Factor VIII

Author: Gianpiero Pescarmona
Date: 09/02/2012



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It is released upon stimulation by vasopressin


[High concentration of coagulation factor VIII as a risk factor for thrombosis]. 2001

High factor VIII antigen levels increase the risk of venous thrombosis but are not associated with polymorphisms in the von Willebrand factor and factor VIII gene., 2001

In 301 thrombosis patients and 301 matched healthy controls, factor VIII antigen (VIII:Ag) levels > or = 150 IU/dl increased the thrombosis risk more than fivefold.

Cerebral venous thrombosis and plasma concentrations of factor VIII and von Willebrand factor: a case control study. 2007

Our study suggests that elevation of plasma factor VIII levels is the most common prothrombotic risk factor for CSVT. Elevation of VWF is also associated with an increased risk of CSVT but its effect seems to be partly mediated through FVIII.

von Willebrand factor and factor VIII as risk factors for arterial and venous thrombosis. 2005

Cortisol ?

The Hypercoagulable State in Cushing's Disease Is Associated with Increased Levels of Procoagulant Factors and Impaired Fibrinolysis, But Is Not Reversible after Short-Term Biochemical Remission Induced by Medical Therapy. 2012

Context:Cushing's disease (CD) is accompanied by an increased risk of venous thromboembolism. Surgery is the primary treatment of CD.Objective:The aim of the study was to compare hemostatic parameters between patients with CD and controls and to evaluate the effect of medical treatment of CD on hemostasis.Design and Setting:During 80 d, stepwise medical treatment was applied with the somatostatin analog pasireotide, the dopamine agonist cabergoline, and ketoconazole, which suppresses adrenocortical steroidogenesis, at four university medical centers in The Netherlands.Patients:Seventeen patients with de novo, residual, or recurrent CD were included.Main Outcome Measures:We measured urinary free cortisol and parameters of coagulation and fibrinolysis.Results:Patients with CD had significantly higher body mass index (P < 0.001), shortened activated partial thromboplastin time (P < 0.01), and higher levels of fibrinogen, Factor VIII, and protein S activity (P < 0.05) compared to healthy control subjects. In addition, fibrinolytic capacity was impaired in patients with CD as reflected by prolonged clot lysis time (P < 0.001) and higher levels of plasminogen activator inhibitor type 1, thrombin-activatable fibrinolysis inhibitor, and α2-antiplasmin (P < 0.01). There were no statistically significant differences in von Willebrand factor:antigen, antithrombin, and protein C activity. After 80 d, 15 of 17 patients had normalized urinary free cortisol excretion. Despite biochemical remission, only slight decreases in antithrombin (P < 0.01) and thrombin-activatable fibrinolysis inhibitor (P < 0.05) levels were observed. Other parameters of coagulation and fibrinolysis did not change significantly.Conclusions:The hypercoagulable state in patients with CD, which is explained by both increased production of procoagulant factors and impaired fibrinolysis, is not reversible upon short-term biochemical remission after successful medical therapy. This may have implications for the duration of anticoagulant prophylaxis in patients with (cured) CD.


Analysis of inflammation- and atherosclerosis-related gene polymorphisms in branch retinal vein occlusion. 2009

Furthermore, IL-6 promotes coagulation by upregulating the transcription of tissue factor, fibrinogen, and factor VIII.

Particulate Matter-Induced Lung Inflammation Increases Systemic Levels of PAI-1 and Activates Coagulation Through Distinct Mechanisms. 2011

We previously reported that PM-treated animals exhibited selective, IL-6 dependent increases in fibrinogen, FVIII and vWF .

IL6 Factor VIII




Hepatic low-density lipoprotein receptor-related protein deficiency in mice increases atherosclerosis independent of plasma cholesterol. 2004

Lower plasma cholesterol in MX1Cre(+)LRP-LDLRAPOE mice coincided with increased plasma lipoprotein lipase (71.2 +/- 7.5 vs 19.1 +/- 2.4 ng/ml, P =.002), coagulation factor VIII (4.4 +/- 1.1 vs 1.9 +/- 0.5 U/mL, P =.001), von Willebrand factor (2.8 +/- 0.6 vs 1.4 +/- 0.3 U/mL, P =.001), and tissue-type plasminogen activator (1.7 +/- 0.7 vs 0.9 +/- 0.5 ng/ml, P =.008) compared with controls.

[Blood coagulation in normotensives and hypertensives in relation to their body mass index]. 2002

Pearson correlation showed a significant (p < 0.001) positive relationship between PAI-1 and body mass index (BMI) (0.539), triglycerides (0.512), blood pressure (0.388 to 0.534), fibrinogen (0.404, and a negative one with HDL-cholesterol (0.625). BMI also correlated with fibrinogen (0.509; p < 0.001) and factor VIII (0.337; p < 0.01).


The Factor VIII acute phase response requires the participation of NFkappaB and C/EBP. 2000

In this study, we have demonstrated that the human Factor VIII promoter is activated in cultured hepatocytes exposed to bacterial lipopolysaccharide (LPS).

Acquired inhibitor to factor VIII in small cell lung cancer: a case report and review of the literature. 2012

Vasopressin Factor VIII
The effect of DDAVP on plasma levels of von Willebrand antigen II in normal individuals and patients with von Willebrand's disease. 1984

The infusion of 1-deamino-(8-D-arginine)-vasopressin (DDAVP) causes not only an elevation in factor VIII-related antigen (FVIIIR:Ag), but also a marked elevation of plasma von Willebrand antigen II (vWAgII). vWAgII reaches a peak concentration at 60 min and is elevated 3-8-fold over basal levels in normal individuals and individuals with type I, IIA, and IIB von Willebrand's disease.

2012-02-22T23:32:33 - carlotta alovisi

Vasopressin plays a role in factor VIII expression.


The VIII Factor (FVIII) plays an essential role over blood coagulation also as anti-hemophiliac (AHF). In human beings, VIII factor is codified by F8 gene on X chromosome.
Is produced by liver and endothelial cells.


In normal conditions circulating platelets don’t neither stick to the undamaged endothelium, neither gather together, while the exposition to sub endothelial matrix made by the endothelial damage, provokes their joining.
The plateletic activation process (that lies in morphological variations of platelet’s surface with exposition of fibrinogen’s joining sites) is originated by platelets’ contact with matrix collagen and allows platelet to gather together.
The aggregation of platelets is mediated by von Willebrand’s factor (vWF), a protein synthesized in endothelial cells and stocked into Weibel-Palade’s corps from which can be released as a response to stimulus of different agonists. vWF is stocked into platelets in alpha granules. As a consequence of the endothelial damage, endothelial cells release vWF factor that causes exposition of many different intrinsic sites for glicoproteins (GPlb) on the platelet’s membrane.
Until recently everyone thought that vWF owned both factor VIII coagulant activity and capacity to promote platelets’ joining to the damaged vasal tissue. We now know that vWF is responsible only for platelet’s adhesion while VIII factor has coagulant activity.
The formation of vWF/FVIII complex stabilizes factor VIII molecule in plasma and protects it from degradation.
Vasopressin is released as a consequence of small increases in sieric osmolality and of a bigger decline of extracellular flows, provoked by an endothelial damage and so by a blood spill from vases.
Vasopressin is bound to V2 extra kidney endothelial receptor in order to activate an adeniylyl ciclase system that stimulates intracellular protein kinase by stimulating factor VIII and vWF release.
Ormonal modifications, associated with stress (cortisol) or pregnancy (estrogens), estroprogestinic therapies, and a reaction to a severe stage or a inflammation, stimulate the increase of vWF synthesis, raising the vWF plasmatic level as well. Also high glucocorticoids levels activate endothelial production of vWF.
Other factors influence vWF levels such as age, gender, infectious diseases, autoimmune and malignant. It is well known that steroids can increase factor VIII and vWF levels and induce synthesis of bad molecular structures like the ones with high molecular weight and increased biological half-life. Those multimers are able to cause platelets aggregations in particular in high shear stress conditions. It is not clear how steroids can increase factor VIII and vWF levels, even if it is possible to presuppose an expantion in vWF synthesis from endothelial cells through the growth in vWF’s gene transcription in 21st band into 12th cromosome.

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