| pubmed-article:14754908 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:14754908 | lifeskim:mentions | umls-concept:C1412058 | lld:lifeskim |
| pubmed-article:14754908 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
| pubmed-article:14754908 | pubmed:issue | 5 | lld:pubmed |
| pubmed-article:14754908 | pubmed:dateCreated | 2004-4-16 | lld:pubmed |
| pubmed-article:14754908 | pubmed:abstractText | Apolipoprotein E (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 (125)I-apoA-I to ABCA1 more efficiently than reconstituted HDL particles (IC(50) = 2.5 +/- 0.4 microg/ml vs. 12.3 +/- 1.3 microg/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 (C1477R) abolished both apoE3 binding and apoE3-mediated cholesterol efflux. Analysis of apoE3-containing particles generated during the incubation of lipid-free apoE3 with stimulated normal cells showed nascent apoE3/cholesterol/phospholipid complexes that exhibited prebeta-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 4). the lipid translocase activity of ABCA1 generates apoE-containing high density-sized lipoprotein particles. Thus, ABCA1 is essential for the biogenesis of high density-sized lipoprotein containing only apoE particles in vivo. | lld:pubmed |
| pubmed-article:14754908 | pubmed:language | eng | lld:pubmed |
| pubmed-article:14754908 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14754908 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:14754908 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14754908 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14754908 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14754908 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14754908 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14754908 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:14754908 | pubmed:month | May | lld:pubmed |
| pubmed-article:14754908 | pubmed:issn | 0022-2275 | lld:pubmed |
| pubmed-article:14754908 | pubmed:author | pubmed-author:GenestJacques... | lld:pubmed |
| pubmed-article:14754908 | pubmed:author | pubmed-author:MarcilMichelM | lld:pubmed |
| pubmed-article:14754908 | pubmed:author | pubmed-author:HaidarBassamB | lld:pubmed |
| pubmed-article:14754908 | pubmed:author | pubmed-author:DenisMaximeM | lld:pubmed |
| pubmed-article:14754908 | pubmed:author | pubmed-author:KrimbouLarbiL | lld:pubmed |
| pubmed-article:14754908 | pubmed:author | pubmed-author:CarrierMarily... | lld:pubmed |
| pubmed-article:14754908 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:14754908 | pubmed:volume | 45 | lld:pubmed |
| pubmed-article:14754908 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:14754908 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:14754908 | pubmed:pagination | 839-48 | lld:pubmed |
| pubmed-article:14754908 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:14754908 | pubmed:meshHeading | pubmed-meshheading:14754908... | lld:pubmed |
| pubmed-article:14754908 | pubmed:meshHeading | pubmed-meshheading:14754908... | lld:pubmed |
| pubmed-article:14754908 | pubmed:meshHeading | pubmed-meshheading:14754908... | lld:pubmed |
| pubmed-article:14754908 | pubmed:meshHeading | pubmed-meshheading:14754908... | lld:pubmed |
| pubmed-article:14754908 | pubmed:meshHeading | pubmed-meshheading:14754908... | lld:pubmed |
| pubmed-article:14754908 | pubmed:meshHeading | pubmed-meshheading:14754908... | lld:pubmed |
| pubmed-article:14754908 | pubmed:meshHeading | pubmed-meshheading:14754908... | lld:pubmed |
| pubmed-article:14754908 | pubmed:meshHeading | pubmed-meshheading:14754908... | lld:pubmed |
| pubmed-article:14754908 | pubmed:meshHeading | pubmed-meshheading:14754908... | lld:pubmed |
| pubmed-article:14754908 | pubmed:meshHeading | pubmed-meshheading:14754908... | lld:pubmed |
| pubmed-article:14754908 | pubmed:meshHeading | pubmed-meshheading:14754908... | lld:pubmed |
| pubmed-article:14754908 | pubmed:year | 2004 | lld:pubmed |
| pubmed-article:14754908 | pubmed:articleTitle | Molecular interactions between apoE and ABCA1: impact on apoE lipidation. | lld:pubmed |
| pubmed-article:14754908 | pubmed:affiliation | Cardiovascular Genetics Laboratory, Division of Cardiology, McGill University Health Centre/Royal Victoria Hospital, Montréal, Québec H3A 1A1, Canada. | lld:pubmed |
| pubmed-article:14754908 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:14754908 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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