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Structural comparisons between mouse and human prealbumin.

S Wakasugi, S Maeda, K Shimada

    Journal of Biochemistry
    |December 1, 1985
    PubMed
    Summary
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    Researchers cloned mouse prealbumin cDNA to create models for familial amyloidotic polyneuropathy. This mouse prealbumin shares structural similarities with human prealbumin, aiding in amyloidosis research.

    Area of Science:

    • Molecular Biology
    • Genetics
    • Biochemistry

    Background:

    • Familial amyloidotic polyneuropathy (FAP) is a debilitating disease.
    • Mouse models are crucial for understanding and treating human diseases.

    Purpose of the Study:

    • To clone mouse prealbumin cDNA for developing FAP model systems.
    • To analyze the structural differences between mouse and human prealbumin.

    Main Methods:

    • Cloning mouse prealbumin cDNA using human prealbumin cDNA as a probe.
    • Deducing primary protein structure from cDNA sequence analysis.

    Main Results:

    • Mouse prealbumin consists of 147 amino acids (127 mature, 20 signal sequence), similar to human prealbumin.

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  • 25 amino acid substitutions were found in mouse prealbumin compared to human.
  • Most substitutions are on the protein's surface, with conserved core and channel regions.
  • Conclusions:

    • The cloned mouse prealbumin cDNA is valuable for creating FAP models.
    • Structural conservation suggests functional similarities relevant to amyloidosis research.