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A cholesteryl ester transfer complex in human plasma.

P E Fielding, C J Fielding

    Proceedings of the National Academy of Sciences of the United States of America
    |June 1, 1980
    PubMed
    Summary
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    This study reveals human plasma lecithin:cholesterol acyltransferase (LCAT) exists exclusively in complexes with apolipoprotein D (apo D) and apolipoprotein A-1 (apo A-1). Most apo D also forms enzyme-free complexes with apolipoprotein A-2 (apo A-2).

    Area of Science:

    • Biochemistry
    • Lipid Metabolism
    • Protein Chemistry

    Background:

    • Lecithin:cholesterol acyltransferase (LCAT) is crucial for lipoprotein metabolism.
    • The structural organization of LCAT and associated proteins in human plasma is not fully understood.

    Purpose of the Study:

    • To elucidate the structural organization and complex formation of LCAT in human plasma.
    • To define the roles of apolipoproteins A-1, A-2, and D in LCAT complex formation.

    Main Methods:

    • Immunoadsorption affinity chromatography was employed using specific antibodies.
    • Antibodies against apolipoprotein D (apo D), apolipoprotein A-1 (apo A-1), and apolipoprotein A-2 (apo A-2) were utilized.
    • Ultracentrifugal flotation was used to assess substrate activity.

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    Main Results:

    • LCAT was exclusively detected in complexes with apo A-1 and apo D.
    • Approximately 80% of apo D was found in enzyme-free complexes with apo A-1 and apo A-2.
    • Removal of LCAT abolished plasma substrate activity, which could be restored by ultracentrifugation.

    Conclusions:

    • LCAT circulates in human plasma as a stable complex with apo A-1 and apo D.
    • A significant portion of apo D exists independently of LCAT, complexed with apo A-1 and apo A-2.
    • These findings clarify the structural basis of LCAT activity and lipoprotein assembly.