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J Biol Chem, Vol. 274, Issue 4, 2021-2028, January 22, 1999
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From the Department of Biochemistry, MCP Hahnemann University,
Philadelphia, Pennsylvania 19129, the ¶ Departments of Medicine,
Biochemistry, and Molecular Genetics and the Atherosclerosis Research
Unit, University of Alabama at Birmingham Medical Center, Birmingham,
Alabama 35294, the Lipid-free apolipoprotein (apo) A-I
contributes to the reverse transport of cholesterol from the periphery
to the liver by solubilizing plasma membrane phospholipid and
cholesterol. The features of the apolipoprotein required for this
process are not understood and are addressed in the current study.
Membrane microsolubilization of human fibroblasts is not specific for
apo A-I; unlipidated apos A-II, C, and E incubated with the fibroblast
monolayers at a saturating concentration of 50 µg/ml are all able to
release cholesterol and phospholipid similarly. To determine the
properties of the apolipoprotein that drive the process, apo A-I
peptides spanning the entire sequence of the protein were utilized; the peptides correspond to the 11- and 22-residue amphipathic Center for Molecular and Vascular Biology,
University of Leuven, B-3000 Leuven, Belgium, and the ** Gladstone
Foundation Laboratories for Cardiovascular Disease, Department of
Pathology, Cardiovascular Research Institute, University of California,
San Francisco, California 94140
-helical segments, as well as adjacent combinations of the helices. Of the 20 helical peptides examined, only peptides representing the N-and
C-terminal portions of the protein had the ability to solubilize phospholipid and cholesterol. Cholesterol efflux to the most effective peptides, 44-65 and 209-241, was approximately 50 and 70%,
respectively, of that to intact apo A-I. Deletion mutants of apo E and
apo A-I were constructed that have reduced lipid binding affinities as compared with the intact molecule. The proteins, apo A-I (
222-243), apo A-I (190-243), apo E3 (192-299) and apo E4 (192-299)
all exhibited a decreased ability to remove cellular cholesterol and phospholipid. These decreases correlated with the reduced ability of
these proteins to penetrate into a phospholipid monomolecular film.
Overall, the results indicate that insertion of amphipathic -helices
between the plasma membrane phospholipid molecules is a required step
in the mechanism of apolipoprotein-mediated cellular lipid efflux.
Therefore the lipid binding ability of the apolipoprotein is critical
for efficient membrane microsolubilization.
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