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Full-Text Articles in Medicine and Health Sciences
Evidence That Α2-Antiplasmin Becomes Covalently Ligated To Plasma Fibrinogen In The Circulation: A New Role For Plasma Factor Xiii In Fibrinolysis Regulation, Michael W. Mosesson, Kevin R. Siebenlist, Irene Hernandez, K. N. Lee, V. J. Christiansen, P. A. Mckee
Evidence That Α2-Antiplasmin Becomes Covalently Ligated To Plasma Fibrinogen In The Circulation: A New Role For Plasma Factor Xiii In Fibrinolysis Regulation, Michael W. Mosesson, Kevin R. Siebenlist, Irene Hernandez, K. N. Lee, V. J. Christiansen, P. A. Mckee
Biomedical Sciences Faculty Research and Publications
Background:
Plasma alpha2-antiplasmin (α2AP) is a rapid and effective inhibitor of the fibrinolytic enzyme plasmin. Congenital α2AP deficiency results in a severe hemorrhagic disorder due to accelerated fibrinolysis. It is well established that in the presence of thrombin-activated factor XIII (FXIIIa), α2AP becomes covalently ligated to the distal α chains of fibrin or fibrinogen at lysine 303 (two potential sites per molecule). Some time ago we showed that α2AP is covalently linked to plasma fibrinogen . That singular observation led to our hypothesis that native plasma factor XIII (FXIII), …