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Characterization of a cDNA coding for human protein C.

D Foster, E W Davie

    Proceedings of the National Academy of Sciences of the United States of America
    |August 1, 1984
    PubMed
    Summary
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    Researchers isolated cDNA clones coding for human protein C, a vital plasma serine protease. This protein regulates blood coagulation by inactivating key factors, and its sequence shows homology to other vitamin K-dependent proteases.

    Area of Science:

    • Biochemistry
    • Molecular Biology
    • Genetics

    Background:

    • Protein C is a mammalian plasma precursor to a serine protease.
    • Activated Protein C inactivates factors Va and VIIIa, crucial cofactors in blood coagulation.
    • Understanding Protein C's genetic basis is essential for studying coagulation disorders.

    Purpose of the Study:

    • To isolate and characterize cDNA clones encoding human Protein C.
    • To elucidate the structure and sequence of human Protein C.
    • To compare human Protein C with related plasma serine proteases.

    Main Methods:

    • Screening of a human liver cDNA lambda gt11 library using an antibody to human Protein C.
    • Isolation and plaque-purification of positive clones.

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  • Sequencing of cDNA inserts to determine the coding sequence and non-coding regions.

    • Main Results:

    • Seven positive clones were isolated from 2 x 10^6 phage.
    • Two sequenced clones contained cDNA inserts coding for human Protein C, including light chain, connecting region, heavy chain, stop codon, and poly(A) tail.
    • Amino acid sequence analysis indicated synthesis as a single polypeptide chain, processed into light and heavy chains linked by a disulfide bond.
    • High homology was observed between human and bovine Protein C sequences.
    • Significant DNA and amino acid sequence identity was found with prothrombin, factor IX, and factor X, particularly in the catalytic region.

    Conclusions:

    • The isolated cDNA clones provide the genetic sequence for human Protein C.
    • Human Protein C is synthesized as a precursor that undergoes post-translational modification.
    • The sequence homology highlights evolutionary relationships among vitamin K-dependent serine proteases.