Binding of ATP to its receptors in the platelet surface activate cascade of reactions which end up by activation of the glycoprotein receptors on the platelet surface which mediate the aggregation of fibrin strands to platelet. Clopidogel inhibits the bin

Fibrin Degradation

Fibrinogen is activated into fibrin strands which cluster together to form stable net. Prothrombin is activated into thrombin which the formation of fibrin net. Plasminogen is activated into plasminogen which degrade the fibrin net.

Gp IIb-IIIa Inhibitors

Fibrinogen binds to GP IIb-IIIa receptors on the platelets surface and play important role in platelet aggregation. GP IIb-IIIa inhibitors inhibit the binding of fibrinogen to platelets and thus interfere with platelet aggregation.


Antithrombin bind to and inactivate coagulation factors II and X. This process is naturally slow. Heparin binds to antithrombin and enhance this process. Low molecule weight heparin inactivate only factor X. fondaparinux is the shortest molecule.


The inactive coagulation factors X, IX, VII and II is carboxylated to their active forms. Reduced vitamin K works as cofactor for this reaction. The oxidized vitamin K is returned back into its reduced form with help of NADPH. Warfarin inhibit the reduct