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Human plasma lipoprotein [a]. Structural properties.

J W Gaubatz, C Heideman, A M Gotto

    The Journal of Biological Chemistry
    |April 10, 1983
    PubMed
    Summary
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    Lipoprotein [a] apoprotein consists of two disulfide-bonded subunits: one with apolipoprotein [a] and the other with apolipoprotein B. Its structure differs significantly from other lipoproteins.

    Area of Science:

    • Biochemistry
    • Molecular Biology
    • Cardiovascular Science

    Background:

    • Lipoprotein [a] (Lp[a]) is an atherogenic lipoprotein particle.
    • Understanding Lp[a] structure is crucial for cardiovascular disease research.

    Purpose of the Study:

    • To elucidate the subunit composition and secondary structure of the apoprotein in Lipoprotein [a].

    Main Methods:

    • Electrophoresis using sodium dodecyl sulfate-polyacrylamide gels.
    • Chemical reduction to analyze subunit disulfide bonds.
    • Circular dichroism spectroscopy to assess secondary structure.

    Main Results:

    • Apoprotein of Lp[a] (1.2 million Da) dissociates into two subunits (approx. 490,000 Da and 645,000 Da) upon reduction, indicating disulfide bonds.

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  • Apolipoprotein [a] and apolipoprotein B immunoreactivities were initially co-localized but separated after reduction.
  • Lp[a] showed significantly less alpha-helical structure (30%) and more disordered structure compared to LDL (48%) and HDL (70%).

    • Conclusions:

    • The apoprotein of Lp[a] is composed of two distinct subunits linked by disulfide bonds.
    • Lp[a] possesses a unique secondary structure distinct from LDL and HDL, potentially influencing its function and atherogenicity.