Evidence that alpha2-antiplasmin becomes covalently ligated to plasma fibrinogen in the circulation: a new role for plasma factor XIII in fibrinolysis regulation.

@article{Mosesson2008EvidenceTA,
  title={Evidence that alpha2-antiplasmin becomes covalently ligated to plasma fibrinogen in the circulation: a new role for plasma factor XIII in fibrinolysis regulation.},
  author={Michael W. Mosesson and Kevin R. Siebenlist and Irene Crespo Hern{\'a}ndez and Kyung Nam Lee and Victoria J. Christiansen and Patrick A. McKee},
  journal={Journal of thrombosis and haemostasis : JTH},
  year={2008},
  volume={6 9},
  pages={1565-70}
}
BACKGROUND Plasma alpha2-antiplasmin (alpha2AP) is a rapid and effective inhibitor of the fibrinolytic enzyme plasmin. Congenital alpha2AP 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), alpha2AP becomes covalently ligated to the distal alpha chains of fibrin or fibrinogen at lysine 303 (two potential sites per molecule). Some time ago we showed that alpha2AP is… CONTINUE READING