pubmed-article:11504730 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:11504730 | lifeskim:mentions | umls-concept:C0007634 | lld:lifeskim |
pubmed-article:11504730 | lifeskim:mentions | umls-concept:C0023688 | lld:lifeskim |
pubmed-article:11504730 | lifeskim:mentions | umls-concept:C0205227 | lld:lifeskim |
pubmed-article:11504730 | lifeskim:mentions | umls-concept:C1612060 | lld:lifeskim |
pubmed-article:11504730 | lifeskim:mentions | umls-concept:C0172934 | lld:lifeskim |
pubmed-article:11504730 | pubmed:issue | 42 | lld:pubmed |
pubmed-article:11504730 | pubmed:dateCreated | 2001-10-15 | lld:pubmed |
pubmed-article:11504730 | pubmed:abstractText | The nuclear receptors liver X receptor alpha (LXRalpha) (NR1H3) and LXRbeta (NR1H2) are important regulators of genes involved in lipid metabolism, including ABCA1, ABCG1, and sterol regulatory element-binding protein-1c (SREBP-1c). Although it has been demonstrated that oxysterols are LXR ligands, little is known about the identity of the physiological activators of these receptors. Here we confirm earlier studies demonstrating a dose-dependent induction of ABCA1 and ABCG1 in human monocyte-derived macrophages by cholesterol loading. In addition, we show that formation of 27-hydroxycholesterol and cholestenoic acid, products of CYP27 action on cholesterol, is dependent on the dose of cholesterol used to load the cells. Other proposed LXR ligands, including 20(S)-hydroxycholesterol, 22(R)-hydroxycholesterol, and 24(S),25-epoxycholesterol, could not be detected under these conditions. A role for CYP27 in regulation of cholesterol-induced genes was demonstrated by the following findings. 1) Introduction of CYP27 into HEK-293 cells conferred an induction of ABCG1 and SREBP-1c; 2) upon cholesterol loading, CYP27-expressing cells induce these genes to a greater extent than in control cells; 3) in CYP27-deficient human skin fibroblasts, the induction of ABCA1 in response to cholesterol loading was ablated; and 4) in a coactivator association assay, 27-hydroxycholesterol functionally activated LXR. We conclude that 27-hydroxylation of cholesterol is an important pathway for LXR activation in response to cholesterol overload. | lld:pubmed |
pubmed-article:11504730 | pubmed:language | eng | lld:pubmed |
pubmed-article:11504730 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11504730 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:11504730 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11504730 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11504730 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11504730 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11504730 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11504730 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11504730 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:11504730 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11504730 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11504730 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11504730 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11504730 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11504730 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11504730 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11504730 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11504730 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:11504730 | pubmed:month | Oct | lld:pubmed |
pubmed-article:11504730 | pubmed:issn | 0021-9258 | lld:pubmed |
pubmed-article:11504730 | pubmed:author | pubmed-author:ChenYY | lld:pubmed |
pubmed-article:11504730 | pubmed:author | pubmed-author:LunaE JEJ | lld:pubmed |
pubmed-article:11504730 | pubmed:author | pubmed-author:GeII | lld:pubmed |
pubmed-article:11504730 | pubmed:author | pubmed-author:WrightS DSD | lld:pubmed |
pubmed-article:11504730 | pubmed:author | pubmed-author:ZhouGG | lld:pubmed |
pubmed-article:11504730 | pubmed:author | pubmed-author:SparrowC PCP | lld:pubmed |
pubmed-article:11504730 | pubmed:author | pubmed-author:MacNaulK LKL | lld:pubmed |
pubmed-article:11504730 | pubmed:author | pubmed-author:MenkeJ GJG | lld:pubmed |
pubmed-article:11504730 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:11504730 | pubmed:day | 19 | lld:pubmed |
pubmed-article:11504730 | pubmed:volume | 276 | lld:pubmed |
pubmed-article:11504730 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:11504730 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:11504730 | pubmed:pagination | 38378-87 | lld:pubmed |
pubmed-article:11504730 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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pubmed-article:11504730 | pubmed:year | 2001 | lld:pubmed |
pubmed-article:11504730 | pubmed:articleTitle | 27-hydroxycholesterol is an endogenous ligand for liver X receptor in cholesterol-loaded cells. | lld:pubmed |
pubmed-article:11504730 | pubmed:affiliation | Department of Atherosclerosis and Endocrinology, and Metabolic Research, Merck Research Laboratories, Rahway, New Jersey 07065, USA. | lld:pubmed |
pubmed-article:11504730 | pubmed:publicationType | Journal Article | lld:pubmed |
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