[Importance of the structure of the clot in thrombolysis].

Abstract

Activation of plasminogen by tissue-type plasminogen activator (tpA) is potentiated by fibrin. We have demonstrated the role of fibrin polymerization in the potentiating effect of tpA-induced fibrinolysis. Therefore a pathogenic mechanism of thrombotic disorder may be related to an abnormal fibrin polymerization: the abnormal clot being less accessible to fibrinolysis than normal one. This defective lysis may be due to a defective enhancement by the abnormal fibrin of plasminogen activation by tpA, as demonstrated for fibrinogen Dusard, a congenital dysfibrinogenemia associated with a very severe thrombotic disorder. In some other cases, a decrease in the availability of the plasmin cleavage sites in fibrin clot may be involved. On the contrary, some antithrombotic drugs such as pentosane polysulfate in modifying clot structure allow a better degradation of fibrin clot by fibrinolytic enzymes. It is speculated that this enhanced fibrinolysis could explain, almost in part, the antithrombotic action of these drugs.

• Authors: C Soria, J Soria, M Mirshahi, P Desvignes, P Bonnet, J P Caen
• Journal: Annales de biologie clinique (Ann Biol Clin (Paris)) Vol. 45 Issue 2 Pg. 207-11 ( 1987) ISSN: 0003-3898 [Print] France
• Vernacular Title: Importance de la structure du caillot sur la thrombolyse.
• PMID: 2441630 (Publication Type: English Abstract, Journal Article)

Chemical References

• Pentosan Sulfuric Polyester
• Fibrin
• Thrombin

Topics

• Blood Coagulation (drug effects)
• Fibrin (metabolism)
• Fibrinolysis (drug effects)
• Humans
• Pedigree
• Pentosan Sulfuric Polyester (pharmacology)
• Syndrome
• Thrombin (metabolism)
• Thrombosis (blood, genetics)