Thrombomodulin
Thrombomodulin | ||
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Properties of human protein | ||
Mass / length primary structure | 557 amino acids | |
Secondary to quaternary structure | single pass type 1 membrane protein | |
Identifier | ||
Gene names | THBD ; TM; CD141; THRM | |
External IDs | ||
Occurrence | ||
Homology family | TH | |
Parent taxon | Higher mammals |
Thrombomodulin (THBD) is a protein that acts as a transmembrane receptor for thrombin in endothelial cells , and a thousandfold the ability of thrombin to activate protein C. It thus plays a key role in inhibiting blood clotting (anticoagulation). A lack of thrombomodulin due to mutations in the THBD gene can lead to thrombophilia and a tendency to infarct .
The ligand thrombin acts as a coagulation factor in hemostasis for blood clotting. However, the blood should only clot where the injury is. And if it has coagulated, it should only be released again when it is healed. Thrombomodulin is the binding site for thrombin in the blood vessel , which is not damaged. From here on, the process continues in two ways:
On the one hand, thrombin is inactivated by the binding, but is still able to activate the protein C / protein S complex, which inactivates the coagulation factors FV and FVIII . These factors can therefore no longer trigger blood clotting.
On the other hand, by binding thrombin, thrombomodulin activates TAFI (thrombin activatable fibrinolysis inhibitor = "thrombin-activatable inhibitor of fibrinolysis "). This ensures the inhibition of coagulation dissolution. The plug that has already formed is not released again as long as the coagulation is still running.
Individual evidence
- ↑ Thrombomodulin. In: Online Mendelian Inheritance in Man . (English).