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Visualization and analysis of apolipoprotein A-I interaction with binary phospholipid bilayers.

M Alejandra Tricerri1, Juan D Toledo, Susana A Sanchez

  • 1Instituto de Investigaciones Bioquímicas, Consejo Nacional de Investigaciones Cientificas y Technológicas-Universidad Nacional de La Plata, La Plata, Argentina, 1900.

Journal of Lipid Research
|January 18, 2005
PubMed
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Apolipoprotein A-I (apoA-I) selectively removes lipids from fluid domains in cell membranes. This interaction is most effective when fluid lipid domains are present within a solid phase, facilitating cholesterol and phospholipid efflux.

Area of Science:

  • Biochemistry
  • Biophysics
  • Cell Biology

Background:

  • Apolipoprotein A-I (apoA-I) is crucial for lipid metabolism and reverse cholesterol transport.
  • Previous studies suggested apoA-I interacts with cell lipid domains to promote lipid efflux.
  • Understanding this interaction requires analyzing apoA-I's behavior with defined lipid bilayers.

Purpose of the Study:

  • To investigate the interaction between apoA-I and lipid bilayers composed of dimyristoylphosphatidylcholine/distearoylphosphatidylcholine (DMPC/DSPC) at a phase-coexisting temperature.
  • To determine the selectivity of apoA-I for different lipid domains (solid vs. liquid-crystalline).
  • To characterize the lipid-protein complexes formed and the conditions favoring efficient lipid removal.

Main Methods:

  • Giant unilamellar vesicles (GUVs) and small unilamellar vesicles (SUVs) composed of DMPC/DSPC were used.

Related Experiment Videos

  • Two-photon fluorescence microscopy with Laurdan dye was employed to visualize lipid domains.
  • Changes in vesicle size, morphology, and lipid composition were monitored in real-time.
  • Lipid-protein complexes were isolated and quantified after incubation.

    • Main Results:

    • ApoA-I induced a decrease in GUV size and shape deformation, with enrichment in the solid DSPC component.
    • Real-time monitoring revealed selective lipid removal by apoA-I from liquid-crystalline domains.
    • Protein-lipid complexes formed were enriched in the fluid lipid components.
    • Optimal apoA-I-lipid interaction occurred under conditions favoring nucleation of fluid domains within a gel phase.

    Conclusions:

    • ApoA-I preferentially interacts with and removes lipids from fluid domains in DMPC/DSPC bilayers.
    • The efficiency of lipid removal is dependent on specific bilayer conditions, particularly the presence of nucleated fluid domains.
    • These findings provide insights into the mechanism of apoA-I-mediated lipid efflux at the membrane interface.