Molecular Mechanisms of Fibrinolysis

Br J Haematol. 2005 May;129(3):307-21. doi: 10.1111/j.1365-2141.2005.05444.x.


The molecular mechanisms that finely co-ordinate fibrin formation and fibrinolysis are now well defined. The structure and function of all major fibrinolytic proteins, which include serine proteases, their inhibitors, activators and receptors, have been characterized. Measurements of real time, dynamic molecular interactions during fibrinolysis of whole blood clots can now be carried out in vitro. The development of gene-targeted mice deficient in one or more fibrinolytic protein(s) has demonstrated expected and unexpected roles for these proteins in both intravascular and extravascular settings. In addition, genetic analysis of human deficiency syndromes has revealed specific mutations that result in human disorders that are reflective of either fibrinolytic deficiency or excess. Elucidation of the fine control of fibrinolysis under different physiological and pathological haemostatic states will undoubtedly lead to novel therapeutic interventions. Here, we review the fundamental features of intravascular plasmin generation, and consider the major clinical syndromes resulting from abnormalities in fibrinolysis.

Publication types

  • Review

MeSH terms

  • Animals
  • Blood Coagulation Disorders / blood
  • Blood Coagulation Disorders / genetics
  • Fibrinolysin / physiology
  • Fibrinolysis / genetics*
  • Fibrinolysis / physiology
  • Humans
  • Mice
  • Models, Animal
  • Plasminogen / deficiency
  • Plasminogen / physiology


  • Plasminogen
  • Fibrinolysin