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Interaction of coagulation factor Xa with human platelets.

J P Miletich, C M Jackson, P W Majerus

    Proceedings of the National Academy of Sciences of the United States of America
    |September 1, 1977
    PubMed
    Summary
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    Platelets have specific receptors for Factor Xa (FXa) that appear after the release reaction. These FXa receptors significantly accelerate thrombin generation on the platelet surface.

    Area of Science:

    • Biochemistry
    • Hematology
    • Cell Biology

    Background:

    • Platelets play a crucial role in hemostasis and thrombosis.
    • Factor Xa (FXa) is a key enzyme in the coagulation cascade.
    • The interaction between FXa and platelets is critical for thrombin generation.

    Purpose of the Study:

    • To investigate the mechanism of thrombin generation on platelet surfaces.
    • To identify and characterize Factor Xa (FXa) binding sites on human platelets.
    • To understand the role of platelet activation in FXa binding and thrombin formation.

    Main Methods:

    • Incubation of human platelets with 125I-labeled Factor Xa (FXa) and prothrombin.
    • Measurement of thrombin formation.
    • Assessment of FXa binding to platelet receptors.

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  • Use of platelet activators (thrombin, calcium ionophore A23187) and inhibitors (dibutyryl cyclic AMP).

    • Main Results:

    • FXa binding to platelets and subsequent thrombin generation are dependent on the FXa concentration.
    • Platelet activation (release reaction) precedes the appearance of FXa binding sites.
    • FXa binds reversibly to specific, protein-based receptors on the platelet surface after the release reaction.
    • Bound FXa catalyzes thrombin formation at rates significantly higher than FXa in solution.
    • Dibutyryl cyclic AMP inhibits FXa binding and thrombin generation.

    Conclusions:

    • Human platelets possess specific receptors for Factor Xa (FXa) that are distinct from thrombin receptors.
    • These FXa receptors are expressed after the platelet release reaction and are crucial for efficient thrombin generation at the platelet surface.
    • FXa binding to these receptors dramatically enhances its catalytic activity in prothrombin conversion to thrombin.