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Characterization of a cDNA coding for human factor VII.

F S Hagen, C L Gray, P O'Hara

    Proceedings of the National Academy of Sciences of the United States of America
    |April 1, 1986
    PubMed
    Summary
    This summary is machine-generated.

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    Researchers isolated complementary DNA (cDNA) clones for factor VII, a key protein in blood coagulation. This study reveals the complete amino acid sequence and structure of factor VII, crucial for understanding its role in hemostasis.

    Area of Science:

    • Biochemistry
    • Molecular Biology
    • Hematology

    Background:

    • Factor VII is a plasma precursor to a serine protease essential for blood coagulation.
    • Its activated form (Factor VIIa) initiates the coagulation cascade by activating Factor X and/or Factor IX.

    Purpose of the Study:

    • To isolate and characterize complementary DNA (cDNA) clones encoding human Factor VII.
    • To determine the complete amino acid sequence and structural features of Factor VII.

    Main Methods:

    • cDNA libraries were prepared from human liver and Hep G2 cell poly(A) RNA.
    • Amino acid sequencing was performed on the deduced protein sequence from the cDNAs.

    Main Results:

    • cDNA clones for Factor VII were successfully obtained.

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  • The deduced amino acid sequence revealed a prepro-leader sequence and a mature protein of 406 amino acids.
  • Factor VII is converted to Factor VIIa via cleavage, forming light and heavy chains with distinct functional domains (Gla, EGF, serine protease).

    • Conclusions:

    • The study elucidated the complete structure of Factor VII, including its precursor form and mature protein.
    • Factor VII shares significant sequence homology with other vitamin K-dependent plasma proteins, suggesting a common evolutionary origin and functional relationship.