Tissue factor and factor VIIa – Hemostasis and beyond

Tissue factor and hemostasis.

Inhibitors of Factor VIIa/tissue factor.

The formation of the proteolytic complex composed of the serine protease Factor VIIa and the cell-associated glycoprotein tissue factor (FVIIa/TF) initiates a cascade of amplified zymogen activation reactions leading to thrombus formation. The critical role of the coagulation cascade in pathological thrombosis has been the basis for significant efforts to design selective inhibitors of the prot...

Binding of factor VIIa to tissue factor permits rapid antithrombin III/heparin inhibition of factor VIIa.

Because free factor VIIa is inactivated only very slowly by a plasma concentration of antithrombin III (AT III) even in the presence of heparin, it has been assumed that AT III plays no significant role in regulating the initiation of tissue factor-dependent blood coagulation. However, in the present study, we present evidence that factor VIIa bound to tissue factor, unlike free factor VIIa, is...

Tisssue factor and factor viia cross-species compatibility Tisssue factor and factor viia cross-species compatibility

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 ...

Structural biology of factor VIIa/tissue factor initiated coagulation.

Factor VII (FVII) consists of an N-terminal gamma-carboxyglutamic acid domain followed by two epidermal growth factor-like (EGF1 and EGF2) domains and the C-terminal protease domain. Activation of FVII results in a two-chain FVIIa molecule consisting of a light chain (Gla-EGF1-EGF2 domains) and a heavy chain (protease domain) held together by a single disulfide bond. During coagulation, the com...