- thrombin is a vital serine protease enzyme that plays a key role in the coagulation cascade by converting fibrinogen into fibrin, which forms the structural mesh of a blood clot. it is generated from its inactive precursor prothrombin through the action of factor xa in the presence of calcium ions, phospholipids, and factor v. thrombin also activates other coagulation factors and contributes to platelet activation and wound healing.
chemical properties
- molecular weight: ~37 kDa
- structure: consists of two peptide chains (a and b) linked by disulfide bonds
- enzyme class: serine protease (EC 3.4.21.5)
- activation: formed from prothrombin cleavage by prothrombinase complex
usefulness in medicine
- thrombin is central to the formation of stable blood clots and is essential for controlling bleeding.
- topical thrombin is used as a hemostatic agent during surgery to control minor bleeding.
- thrombin is a key target for anticoagulant drugs (e.g., dabigatran) used to prevent or treat thrombosis, stroke, or atrial fibrillation.
- abnormal thrombin activity is associated with both excessive clotting and bleeding disorders.
- it also influences inflammation and tissue repair through signaling pathways beyond clot formation.
antibacterial and antimicrobial activity
- thrombin indirectly supports antimicrobial defense by helping form clots that trap pathogens at injury sites and reduce systemic spread.
- fibrin generated by thrombin serves as a physical barrier that aids immune cells in localizing and neutralizing invaders.
- research highlights:
- bacteria: