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Binding of coagulation factor XI to washed human platelets.

J S Greengard, M J Heeb, E Ersdal

    Biochemistry
    |July 1, 1986
    PubMed
    Summary

    Human coagulation factor XI binds to stimulated platelets, requiring zinc, calcium, and high molecular weight kininogen. This interaction suggests potential saturation of platelet binding sites in plasma.

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    Area of Science:

    • Hematology
    • Biochemistry
    • Molecular Biology

    Background:

    • Coagulation factor XI (FXI) plays a role in the intrinsic pathway of blood coagulation.
    • Platelets are crucial cellular components involved in hemostasis and thrombosis.
    • The interaction between FXI and platelets is not fully understood, particularly under physiological conditions.

    Purpose of the Study:

    • To investigate the binding characteristics of human coagulation factor XI to human platelets.
    • To determine the role of zinc ions, calcium ions, and high molecular weight kininogen (HMWK) in FXI-platelet interactions.
    • To elucidate the potential mechanism and implications of FXI binding to platelets.

    Main Methods:

    • Studied the binding of purified human FXI to washed human platelets.
    • Investigated binding in the presence of physiological concentrations of zinc ions, calcium ions, and HMWK.
    • Utilized Scatchard analysis to quantify binding sites and affinity.
    • Assessed the effects of platelet stimulation on FXI binding.

    Main Results:

    • Significant FXI binding to platelets was observed at physiological ion concentrations when HMWK was present.
    • Binding was specific, reversible, saturable, and required platelet stimulation.
    • Scatchard analysis revealed approximately 1500 binding sites/platelet with a dissociation constant of ~10 nM.
    • Calcium and HMWK synergistically enhanced zinc-promoted FXI binding.
    • Optimal ion concentrations for FXI binding mirrored those for HMWK binding.

    Conclusions:

    • Platelet-bound FXI may be saturated in plasma due to its concentration (~25 nM) relative to binding affinity (~10 nM).
    • HMWK modulates metal ion effects on FXI binding, suggesting a potential complex formation on the platelet surface.
    • FXI and HMWK may form a ternary complex on stimulated platelets, similar to their interactions in solution.

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