Document Detail


5A apolipoprotein mimetic peptide promotes cholesterol efflux and reduces atherosclerosis in mice.
MedLine Citation:
PMID:  20484557     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Intravenous administration of apolipoprotein (apo) A-I complexed with phospholipid has been shown to rapidly reduce plaque size in both animal models and humans. Short synthetic amphipathic peptides can mimic the antiatherogenic properties of apoA-I and have been proposed as alternative therapeutic agents. In this study, we investigated the atheroprotective effect of the 5A peptide, a bihelical amphipathic peptide that specifically effluxes cholesterol from cells by ATP-binding cassette transporter 1 (ABCA1). 5A stimulated a 3.5-fold increase in ABCA1-mediated efflux from cells and an additional 2.5-fold increase after complexing it with phospholipid (1:7 mol/mol). 5A-palmitoyl oleoyl phosphatidyl choline (POPC), but not free 5A, was also found to promote cholesterol efflux by ABCG1. When incubated with human serum, 5A-POPC bound primarily to high-density lipoprotein (HDL) but also to low-density lipoprotein (LDL) and promoted the transfer of cholesterol from LDL to HDL. Twenty-four hours after intravenous injection of 5A-POPC (30 mg/kg) into apoE-knockout (KO) mice, both the cholesterol (181%) and phospholipid (219%) content of HDL significantly increased. By an in vivo cholesterol isotope dilution study and monitoring of the flux of cholesterol from radiolabeled macrophages to stool, 5A-POPC treatment was observed to increase reverse cholesterol transport. In three separate studies, 5A when complexed with various phospholipids reduced aortic plaque surface area by 29 to 53% (n = 8 per group; p < 0.02) in apoE-KO mice. No signs of toxicity from the treatment were observed during these studies. In summary, 5A promotes cholesterol efflux both in vitro and in vivo and reduces atherosclerosis in apoE-KO mice, indicating that it may be a useful alternative to apoA-I for HDL therapy.
Authors:
Marcelo J A Amar; Wilissa D'Souza; Scott Turner; Stephen Demosky; Denis Sviridov; John Stonik; Jayraz Luchoomun; Jason Voogt; Marc Hellerstein; Dmitri Sviridov; Alan T Remaley
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Publication Detail:
Type:  In Vitro; Journal Article; Research Support, N.I.H., Extramural; Research Support, N.I.H., Intramural     Date:  2010-05-19
Journal Detail:
Title:  The Journal of pharmacology and experimental therapeutics     Volume:  334     ISSN:  1521-0103     ISO Abbreviation:  J. Pharmacol. Exp. Ther.     Publication Date:  2010 Aug 
Date Detail:
Created Date:  2010-07-19     Completed Date:  2010-08-17     Revised Date:  2011-08-03    
Medline Journal Info:
Nlm Unique ID:  0376362     Medline TA:  J Pharmacol Exp Ther     Country:  United States    
Other Details:
Languages:  eng     Pagination:  634-41     Citation Subset:  IM    
Affiliation:
Lipoprotein Metabolism Section, Pulmonary and Vascular Medicine Branch, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, Maryland 20892, USA. ma90x@nih.gov
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MeSH Terms
Descriptor/Qualifier:
ATP-Binding Cassette Transporters / metabolism
Animals
Aorta / drug effects,  pathology
Apolipoprotein A-I / chemistry,  physiology*
Apolipoproteins E / genetics
Atherosclerosis / drug therapy*,  metabolism,  pathology
Biological Transport
Cholesterol / metabolism*
Female
Humans
Lipoproteins / metabolism
Lipoproteins, HDL / blood
Lipoproteins, LDL / blood
Macrophages, Peritoneal / drug effects,  metabolism
Male
Mice
Mice, Inbred C57BL
Mice, Knockout
Molecular Mimicry
Peptides / chemistry,  diagnostic use*
Phosphatidylcholines / chemistry
Rats
Rats, Sprague-Dawley
Chemical
Reg. No./Substance:
0/ABCG1 protein, mouse; 0/ATP-Binding Cassette Transporters; 0/Apolipoprotein A-I; 0/Apolipoproteins E; 0/Lipoproteins; 0/Lipoproteins, HDL; 0/Lipoproteins, LDL; 0/Peptides; 0/Phosphatidylcholines; 57-88-5/Cholesterol
Comments/Corrections

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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