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Increased production of prothrombin heightens the risk of blood clotting. Moreover, individuals who carry the mutation can pass it on to their offspring. [8] The mutation increases the risk of developing deep vein thrombosis, [9] which can cause pain and swelling, and sometimes post-thrombotic syndrome, ulcers, or pulmonary embolism. [10]
Hyperprothrombinemia is a state of high of prothrombin levels in the blood [1] which leads to hypercoagulability. An example of a genetic cause includes the mutation prothrombin G20210A. [2] Hyperprothrombinemia is a risk factor for venous thromboembolism. [2]
Recurrent miscarriage is an indication for thrombophilia screening, particularly antiphospholipid antibodies (anti-cardiolipin IgG and IgM, as well as lupus anticoagulant), factor V Leiden and prothrombin mutation, activated protein C resistance and a general assessment of coagulation through an investigation known as thromboelastography.
Prothrombin time (PT) and its derived measures of prothrombin ratio (PR) and INR are measures of the extrinsic pathway of coagulation. This test is also called "ProTime INR" and "INR PT". They are used to determine the clotting tendency of blood, in the measure of warfarin dosage, liver damage, and vitamin K status. [16]
Prothrombin fragment 1+2 (F1+2), also written as prothrombin fragment 1.2 (F1.2), is a polypeptide fragment of prothrombin (factor II) generated by the in vivo cleavage of prothrombin into thrombin (factor IIa) by the enzyme prothrombinase (a complex of factor Xa and factor Va). [1] [2] [3] It is released from the N-terminus of prothrombin. [3]
The fully assembled prothrombinase complex catalyzes the conversion of the zymogen prothrombin to the serine protease thrombin. Specifically, Factor Xa cleaves prothrombin in two locations, following Arg 271 and Arg 320 in human prothrombin. [1] Because there are two cleavage events, prothrombin activation can proceed by two pathways.
Protein C, also known as autoprothrombin IIA and blood coagulation factor XIV, [5]: 6822 [6] is a zymogen, that is, an inactive enzyme.The activated form plays an important role in regulating anticoagulation, inflammation, and cell death and maintaining the permeability of blood vessel walls in humans and other animals.
Anchoring of bovine prothrombin to the membrane through its Gla domain. [16] The molecular weight of prothrombin is approximately 72,000 Da. The catalytic domain is released from prothrombin fragment 1.2 to create the active enzyme thrombin, which has a molecular weight of 36,000 Da. Structurally, it is a member of the large PA clan of proteases.