pubmed-article:2174267 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:2174267 | lifeskim:mentions | umls-concept:C0042153 | lld:lifeskim |
pubmed-article:2174267 | lifeskim:mentions | umls-concept:C0034721 | lld:lifeskim |
pubmed-article:2174267 | lifeskim:mentions | umls-concept:C0034693 | lld:lifeskim |
pubmed-article:2174267 | lifeskim:mentions | umls-concept:C0018207 | lld:lifeskim |
pubmed-article:2174267 | lifeskim:mentions | umls-concept:C0023820 | lld:lifeskim |
pubmed-article:2174267 | lifeskim:mentions | umls-concept:C0008387 | lld:lifeskim |
pubmed-article:2174267 | lifeskim:mentions | umls-concept:C0243144 | lld:lifeskim |
pubmed-article:2174267 | pubmed:issue | 2 | lld:pubmed |
pubmed-article:2174267 | pubmed:dateCreated | 1991-1-16 | lld:pubmed |
pubmed-article:2174267 | pubmed:abstractText | Earlier studies have shown that rat granulosa cells grown in serum-free medium are exquisitely responsive to exogenously provided lipoprotein cholesterol. In this study we compare the amount of cholesterol (cholesteryl ester) actually delivered from various homologous and heterologous cholesterol-rich lipoproteins and examine the intracellular pathways used in the delivery system. Granulosa cells were incubated for 5 or 24 h with 125I-labeled human (h) HDL3, rat (r) HDL or hLDL equipped with non-releasable apoprotein and cholesteryl ether tags which accumulate within cells, even after degradation. We show that all the tested lipoproteins were similarly efficient in cholesteryl ester delivery; i.e., based on cholesterol: protein ratios of the starting ligands, each delivered approximately the same cholesteryl ester mass and evoked a similar progestin response. However, each lipoprotein was processed quite differently by the granulosa cells: hHDL3-cholesteryl ester was taken up almost exclusively by an non-endocytic pathway, hLDL-cholesteryl ester almost exclusively by an endocytic pathway and rHDL-cholesteryl ester by both pathways. In general, there was no correlation between the total amount of lipoprotein bound or apoprotein internalized and/or degraded by the cells with the amount of cholesteryl ester received or the level of the progestin response. Hormone stimulation upregulated the preferred pathway for each lipoprotein. | lld:pubmed |
pubmed-article:2174267 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2174267 | pubmed:language | eng | lld:pubmed |
pubmed-article:2174267 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2174267 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:2174267 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2174267 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2174267 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2174267 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2174267 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2174267 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2174267 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2174267 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2174267 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2174267 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2174267 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2174267 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:2174267 | pubmed:month | Nov | lld:pubmed |
pubmed-article:2174267 | pubmed:issn | 0006-3002 | lld:pubmed |
pubmed-article:2174267 | pubmed:author | pubmed-author:AzharSS | lld:pubmed |
pubmed-article:2174267 | pubmed:author | pubmed-author:ReavenEE | lld:pubmed |
pubmed-article:2174267 | pubmed:author | pubmed-author:TsaiLL | lld:pubmed |
pubmed-article:2174267 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:2174267 | pubmed:day | 12 | lld:pubmed |
pubmed-article:2174267 | pubmed:volume | 1047 | lld:pubmed |
pubmed-article:2174267 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:2174267 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:2174267 | pubmed:pagination | 148-60 | lld:pubmed |
pubmed-article:2174267 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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pubmed-article:2174267 | pubmed:meshHeading | pubmed-meshheading:2174267-... | lld:pubmed |
pubmed-article:2174267 | pubmed:year | 1990 | lld:pubmed |
pubmed-article:2174267 | pubmed:articleTitle | Uptake and utilization of lipoprotein cholesteryl esters by rat granulosa cells. | lld:pubmed |
pubmed-article:2174267 | pubmed:affiliation | Department of Medicine, Stanford University School of Medicine, CA. | lld:pubmed |
pubmed-article:2174267 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:2174267 | pubmed:publicationType | Comparative Study | lld:pubmed |
pubmed-article:2174267 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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