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Papers In Press, published online ahead of print January 16, 2003
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Dept. of Laboratory Medicine, National Inst. of Health, Bethesda, MD 20892-1508
Corresponding Author: aremaley{at}nih.gov
In order to examine the necessary structural features of lipid acceptors, synthetic peptides were tested for lipid efflux on ABCA1-transfected Hela cells (ABCA1 cells) and on control Hela cells lacking ABCA1. 37pA, a peptide that contains class A amphipathic helices, showed a 2–4 fold increase in cholesterol and phospholipid efflux from ABCA1 cells compared to control cells. The 37pA peptide synthesized with a mixture of L and D-amino acids was less effective in solubilizing DMPC vesicles and in effluxing lipid from cells. In contrast, the 37pA peptide synthesized with all D-amino acids was as effective as the L-amino acid form of the peptide. Unlike apoA-I, 37pA was also capable, at a reduced level (75% decrease), of causing cholesterol efflux without ABCA1 from control cells, Tangier cells, or from ABCA1 cells after fixation. In summary, (1) the amphipathic helix was found to be a key structural motif for lipid efflux by ABCA1, (2) there was no stereoselective requirement for lipid efflux by 37pA, which suggests that there is not a receptor-ligand type interaction between ABCA1 and lipid acceptors, and (3) unlike apoA-I, synthetic peptides can also efflux lipid from cells by a passive, energy-independent pathway that does not involve ABCA1.
Revised on January 16, 2003
Accepted on January 15, 2003
Synthetic amphipathic helical peptide mediated efflux of lipid from cells by an ABCA1-dependent and an ABCA1-independent pathway
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