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Related Experiment Videos

Proteolytic processing of human coagulation factor IX by plasmin.

J A Samis1, G D Ramsey, J B Walker

  • 1Departments of Pathology, Biochemistry, and Medicine; Queen's University, Kingston, Ontario, Canada. samisj@post.queensu.ca

Blood
|January 29, 2000
PubMed
Summary

Plasmin significantly reduces factor IX clotting activity and its activated form, factor IXa. This study shows plasmin inactivates factor IX, suggesting a role in down-regulating coagulation.

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Area of Science:

  • Biochemistry
  • Hematology
  • Molecular Biology

Background:

  • Thrombin generation in vivo reduces factor IX (F.IX) activity and generates a cleavage product resembling activated F.IX (F.IXa).
  • Activated fibrinolytic system suggests plasmin may modify F.IX.

Purpose of the Study:

  • To investigate the in vitro effects of plasmin on human factor IX (F.IX) activity and function.

Main Methods:

  • In vitro assays measuring F.IX and F.IXa clotting activity after incubation with plasmin.
  • Analysis of plasmin-hydrolyzed F.IX fragments using SDS-PAGE.
  • Assays for active site binding, antithrombin complex formation, and factor X activation.

Main Results:

  • Plasmin decreased F.IX activity by 80% and F.IXa activity by 50%.

Related Experiment Videos

  • Plasmin hydrolysis produced specific F.IX fragments (45, 30, 20, 14 kd reducing; 52, 14 kd nonreducing).
  • Plasmin-treated F.IX did not bind active site probes, form SDS-stable complexes with antithrombin, or efficiently activate factor X.

    • Conclusions:

    • Plasmin cleaves F.IX at multiple sites but does not generate significant F.IXa.
    • Plasmin inactivates F.IX clotting activity and function, suggesting a role in down-regulating coagulation.
    • Tissue plasminogen activator-induced fibrinolysis in plasma decreases F.IX activity and generates F.IX fragments, supporting plasmin's role in F.IX inactivation.