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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
3
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pubmed:dateCreated |
1998-3-19
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pubmed:abstractText |
The effects of cholesterol esterase (CEase) and acyl coenzyme A:cholesterol acyltransferase (ACAT) inhibitors on the uptake and esterification of cholesterol in Caco-2 cells were examined. CEase increased the uptake of [3H]cholesterol from bile salt mixed-micelles by 2.5- to 3.0-fold and its esterification by greater than 25-fold. Inhibition of cellular ACAT activity with CL277082 or CP113818 had little or no effect on cholesterol uptake measured in the presence or absence of CEase. The subsequent esterification of [3H]cholesterol was reduced greater than 90% by each ACAT inhibitor. Similar results were obtained in cells in which ACAT activity was induced by preincubation either with 25-hydroxycholesterol and mevalonic acid or with CEase and bile salt mixed-micelles containing 100 micromol/L cholesterol. Neither ACAT inhibitor had an effect on CEase-mediated synthesis or hydrolysis of cholesteryl oleate in vitro. Thus, the uptake of cholesterol from bile salt mixed-micelles in the presence or absence of CEase was not regulated by the level of cellular ACAT expression. The subsequent esterification of exogenous sterol was not due to CEase, but was completely dependent on ACAT activity. The dissociation of cholesterol uptake from ACAT activity suggests that the factors controlling the transfer of sterol from extracellular media to the cell are different from the factors regulating the cellular level of cholesterol esterification.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/25-hydroxycholesterol,
http://linkedlifedata.com/resource/pubmed/chemical/Bile Acids and Salts,
http://linkedlifedata.com/resource/pubmed/chemical/CL 277082,
http://linkedlifedata.com/resource/pubmed/chemical/CP 113818,
http://linkedlifedata.com/resource/pubmed/chemical/Cholesterol,
http://linkedlifedata.com/resource/pubmed/chemical/Cholesterol Esters,
http://linkedlifedata.com/resource/pubmed/chemical/Enzyme Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/Hydroxycholesterols,
http://linkedlifedata.com/resource/pubmed/chemical/Mevalonic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Micelles,
http://linkedlifedata.com/resource/pubmed/chemical/Oleic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Phenylurea Compounds,
http://linkedlifedata.com/resource/pubmed/chemical/Pyridines,
http://linkedlifedata.com/resource/pubmed/chemical/Sterol Esterase,
http://linkedlifedata.com/resource/pubmed/chemical/Sterol O-Acyltransferase
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0026-0495
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
47
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
325-32
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:9500571-Bile Acids and Salts,
pubmed-meshheading:9500571-Caco-2 Cells,
pubmed-meshheading:9500571-Cholesterol,
pubmed-meshheading:9500571-Cholesterol Esters,
pubmed-meshheading:9500571-Enzyme Inhibitors,
pubmed-meshheading:9500571-Esterification,
pubmed-meshheading:9500571-Humans,
pubmed-meshheading:9500571-Hydroxycholesterols,
pubmed-meshheading:9500571-Mevalonic Acid,
pubmed-meshheading:9500571-Micelles,
pubmed-meshheading:9500571-Oleic Acid,
pubmed-meshheading:9500571-Phenylurea Compounds,
pubmed-meshheading:9500571-Pyridines,
pubmed-meshheading:9500571-Sterol Esterase,
pubmed-meshheading:9500571-Sterol O-Acyltransferase
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pubmed:year |
1998
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pubmed:articleTitle |
Inhibition of acyl coenzyme A:cholesterol acyltransferase blocks esterification but not uptake of cholesterol in Caco-2 cells.
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pubmed:affiliation |
CV Therapeutics, Palo Alto, CA, USA.
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pubmed:publicationType |
Journal Article
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