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Related Experiment Videos

A polymorphism affecting apolipoprotein A-II translational efficiency determines high density lipoprotein size and

M H Doolittle1, R C LeBoeuf, C H Warden

  • 1Wadsworth Veterans Administration Medical Center, Los Angeles, California 90073.

The Journal of Biological Chemistry
|September 25, 1990
PubMed
Summary

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A mouse gene variation controls high density lipoprotein (HDL) size and cholesterol transport. Increased apolipoprotein A-II (apoA-II) synthesis leads to larger HDL particles with more lipid, offering insights into human HDL metabolism.

Area of Science:

  • Lipid Metabolism
  • Molecular Genetics
  • Cardiovascular Research

Background:

  • High density lipoproteins (HDL) are crucial for reverse cholesterol transport.
  • HDL particles are heterogeneous in size and protein composition.
  • Apolipoprotein A-II (apoA-II) is a major protein component of HDL.

Purpose of the Study:

  • To investigate the genetic basis of HDL size and apolipoprotein heterogeneity in mice.
  • To elucidate the regulatory mechanisms of apoA-II synthesis and its impact on HDL structure.
  • To establish a mouse model for studying HDL lipid metabolism relevant to humans.

Main Methods:

  • Analysis of HDL electrophoretic mobility and apolipoprotein composition in different mouse strains.
  • Genetic linkage analysis to identify the responsible gene locus.

Related Experiment Videos

  • Measurement of apoA-I and apoA-II synthesis and catabolism rates.
  • In vitro translation of apoA-II mRNA and cDNA sequencing.

    • Main Results:

    • A monogenic variation in mice controls HDL size and apoA-II content.
    • Increased apoA-II synthesis, not mRNA levels, correlates with larger HDL particles and higher lipid content.
    • The apoA-II structural gene locus on mouse chromosome 1 is implicated.
    • Nucleotide substitutions in apoA-II cDNA suggest altered translational efficiency.

    Conclusions:

    • HDL particle assembly is regulated by apoA-II production, not fixed stoichiometry.
    • Higher apoA-II levels result in larger, more lipid-rich HDL particles.
    • Mouse HDL polymorphism provides a model for human HDL-lipid metabolic relationships.