New insights into the molecular mechanisms of the fibrinolytic system.
J Thromb Haemost
; 7(1): 4-13, 2009 Jan.
Article
in En
| MEDLINE
| ID: mdl-19017261
ABSTRACT
Fibrinolysis is regulated by specific molecular interactions between its main components. Activation of plasminogen by tissue-type plasminogen activator (t-PA) is enhanced in the presence of fibrin or at the endothelial cell surface. Urokinase-type plasminogen activator (u-PA) binds to a specific cellular u-PA receptor (u-PAR), resulting in enhanced activation of cell-bound plasminogen. Inhibition of fibrinolysis occurs at the level of plasminogen activation or at the level of plasmin. Assembly of fibrinolytic components at the surface of fibrin results in fibrin degradation. Assembly at the surface of cells provides a mechanism for generation of localized cell-associated proteolytic activity. This review includes novel proteins such a thrombin-activatable fibrinolysis inhibitor (TAFI) and discusses new insights into molecular mechanisms obtained from the rapidly growing knowledge of crystal structures of proteins.
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Blood Proteins
/
Fibrinolysis
Limits:
Humans
Language:
En
Journal:
J Thromb Haemost
Journal subject:
HEMATOLOGIA
Year:
2009
Document type:
Article
Affiliation country:
Países Bajos