Source:http://linkedlifedata.com/resource/pubmed/id/11876264
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
2002-3-5
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pubmed:abstractText |
The fatty acid-binding proteins are hypothesized to be involved in cellular fatty acid transport and trafficking. We established CaCo-2 cells stably transfected with intestinal fatty acid-binding protein (I-FABP) and examined how the expression of this protein may influence fatty acid metabolism. I-FABP expression was detectable in I-FABP-transfected cells, whereas parent CaCo-2 cells as well as mock-transfected cells failed to express detectable levels of I-FABP mRNA or protein at any stage of differentiation. For studies of lipid metabolism, cells were incubated with [14C]oleic acid in taurocholate micelles containing monoolein, and distribution of labeled fatty acid in cellular and secreted lipids was examined. In one transfected cell clone, expressing the highest level of I-FABP, labeled cellular triacylglycerol increased approximately twofold as compared to control cells. The level of intracellular triacylglycerol in two other I-FABP-transfected clones resembled that of control cells. However, secretion of triacylglycerol was markedly reduced in all the I-FABP-expressing cell lines. Our data suggest that increased expression of I-FABP leads to reduced triacylglycerol secretion in intestinal cells.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/FABP7 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Fatty Acid-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Fatty Acids,
http://linkedlifedata.com/resource/pubmed/chemical/Neoplasm Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Oleic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/Triglycerides,
http://linkedlifedata.com/resource/pubmed/chemical/Tumor Suppressor Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0024-4201
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
37
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
61-8
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:11876264-Caco-2 Cells,
pubmed-meshheading:11876264-Carrier Proteins,
pubmed-meshheading:11876264-Esterification,
pubmed-meshheading:11876264-Fatty Acid-Binding Proteins,
pubmed-meshheading:11876264-Fatty Acids,
pubmed-meshheading:11876264-Gene Expression,
pubmed-meshheading:11876264-Humans,
pubmed-meshheading:11876264-Intestines,
pubmed-meshheading:11876264-Neoplasm Proteins,
pubmed-meshheading:11876264-Oleic Acid,
pubmed-meshheading:11876264-RNA, Messenger,
pubmed-meshheading:11876264-Transfection,
pubmed-meshheading:11876264-Triglycerides,
pubmed-meshheading:11876264-Tumor Suppressor Proteins
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pubmed:year |
2002
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pubmed:articleTitle |
Reduced secretion of triacylglycerol in CaCo-2 cells transfected with intestinal fatty acid-binding protein.
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pubmed:affiliation |
Department of Pharmacology, School of Pharmacy, University of Oslo, Norway. ane.gedde-dahl@haukeland.no
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pubmed:publicationType |
Journal Article
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