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Cooperative interaction between factor VII and cell surface-expressed tissue factor.

D S Fair, M J MacDonald

    The Journal of Biological Chemistry
    |August 25, 1987
    PubMed
    Summary
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    This study investigated factor VII binding to tissue factor on J82 cells, revealing cooperative binding to a dimeric tissue factor receptor. This explains the assembly of the extrinsic pathway on cell surfaces.

    Area of Science:

    • Biochemistry
    • Cell Biology
    • Hemostasis

    Background:

    • The extrinsic pathway of coagulation is initiated by the binding of factor VII to tissue factor (TF) on cell surfaces.
    • Understanding this interaction is crucial for comprehending hemostasis and developing anticoagulant therapies.

    Purpose of the Study:

    • To investigate the binding kinetics and activity of factor VII (FVII) on the J82 bladder carcinoma cell line expressing tissue factor.
    • To elucidate the molecular mechanism of FVII-TF complex formation and its implications for extrinsic pathway assembly.

    Main Methods:

    • Utilized FVII binding assays on J82 cells, measuring time-, temperature-, and calcium-dependency.
    • Employed monoclonal antibodies against TF to assess binding specificity and inhibition.
    • Analyzed binding data using sigmoidal binding isotherms, Hill plots, and kinetic analyses (Km, Vmax, kcat).

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  • Investigated factor X (FX) activation rates in the presence of varying FVII concentrations.

    • Main Results:

    • FVII binding to J82 cells was specific, saturable, and calcium-dependent, inhibited by anti-TF antibodies.
    • Binding data revealed sigmoidal isotherms and Hill slopes (avg. 2.1), indicating positive cooperativity.
    • Kinetic analysis showed an apparent Km for FX of 274 nM and a Vmax of 4.15 nM/min.
    • FX activation rate exhibited a sigmoidal relationship with FVII concentration, with Hill slopes changing from 2.0 to 1.0.
    • Apparent dissociation constant (Kd) was 222 ± 85 pM, with Vmax for FX cleavage at 5.54 ± 1.04 nM/min.

    Conclusions:

    • FVII binds to at least two sites on TF with positive cooperativity, suggesting TF is a dimer on J82 cell surfaces.
    • The 1:1 stoichiometry of the FVII-TF complex at saturation supports the dimeric TF model.
    • These findings provide critical insights into the molecular basis of extrinsic pathway initiation and TF receptor function.