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Isolation and sequence analysis of a cDNA clone encoding the fifth complement component.

A B Lundwall, R A Wetsel, T Kristensen

    The Journal of Biological Chemistry
    |February 25, 1985
    PubMed
    Summary
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    Researchers synthesized a probe to isolate human C5 complement cDNA, revealing its beta alpha-chain orientation and sequence similarity to other proteins. This study advances understanding of complement system gene expression.

    Area of Science:

    • Molecular Biology
    • Immunology
    • Genetics

    Background:

    • The fifth component of human complement (C5) plays a crucial role in the immune response.
    • Understanding the genetic and molecular basis of C5 is essential for comprehending complement system function.

    Purpose of the Study:

    • To isolate and characterize the complementary DNA (cDNA) encoding human C5.
    • To elucidate the structural organization and sequence of the C5 promolecule.

    Main Methods:

    • Synthesis of a mixed-sequence oligonucleotide probe based on C5a protein sequence.
    • Screening of a human liver cDNA library using the synthesized probe.
    • DNA sequencing of the isolated cDNA clone using the dideoxy method.
    • Northern blot analysis of human liver and Hep G2 cell line RNA.

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    Main Results:

    • Isolation of a 1.85 kilobase pair human C5 cDNA clone.
    • Determination of the predicted protein sequence, including the C5a fragment and flanking regions.
    • Identification of a beta alpha-chain orientation for the C5 promolecule.
    • Sequence similarity found between human C5 and murine C3/human alpha 2-macroglobulin.
    • Detection of a C5 mRNA species of approximately 5.2 kilobase pairs in human liver and Hep G2 cells.

    Conclusions:

    • The study successfully cloned and sequenced a significant portion of human C5 cDNA.
    • The findings confirm the beta alpha-chain orientation of C5 promolecule synthesis.
    • The identified sequence similarities suggest evolutionary relationships within complement proteins.