subsequently accelerates contact activation and is responsible for the full procoagulant activity of FXII.
The XPNPEP2 c-2399A and the ACE insertion/deletion polymorphisms analyzed in a population of patients with hereditary angioedema with F12 mutation were not a major determinant of disease expression.
in the presence of platelet polyphosphate and the downstream substrate fibrin, alphaFXIIa is a highly efficient and favorable plasminogen (show PLG Proteins) activator.
inhibition of FXI (show F11 Proteins) and FXII distinctly alter the biophysical properties of fibrin.
FXII plays an important role in atherosclerotic lesion formation by functioning as a strong inducer of pro-inflammatory cytokines in antigen-presenting cells.
Genetic deficiency of factor XII diminished brain injury-induced bradykinin release and minimized brain lesion size.
FXI (show F11 Proteins) attenuates part of the allergic response to repeated administration of house dust mite in the airways by a mechanism that is independent of activation via FXII
onset and severity of the thrombotic phenotype are dependent on the presence of platelets but not circulating neutrophils. Unexpectedly, FXII has a protective effect.
Wild type mice developed carotid artery occlusion when the vessel was exposed to a 3.5% solution of ferric chloride (FeCl3). FXII-deficient mice were resistant to occlusion at 5% FeCl3 and partially resistant at 10% FeCl3.
the results of this study characterize the mechanism of HAEIII and establish FXII inhibition as a potential therapeutic strategy to interfere with excessive vascular leakage in HAEIII
Inhibiting factor XIIa with rHA-Infestin-4 may present a safe and effective treatment to decrease the morbidity of silent brain ischemia.
PKK (show RIPK4 Proteins) or fXII deficiency reduced thrombus formation in both arterial and venous thrombosis models, without an apparent effect on hemostasis.
fXI (show F11 Proteins) and fXII contribute to thrombus formation even when factor VIIa/tissue factor (show F3 Proteins) initiates thrombosis.
F12 KNOCKOUT MICE, generated to elucidate the biological role(s) of FXII, had a markedly prolonged APTT. Deficiency of murine FXII does not cause thrombophilia or impaired fibrinolysis or affect hemostasis.
This gene encodes coagulation factor XII which circulates in blood as a zymogen. This single chain zymogen is converted to a two-chain serine protease with an heavy chain (alpha-factor XIIa) and a light chain. The heavy chain contains two fibronectin-type domains, two epidermal growth factor (EGF)-like domains, a kringle domain and a proline-rich domain, whereas the light chain contains only a catalytic domain. On activation, further cleavages takes place in the heavy chain, resulting in the production of beta-factor XIIa light chain and the alpha-factor XIIa light chain becomes beta-factor XIIa heavy chain. Prekallikrein is cleaved by factor XII to form kallikrein, which then cleaves factor XII first to alpha-factor XIIa and then to beta-factor XIIa. The active factor XIIa participates in the initiation of blood coagulation, fibrinolysis, and the generation of bradykinin and angiotensin. It activates coagulation factors VII and XI. Defects in this gene do not cause any clinical symptoms and the sole effect is that whole-blood clotting time is prolonged.
, beta-factor XIIa part 1
, beta-factor XIIa part 2
, coagulation factor XII
, coagulation factor XIIa heavy chain
, coagulation factor XIIa light chain
, factor XII
, hageman factor