The cardiovascular risk factor plasminogen activator inhibitor type 1 (PAI 1) has been associated with abdominal obesity, hypertension, hypertriglyceridemia, hyperinsulinemia, glucose intolerance, and type II diabetes, conditions known to be linked with insulin resistance. Plasminogen activator inhibitor 1 (PAI 1) is a member of the serine protease inhibitor (serpin) superfamily and a central regulatory protein in the blood coagulation system. PAI-1 is unique among serpins in exhibiting distinct active and inactive (latent) conformations in vivo. Human PAI 1 is a single-chain glycoprotein with a molecular weight of 43kD. This inhibitor acts as “bait” for tissue-type and urokinase-type plasminogen activators (tPA and uPA) and protein C. Its rapid interaction with tPA may function as a major control point in the regulation of fibrinolysis. The highly mobile reactive-center loop (RCL) is thought to account for both the rapid inhibiton of plasminogen activators, and the rapid and spontaneous transition of the unstable, active form of PAI 1 into the stable, inactive conformation. The inactive form can be partially reactivated by denaturants such as urea, guanidine hydrochloride or SDS. High concentrations of PAI 1 have been associated with human thromboembolic disease. PAI 1 activity may limit the extent of tumor metastasis, since uPA activity is a major contributory factor promoting dissolution of tumor matrix and basement membrane.
Intended for research use only. Not for use in human, therapeutic, or diagnostic applications.