Abstract
Identification of the binding site for plasminogen kringle 5 in the ?-chain of fibrin(ogen) D-fragment
Highlights
Fibrin is the main component of blood clots, which are formed to stop and prevent blood loss after vessel damage
The interaction between plasminogen and tissue activator with polymeric fibrin localizes plasmin generation on the surface of the fibrin clot, and makes possible the selective fibrin hydrolysis and keeps plasmin protected from the plasma inhibitor, α-2-antiplasmin [1,2]
FCB-2 and thrombin-treated N-terminal disulfide knot of fibrin (t-NDSK) were obtained by cyanogen bromide cleavage of fibrin [22]
Summary
Fibrin is the main component of blood clots, which are formed to stop and prevent blood loss after vessel damage. Fibrin clot formation plays the primary role in the development of life-threatening thrombotic conditions and vascular pathologies, such as ischemic heart disease, atherosclerosis, myocardial infarction, stroke, etc. Investigation of the molecular mechanisms of protein interactions related to fibrin degradation has vital clinical implications. Proteolytic enzyme plasmin (EC 3.4.21.7) is the key fibrinolytic proteinase responsible for clot degradation in vivo. Plasmin is derived from circulating non-active zymogen plasminogen. The interaction between plasminogen and tissue activator with polymeric fibrin localizes plasmin generation on the surface of the fibrin clot, and makes possible the selective fibrin hydrolysis and keeps plasmin protected from the plasma inhibitor, α-2-antiplasmin [1,2]
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