By John W. Fenton II (auth.), Barry W. Festoff M.D., Daniel Hantaï M.D., Ph.D. (eds.)
Read Online or Download Serine Proteases and Their Serpin Inhibitors in the Nervous System: Regulation in Development and in Degenerative and Malignant Disease PDF
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Extra resources for Serine Proteases and Their Serpin Inhibitors in the Nervous System: Regulation in Development and in Degenerative and Malignant Disease
Plasminogen Activator Deficiency and Thrombosis. Impairment of fibrinolysis due to deficient synthesis and/or release of t-PA from the vessel wall or to increased levels of PAI-1 is associated with a tendency to thrombosis. Isacson & Nilsson101 found a defective release of t-PA from the vessel wall during venous occlusion and/or a decreased t-PA content in walls of superficial veins in about 70% of a large series of patients with idiopathic recurrent venous thrombosis. This association of recurrent venous thrombosis with a defect in the fibrinolytic system is more frequent than with any other known disturbance of hemostasis.
Alph~-antiplasmin is a single-chain glycoprotein with a molecular weight of 70,000 consisting of 452 amino acids. 39 Q2-Antiplasmin forms a 1:1 stoichiometric inactive complex with plasmin. This occurs in two successive reactions: a fast reversible second-order reaction followed by a slower irreversible first-order transition. The model can be represented by: P+A kl o(~ k-l PA k2 ~ PA' in which P is plasmin, A is Q2-antiplasmin, PA a reversible inactive complex and PA' an irreversible inactive complex.
Upon addition of plasminogen, cell bound plasmin as well as cell bound twochain uPA is formed. 54 The plasminogen activation occurs at the cell surface and is decreased by preincubation with diisopropyl fluorophosphate-inhibited uPA (DFPuPA), indicating that a large part, if not all, of the cell surface plasminogen activation is catalyzed by receptor-bound uPA. Likewise the formation of two-chain uPA is inhibited by low concentrations of tranexamic acid, indicating that it is catalyzed by surface bound plasmin.