Fibrinogen αC Domains Contain Cryptic Plasminogen and tPA Binding Sites
- 1 June 2001
- journal article
- review article
- Published by Wiley in Annals of the New York Academy of Sciences
- Vol. 936 (1) , 328-330
- https://doi.org/10.1111/j.1749-6632.2001.tb03518.x
Abstract
Surface plasmon resonance and ELISA experiments revealed that recombinant fibrinogen alpha C fragment (residues A alpha 221-610) corresponding to the alpha C domain binds tPA and plasminogen with high affinity. This binding was found to be Lys-dependent and occurred via independent binding sites. Study with truncated variants of the alpha C fragment located these sites in its COOH-terminal half. Binding of tPA and plasminogen to these sites stimulated activation of the latter whereas proteolytic degradation of the alpha C fragment reduced this effect substantially, suggesting the importance of the alpha C domains in regulation of fibrinolysis.Keywords
This publication has 4 references indexed in Scilit:
- Factor XIIIa Cross-Linking of the Marburg Fibrin: Formation of αm·γn-Heteromultimers and the α-Chain–Linked Albumin·γ Complex, and Disturbed Protofibril Assembly Resulting in Acquisition of Plasmin Resistance Relevant to ThrombophilaBlood, 1998
- Molecular basis for fibrinogen Dusart (A alpha 554 Arg-->Cys) and its association with abnormal fibrin polymerization and thrombophilia.Journal of Clinical Investigation, 1993
- Chapter 7 Fibrinogen, fibrin and factor XIIIPublished by Elsevier ,1986
- Dysfibrinogenemia (Fibrinogen Dusard) Associated with Impaired Fibrin-Enhanced Plasminogen ActivationThrombosis and Haemostasis, 1984