Fibrinmonomer

Fibrinmonomer is a soluble protein fragment that plays a crucial role in blood coagulation. It is derived from fibrinogen, a larger protein synthesized in the liver and present in blood plasma. During the clotting process, the enzyme thrombin cleaves fibrinogen, releasing fibrinmonomer units. These fibrinmonomer molecules then spontaneously aggregate to form a mesh-like structure. This fibrin mesh traps blood cells and platelets, forming a stable clot that seals injured blood vessels and prevents excessive bleeding.

The polymerization of fibrinmonomer is a complex process that involves specific interactions between the released fragments. Initially, the aggregation forms soluble fibrin polymers. These polymers then undergo a process of stabilization, often through the action of another enzyme called factor XIII, which cross-links the fibrin strands. This cross-linking makes the clot more robust and resistant to mechanical stress. The concentration of fibrinogen and the activity of thrombin are critical factors in regulating the rate and extent of fibrinmonomer polymerization and, consequently, the efficiency of hemostasis. Disruptions in this process can lead to either excessive bleeding or the formation of unwanted blood clots within blood vessels.