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Characterization of Factor V activation intermediates.

M E Nesheim, W B Foster, R Hewick

    The Journal of Biological Chemistry
    |March 10, 1984
    PubMed
    Summary
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    Bovine Factor V activation by thrombin generates intermediate proteins B and C. These subunits form a calcium-dependent complex essential for biological activity, with distinct precursor-product relationships identified.

    Area of Science:

    • Biochemistry
    • Molecular Biology
    • Protein Chemistry

    Background:

    • Bovine Factor V is a crucial coagulation protein.
    • Partial activation by thrombin generates various intermediates and end products.
    • Understanding the activation pathway is key to comprehending hemostasis.

    Purpose of the Study:

    • To elucidate the intermediate and end products of bovine Factor V partial activation.
    • To characterize the subunit composition and biological activity of activation intermediates.
    • To define the precursor-product relationships during Factor V activation.

    Main Methods:

    • Column chromatography under nondenaturing conditions.
    • Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE).

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  • Protein staining (Coomassie blue, Schiff-periodate, silver), Ca2+ and EDTA treatments, NH2-terminal sequencing, and amino acid composition analysis.

    • Main Results:

    • Partial activation yielded intermediates B and C, and end products C1, D, E, F, and G.
    • Intermediates B and C form a Ca2+-dependent, biologically active complex, with both subunits required for activity.
    • Precursor-product relationships were established: B yields C1, E, G; C yields D, F. End product D originates from C's NH2 terminus, and C1 from B's NH2 terminus.

    Conclusions:

    • Bovine Factor V activation involves a single cleavage generating NH2-terminal C and COOH-terminal B fragments.
    • The B-C complex is a Ca2+-stabilized heterodimer essential for Factor V activity.
    • Specific cleavage events and subunit origins define the activation cascade and product formation.