| pubmed-article:16278492 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:16278492 | lifeskim:mentions | umls-concept:C0023823 | lld:lifeskim |
| pubmed-article:16278492 | lifeskim:mentions | umls-concept:C2717940 | lld:lifeskim |
| pubmed-article:16278492 | lifeskim:mentions | umls-concept:C0522534 | lld:lifeskim |
| pubmed-article:16278492 | lifeskim:mentions | umls-concept:C0392756 | lld:lifeskim |
| pubmed-article:16278492 | lifeskim:mentions | umls-concept:C0486616 | lld:lifeskim |
| pubmed-article:16278492 | lifeskim:mentions | umls-concept:C0392747 | lld:lifeskim |
| pubmed-article:16278492 | lifeskim:mentions | umls-concept:C0243144 | lld:lifeskim |
| pubmed-article:16278492 | lifeskim:mentions | umls-concept:C0597177 | lld:lifeskim |
| pubmed-article:16278492 | lifeskim:mentions | umls-concept:C0443172 | lld:lifeskim |
| pubmed-article:16278492 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:16278492 | pubmed:dateCreated | 2006-1-26 | lld:pubmed |
| pubmed-article:16278492 | pubmed:abstractText | The ability of human postprandial triacylglycerol-rich lipoproteins (TRLs), isolated after meals enriched in saturated fatty acids (SFAs), n-6 PUFAs, and MUFAs, to inhibit the uptake of 125I-labeled LDL by the LDL receptor was investigated in HepG2 cells. Addition of TRLs resulted in a dose-dependent inhibition of heparin-releasable binding, cell-associated radioactivity, and degradation products of 125I-labeled LDL (P < 0.001). SFA-rich Svedberg flotation rate (Sf) 60-400 resulted in significantly greater inhibition of cell-associated radioactivity than PUFA-rich particles (P = 0.016) and total uptake of 125I-labeled LDL compared with PUFA- and MUFA-rich particles (P < 0.02). Normalization of the apolipoprotein (apo)E but not apoC-III content of the TRLs removed the effect of meal fatty acid composition, and addition of an anti-apoE antibody reversed the inhibitory effect of TRLs on the total uptake of 125I-labeled LDL. Real time RT-PCR showed that the SFA-rich Sf 60-400 increased the expression of genes involved in hepatic lipid synthesis (P < 0.05) and decreased the expression of the LDL receptor-related protein 1 compared with MUFAs (P = 0.008). In conclusion, these findings suggest an alternative or additional mechanism whereby acute fat ingestion can influence LDL clearance via competitive apoE-dependent effects of TRL on the LDL receptor. | lld:pubmed |
| pubmed-article:16278492 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:16278492 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:16278492 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:16278492 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:16278492 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:16278492 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:16278492 | pubmed:issn | 0022-2275 | lld:pubmed |
| pubmed-article:16278492 | pubmed:author | pubmed-author:WilliamsChris... | lld:pubmed |
| pubmed-article:16278492 | pubmed:author | pubmed-author:LeakeDavid... | lld:pubmed |
| pubmed-article:16278492 | pubmed:author | pubmed-author:JacksonKim... | lld:pubmed |
| pubmed-article:16278492 | pubmed:author | pubmed-author:MaitinVatsala... | lld:pubmed |
| pubmed-article:16278492 | pubmed:author | pubmed-author:YaqoobParveen... | lld:pubmed |
| pubmed-article:16278492 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:16278492 | pubmed:volume | 47 | lld:pubmed |
| pubmed-article:16278492 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:16278492 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:16278492 | pubmed:pagination | 393-403 | lld:pubmed |
| pubmed-article:16278492 | pubmed:dateRevised | 2011-11-17 | lld:pubmed |
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| pubmed-article:16278492 | pubmed:year | 2006 | lld:pubmed |
| pubmed-article:16278492 | pubmed:articleTitle | Saturated fat-induced changes in Sf 60-400 particle composition reduces uptake of LDL by HepG2 cells. | lld:pubmed |
| pubmed-article:16278492 | pubmed:affiliation | School of Food Biosciences, University of Reading, Reading, Berkshire, United Kingdom. k.g.jackson@reading.ac.uk | lld:pubmed |
| pubmed-article:16278492 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:16278492 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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