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Papers In Press, published online ahead of print February 1, 2004
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Department of Cardiology, McGill University Health Centre, Montreal, QC H3A 1A1
Corresponding Author: michel.marcil{at}mcgill.ca
ApoE/ABCA1 interactions were investigated in human intact fibroblasts induced with 22 (R)-hydroxycholesterol and 9-cis-retinoic acid (stimulated cells). Here we show that purified human plasma apoE3 forms a complex with ABCA1 in normal fibroblasts. Lipid-free apoE3 inhibited the binding of 125I-apoA-I to ABCA1 more efficiently than reconstituted HDL particles r(LpE3) (IC50=2.5±0.4 vs. 12.3±1.3 µg/mL). ApoE isoforms showed similar binding for ABCA1 and exhibited identical kinetics in their abilities to induce ABCA1-dependent cholesterol efflux. Mutation of ABCA1 associated with Tangier disease (TD) (C1477R) abolished both apoE3 binding and apoE3-mediated cholesterol efflux. Analysis of apoE3-containing particles generated during incubation of lipid-free apoE3 with stimulated normal cells showed nascent apoE3/cholesterol/phospholipid complexes that exhibited pre-
Revised on December 23, 2003
Accepted on January 23, 2004
Molecular interactions between apolipoprotein E and the ATP-binding cassette transporter A1 (ABCA1): Impact on ApoE lipidation
-electrophoretic mobility with a particle size ranging from 9 to 15 nm, whereas lipid-free apoE3 incubated with ABCA1 mutant (C1477R) cells was unable to form such particles. These results demonstrate that: 1) apoE association with lipids reduced its ability to interact with ABCA1; 2) apoE isoforms did not affect apoE binding to ABCA1; 3) apoE-mediated ABCA1-dependent cholesterol efflux was not affected by apoE isoforms in fibroblasts; and 3) the lipid translocase activity of ABCA1 generates pre--LpE3-like particles. Thus, ABCA1 is essential for HDL-LpE biogenesis.
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