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Human factor XIa cleaves fibrinogen: effects on structure and function.

C F Scott, R L Mentzer, A Z Budzynski

    Archives of Biochemistry and Biophysics
    |September 1, 1986
    PubMed
    Summary
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    Factor XIa cleaves fibrinogen, hindering clot formation and fibrin monomer polymerization. This enzyme

    Area of Science:

    • Biochemistry
    • Hematology
    • Proteolysis

    Background:

    • Factor XIa is the activated enzymatic form of factor XI, crucial in coagulation.
    • Factor XIa is generated via factor XII-dependent surface activation in plasma.
    • Known functions include degrading high molecular weight kininogen and activating factor IX.

    Purpose of the Study:

    • To investigate the potential of factor XIa to cleave fibrinogen.
    • To determine the effect of factor XIa on thrombin-catalyzed fibrin clot formation.
    • To analyze the impact of factor XIa-digested fibrinogen on fibrin monomer polymerization.

    Main Methods:

    • Incubation of purified fibrinogen with purified factor XIa.
    • Analysis of fibrinogen cleavage products using proteolysis assays.

    Related Experiment Videos

  • Assessment of fibrin clot formation and fibrin monomer polymerization rates.
  • Comparison of factor XIa activity with thrombin and plasmin.

    • Main Results:

    • Factor XIa cleaves fibrinogen, reducing thrombin-catalyzed fibrin clot formation.
    • Factor XIa-digested fibrinogen fragments significantly inhibit fibrin monomer polymerization.
    • Factor XIa preferentially cleaves the A alpha-chain, then the B beta-chain of fibrinogen, with distinct sites from thrombin.
    • Gamma-chain degradation occurs after prolonged factor XIa exposure.
    • Factor XIa proteolysis differs from plasmin; it does not cleave the B beta-chain N-terminus or hydrolyze fibrin.

    Conclusions:

    • Factor XIa possesses fibrinogenolytic activity that interferes with clot formation.
    • The degradation products of fibrinogen by factor XIa act as potent inhibitors of fibrin polymerization.
    • Factor XIa exhibits distinct substrate specificity compared to plasmin and thrombin, offering new insights into coagulation regulation.