Tissue factor (TF) is the cell-surface transmembrane receptor that initiates both the extrinsic and intrinsic blood coagulation cascades. The abilities of TF to associate with Factor VIIa and Factor X in a ternary complex and to enable proteolytic activation of Factor X by Factor VIIa reside in the extracellular domain of TF. We describe the expression of the surface domain of TF (truncated TF,...

The effects of factor IX concentrate therapy on hemostasis in hemophilia patients were studied by means of the radiometric factor IXa assay, the coupled amidolytic assay for factor VIIa, and coagulant assays for factors II, IX, and X, and antithrombin III. Both activated and unactivated concentrates contained factors VIIa and IXa, with the highest levels in the activated concentrates. Factors V...

A new assay for the activation of bovine coagulation Factor X by two-chain Factor VII (cu-VIIa) is described. The assay measures the release of the radiolabeled activation peptide which is soluble in 5% trichloroacetic acid. The rate of release is shown to be a linear function of a-VIIa concentration in a system saturated with tissue factor. It could therefore be used to derive kinetic paramete...

In the present study we demonstrate that human monocytes can be induced by the model stimulus, lipopolysaccharide (LPS), to produce and assemble on their surface functional Factor VII/VIIa. This protease was not induced in relatively purified monocytes alone following exposure to LPS; but was induced in the presence of Leu-3a positive helper/inducer T cells. The Factor VII/VIIa protease activit...

BACKGROUND AND PURPOSE Recombinant Factor VIIa decreases hematoma growth after spontaneous intracerebral hemorrhage (ICH) and rapidly decreases international normalized ratios in patients on warfarin but is also associated with an increased risk for thromboembolic complications. In this study, we assessed the risk of thromboembolic events in patients receiving recombinant Factor VIIa after ICH ...

Tissue factor pathway inhibitors (TFPI and TFPI-2) are Kunitz domain-type serine protease inhibitors which inhibit factor VIIa/tissue factor (VIIa/TF) complexes in a factor Xa-dependent manner. The VIIa/TF and Xa inhibitory activity has been localized to the first two Kunitz domains, respectively. Unlike TFPI, TFPI-2 has been reported to exhibit significant Xa-independent VIIa/TF inhibitory act...

1. Astract 2. Introduction 3. TF and FVIIa 3.1. Purification, cloning and expression of TF 3.2. TF structure and function 3.3. Purification, cloning and expression of FVII 3.4. FVIIa structure and function 3.5. Interaction of FVIIa with TF 3.6. Binding of human FVIIa to sTF, lipidated TF and cell surface TF 3.6.1. FVIIa binding to sTF 3.6.2. FVIIa binding to lipidated TF and to cell surface TF ...