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Apolipoprotein A-I: structure-function relationships.

P G Frank1, Y L Marcel

  • 1Lipoprotein & Atherosclerosis Group, University of Ottawa Heart Institute, 40 Ruskin Street, Ottawa, Ontario, Canada K1Y 4W7.

Journal of Lipid Research
|May 29, 2000
PubMed
Summary
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Apolipoprotein A-I (apoA-I) alpha-helices are key to high-density lipoprotein (HDL) function in reverse cholesterol transport. Understanding apoA-I structure, particularly its tertiary form, is crucial for developing therapies for coronary heart disease.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cardiovascular Science

Background:

  • High-density lipoprotein (HDL) and apolipoprotein A-I (apoA-I) are inversely correlated with coronary heart disease risk.
  • The function of HDL in reverse cholesterol transport (RCT) is mediated by apoA-I's ability to facilitate cholesterol efflux, lipid binding, and lecithin:cholesterol acyltransferase (LCAT) activation.

Purpose of the Study:

  • To elucidate the tertiary structure of apoA-I in both lipid-free and lipid-bound states.
  • To define the specific roles of apoA-I's amphipathic alpha-helices in lipid binding, HDL formation, and LCAT activation.

Main Methods:

  • Analysis of apoA-I secondary structure to understand lipid-binding specificity.
  • Evaluation of proposed models (picket fence vs. belt model) for discoidal lipoprotein structure.

Related Experiment Videos

  • Identification of key alpha-helical domains involved in lipid association and LCAT activation.

    • Main Results:

    • ApoA-I's amphipathic alpha-helices dictate lipid-binding specificity.
    • Evidence supports the 'belt model' for apoA-I-phospholipid complexes, though other models remain possible.
    • Specific N-terminal and C-terminal helices are crucial for initial lipid association, while central helices are vital for mature HDL formation.

    Conclusions:

    • ApoA-I structure-function relationships are complex, with distinct helical regions mediating different aspects of RCT.
    • The LCAT activation domain is primarily helix 144-165, with secondary involvement of helix 166-186.
    • Further research into apoA-I's lipoprotein topology and interactions is needed to fully understand HDL metabolism.