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• W2020565669 abstract "H EMOSTASIS DEPENDS on several factors: platelets, coagulation factors, blood vessel endothelium, and fibrinolysis. The coagulation cascade represents the mechanism by which a stable fibrin clot is formed (Fig 1). Most of the coagulation factors are glycoproteins synthesized in the liver. The cascade is composed of intrinsic, extrinsic, and common pathways. Factor XII, high molecular weight kininogen, prekallikrein, and factor XI form the surface activation group. Disruption in the endothelial cell layer initiates the conversion of factor XII to factor XIIa. High molecular weight kininogen together with factor XIIa, cause transformation of prekallikrein to kallikrein and activation of factor XI to factor XIa. The end product of the intrinsic pathway is factor X conversion to Xa that is catalyzed by factor IXa and VIII. Factor X, which is the junction of both pathways, starts what is called the common pathway. Activation of factor X can be achieved via the intrinsic and extrinsic pathways. The extrinsic pathways refers to the location of these factors with regard to the vasculature. The extrinsic pathway is initiated with tissue thromboplastin (factor III) that transforms factor VII to VIIa. Factor VIIa and X then act as coinitiators with the help of platelets, phospholipids, and Ca ++, to generate Factor Xa. In the common pathway, factor Xa in combination with Ca ++, phospholipids and factor Va cleaves prothrombin to produce thrombin. Fibrin (the product of thrombin cleavage of fibrinogen) is then crosslinked to form a stable clot by factor XIIIa. Platelet function is one of the most important factors in hemostasis. The platelets that are free flowing in the blood vessels initially respond to damaged or injured vessel endothelium by adhesion. On contact, platelets release several factors that propogate further platelet activation and aggregation. Once the clot is formed, some natural fibrin breakdown occurs as part of the normal healing process. Fibrinolysis is initiated by plasminogen, which is a serine protease synthesized by the liver. The degradation ofplasminogen is caused by tissue plasminogen activator (t-PA) and factor XIIa to plasmin. Plasmin splits fibrin or fibrinogen to produce fibrin or fibrinogen split products (Fig 2). There is normal local fibrinolysis wherever normal hemostasis occurs. Fibrinolysis is one of the most important causes of bleeding after cardiopulmonary bypass (CPB). A number of pharmocological strategies exist to inhibit excessive fibrinolysis. Epsilon Amino-Caproic Acid (EACA) and tranexamic acid (TA) are two synthetic antifibrinolytics that bind to plasminogen and plasmin (Fig 2) and inhibit the effect of plasmin on fibrin. Aprotinin is a serine protease inhibitor, which is isolated from bovine lung. Aprotinin was isolated and its activity then defined both as a kallikrein and a trypsin inhibitor in the 1930s. I" @default.
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• W2020565669 title "Clinical evaluation of aprotinin" @default.
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