Plasminogen activator inhibitor-1

Plasminogen activator inhibitor-1 (PAI-1) is a protein that in humans is encoded by the SERPINE1 gene. It is a member of the serpin superfamily of proteins, which function as serine protease inhibitors. PAI-1 is the primary inhibitor of tissue plasminogen activator (tPA) and urokinase (uPA), the activators of plasminogen and hence fibrinolysis.

Function[edit | edit source]

PAI-1 inhibits the tissue plasminogen activator and urokinase, which are involved in fibrinolysis, the physiological process that degrades blood clots. The high concentration of PAI-1 is thought to contribute to thrombosis, as it can inhibit the breakdown of clots.

Clinical significance[edit | edit source]

Elevated levels of PAI-1 have been linked to an increased risk of thrombosis and a number of other diseases, including cardiovascular disease, stroke, and diabetes. It is also involved in cell adhesion and migration, which has implications for tumor growth and metastasis.

Genetics[edit | edit source]

The SERPINE1 gene encoding PAI-1 is located on chromosome 7 (7q21.3-q22). Several polymorphisms in this gene have been associated with variations in PAI-1 levels and activity.

Pharmacology[edit | edit source]

Several drugs have been developed to inhibit PAI-1, with the aim of preventing or treating thrombosis and other conditions associated with elevated PAI-1 levels. These include anisoylated plasminogen-streptokinase activator complex (APSAC), tissue-type plasminogen activator (tPA), and urokinase-type plasminogen activator (uPA).