Alpha-2-Antiplasmin

Alpha-2-Antiplasmin (also known as A2AP, SERPINF2, or plasmin inhibitor) is a serine protease inhibitor (serpin) responsible for inhibiting plasmin, an important enzyme that dissolves blood clots. It is a key protein in the regulation of blood coagulation and fibrinolysis.

Structure

Alpha-2-Antiplasmin is a single-chain glycoprotein with a molecular weight of approximately 70,000 Da. It is synthesized in the liver and consists of 464 amino acids, including an 18-amino acid signal peptide. The mature protein contains several glycosylation sites, which are important for its stability and activity.

Function

The primary function of Alpha-2-Antiplasmin is to inhibit plasmin, an enzyme that degrades fibrin, a protein that forms the framework of blood clots. By inhibiting plasmin, Alpha-2-Antiplasmin prevents the dissolution of fibrin and thus helps to maintain the integrity of blood clots.

Clinical significance

Deficiency of Alpha-2-Antiplasmin can lead to a bleeding disorder due to increased fibrinolysis, resulting in a condition known as Alpha-2-Antiplasmin deficiency. This condition is characterized by prolonged bleeding times, easy bruising, and an increased risk of hemorrhage. Conversely, an excess of Alpha-2-Antiplasmin can lead to thrombosis, as the normal process of clot dissolution is impaired.

See also

• Coagulation
• Fibrinolysis
• Plasmin
• Serine protease inhibitor

References

‎