factor va造句

• This complex is the pro-coagulant factor Va.
• Other proteases also activate Factor Va, but this cleavage is primarily carried out by thrombin.
• Factor Va is degraded by activated protein C, one of the principal physiological inhibitors of coagulation.
• Activated protein C ( with protein S as a cofactor ) degrades Factor Va and Factor VIIIa.
• The light and heavy chains of Factor Va are linked via a divalent metal ion, such as calcium.
• Prothrombinase assembly begins with the binding of Factor Xa and Factor Va to negatively charged phospholipids on plasma membranes.
• Factor Va also decreases the Km of the reaction by enhancing the binding of prothrombin to the prothrombinase complex.
• Activated protein C interacts tightly and exclusively with the light chain of Factor Va, and this interaction is calcium independent.
• First, activated protein C normally inactivates Factor Va by cleaving the cofactor at Arg 306, Arg 506, and Arg 679.
• Factor Va is inactivated following cleavage by activated protein C . Activated protein C cleaves Factor Va in both its light and heavy chains.
• Factor Va is inactivated following cleavage by activated protein C . Activated protein C cleaves Factor Va in both its light and heavy chains.
• Once bound to the plasma membrane, Factor Xa and Factor Va rapidly associate in a 1 : 1 stoichiometric ratio to form the prothrombinase complex.
• Activated Factor Xa and Factor Va bind to the plasma membranes of a variety of different cell types, including monocytes, platelets, and endothelial cells.
• Following cleavage, Factor Va contains a heavy chain, composed of the A1 and A2 domains and a light chain, consisting of the A3, C1, and C2 domains.
• Activated protein C resistance is the inability of protein C to cleave Factor Va and / or Factor VIIIa, which allows for longer duration of thrombin generation and may lead to a hypercoagulable state.
• In addition, reduced levels of protein S lead to a reduction in activity of protein C ( for which it is the co-factor ) and therefore reduced degradation of factor Va and factor VIIIa.
• Both Factor Xa and Factor Va associate with the membrane via their light chains, with Factor Xa binding via its Gla-domain in a calcium-dependent manner and Factor Va via its C2 and C1 domains.
• Both Factor Xa and Factor Va associate with the membrane via their light chains, with Factor Xa binding via its Gla-domain in a calcium-dependent manner and Factor Va via its C2 and C1 domains.
• Since protein C is involved in factor Va degradation Apo-H indirectly inhibits the degradation of factor Va . This inhibitory activity was diminished by adding phospholipids suggesting the Apo-H inhibition of protein C is phospholipid competitive.
• Since protein C is involved in factor Va degradation Apo-H indirectly inhibits the degradation of factor Va . This inhibitory activity was diminished by adding phospholipids suggesting the Apo-H inhibition of protein C is phospholipid competitive.