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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
1991-1-16
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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.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Bucladesine,
http://linkedlifedata.com/resource/pubmed/chemical/Cholesterol,
http://linkedlifedata.com/resource/pubmed/chemical/Cholesterol Esters,
http://linkedlifedata.com/resource/pubmed/chemical/Iodine Radioisotopes,
http://linkedlifedata.com/resource/pubmed/chemical/Lipoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Lipoproteins, HDL,
http://linkedlifedata.com/resource/pubmed/chemical/Lipoproteins, HDL3,
http://linkedlifedata.com/resource/pubmed/chemical/Lipoproteins, LDL,
http://linkedlifedata.com/resource/pubmed/chemical/Tyramine,
http://linkedlifedata.com/resource/pubmed/chemical/cholesteryl linoleyl ether,
http://linkedlifedata.com/resource/pubmed/chemical/dilactitol tyramine
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0006-3002
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
12
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pubmed:volume |
1047
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
148-60
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:2174267-Animals,
pubmed-meshheading:2174267-Bucladesine,
pubmed-meshheading:2174267-Cells, Cultured,
pubmed-meshheading:2174267-Cholesterol,
pubmed-meshheading:2174267-Cholesterol Esters,
pubmed-meshheading:2174267-Endocytosis,
pubmed-meshheading:2174267-Female,
pubmed-meshheading:2174267-Granulosa Cells,
pubmed-meshheading:2174267-Iodine Radioisotopes,
pubmed-meshheading:2174267-Lipoproteins,
pubmed-meshheading:2174267-Lipoproteins, HDL,
pubmed-meshheading:2174267-Lipoproteins, HDL3,
pubmed-meshheading:2174267-Lipoproteins, LDL,
pubmed-meshheading:2174267-Microscopy, Electron,
pubmed-meshheading:2174267-Rats,
pubmed-meshheading:2174267-Rats, Inbred Strains,
pubmed-meshheading:2174267-Tyramine
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pubmed:year |
1990
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pubmed:articleTitle |
Uptake and utilization of lipoprotein cholesteryl esters by rat granulosa cells.
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pubmed:affiliation |
Department of Medicine, Stanford University School of Medicine, CA.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, P.H.S.
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