|
rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
2
|
|
pubmed:dateCreated |
2006-1-26
|
|
pubmed:abstractText |
The ability of human postprandial triacylglycerol-rich lipoproteins (TRLs), isolated after meals enriched in saturated fatty acids (SFAs), n-6 PUFAs, and MUFAs, to inhibit the uptake of 125I-labeled LDL by the LDL receptor was investigated in HepG2 cells. Addition of TRLs resulted in a dose-dependent inhibition of heparin-releasable binding, cell-associated radioactivity, and degradation products of 125I-labeled LDL (P < 0.001). SFA-rich Svedberg flotation rate (Sf) 60-400 resulted in significantly greater inhibition of cell-associated radioactivity than PUFA-rich particles (P = 0.016) and total uptake of 125I-labeled LDL compared with PUFA- and MUFA-rich particles (P < 0.02). Normalization of the apolipoprotein (apo)E but not apoC-III content of the TRLs removed the effect of meal fatty acid composition, and addition of an anti-apoE antibody reversed the inhibitory effect of TRLs on the total uptake of 125I-labeled LDL. Real time RT-PCR showed that the SFA-rich Sf 60-400 increased the expression of genes involved in hepatic lipid synthesis (P < 0.05) and decreased the expression of the LDL receptor-related protein 1 compared with MUFAs (P = 0.008). In conclusion, these findings suggest an alternative or additional mechanism whereby acute fat ingestion can influence LDL clearance via competitive apoE-dependent effects of TRL on the LDL receptor.
|
|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antibodies, Monoclonal,
http://linkedlifedata.com/resource/pubmed/chemical/Apolipoprotein B-100,
http://linkedlifedata.com/resource/pubmed/chemical/Apolipoprotein B-48,
http://linkedlifedata.com/resource/pubmed/chemical/Apolipoprotein C-III,
http://linkedlifedata.com/resource/pubmed/chemical/Apolipoproteins B,
http://linkedlifedata.com/resource/pubmed/chemical/Apolipoproteins C,
http://linkedlifedata.com/resource/pubmed/chemical/Apolipoproteins E,
http://linkedlifedata.com/resource/pubmed/chemical/Cholesterol,
http://linkedlifedata.com/resource/pubmed/chemical/Chylomicrons,
http://linkedlifedata.com/resource/pubmed/chemical/Dietary Fats,
http://linkedlifedata.com/resource/pubmed/chemical/Dietary Fats, Unsaturated,
http://linkedlifedata.com/resource/pubmed/chemical/Fatty Acid Synthetase Complex,
http://linkedlifedata.com/resource/pubmed/chemical/Fatty Acids,
http://linkedlifedata.com/resource/pubmed/chemical/Hydroxymethylglutaryl CoA Reductases,
http://linkedlifedata.com/resource/pubmed/chemical/Intracellular Signaling Peptides...,
http://linkedlifedata.com/resource/pubmed/chemical/Lipoproteins, LDL,
http://linkedlifedata.com/resource/pubmed/chemical/Lipoproteins, VLDL,
http://linkedlifedata.com/resource/pubmed/chemical/Low Density Lipoprotein...,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Proprotein Convertases,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, LDL,
http://linkedlifedata.com/resource/pubmed/chemical/SREBF1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/SREBP cleavage-activating protein,
http://linkedlifedata.com/resource/pubmed/chemical/Serine Endopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/Sterol O-Acyltransferase,
http://linkedlifedata.com/resource/pubmed/chemical/Sterol Regulatory Element Binding...,
http://linkedlifedata.com/resource/pubmed/chemical/Triglycerides,
http://linkedlifedata.com/resource/pubmed/chemical/membrane-bound transcription...
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Feb
|
|
pubmed:issn |
0022-2275
|
|
pubmed:author |
|
|
pubmed:issnType |
Print
|
|
pubmed:volume |
47
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
393-403
|
|
pubmed:dateRevised |
2011-11-17
|
|
pubmed:meshHeading |
pubmed-meshheading:16278492-Adult,
pubmed-meshheading:16278492-Antibodies, Monoclonal,
pubmed-meshheading:16278492-Apolipoprotein B-100,
pubmed-meshheading:16278492-Apolipoprotein B-48,
pubmed-meshheading:16278492-Apolipoprotein C-III,
pubmed-meshheading:16278492-Apolipoproteins B,
pubmed-meshheading:16278492-Apolipoproteins C,
pubmed-meshheading:16278492-Apolipoproteins E,
pubmed-meshheading:16278492-Binding, Competitive,
pubmed-meshheading:16278492-Carcinoma, Hepatocellular,
pubmed-meshheading:16278492-Cell Line, Tumor,
pubmed-meshheading:16278492-Cholesterol,
pubmed-meshheading:16278492-Chylomicrons,
pubmed-meshheading:16278492-Dietary Fats,
pubmed-meshheading:16278492-Dietary Fats, Unsaturated,
pubmed-meshheading:16278492-Endocytosis,
pubmed-meshheading:16278492-Fatty Acid Synthetase Complex,
pubmed-meshheading:16278492-Fatty Acids,
pubmed-meshheading:16278492-Gene Expression,
pubmed-meshheading:16278492-Humans,
pubmed-meshheading:16278492-Hydroxymethylglutaryl CoA Reductases,
pubmed-meshheading:16278492-Intracellular Signaling Peptides and Proteins,
pubmed-meshheading:16278492-Lipoproteins, LDL,
pubmed-meshheading:16278492-Lipoproteins, VLDL,
pubmed-meshheading:16278492-Low Density Lipoprotein Receptor-Related Protein-1,
pubmed-meshheading:16278492-Male,
pubmed-meshheading:16278492-Membrane Proteins,
pubmed-meshheading:16278492-Middle Aged,
pubmed-meshheading:16278492-Proprotein Convertases,
pubmed-meshheading:16278492-Receptors, LDL,
pubmed-meshheading:16278492-Serine Endopeptidases,
pubmed-meshheading:16278492-Sterol O-Acyltransferase,
pubmed-meshheading:16278492-Sterol Regulatory Element Binding Protein 1,
pubmed-meshheading:16278492-Triglycerides
|
|
pubmed:year |
2006
|
|
pubmed:articleTitle |
Saturated fat-induced changes in Sf 60-400 particle composition reduces uptake of LDL by HepG2 cells.
|
|
pubmed:affiliation |
School of Food Biosciences, University of Reading, Reading, Berkshire, United Kingdom. k.g.jackson@reading.ac.uk
|
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|
