Source:http://linkedlifedata.com/resource/pubmed/id/11123936
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
51
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pubmed:dateCreated |
2001-1-8
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pubmed:abstractText |
To determine the importance of hepatic apolipoprotein (apo) E in lipoprotein metabolism, HepG2 cells were transfected with a constitutive expression vector (pRc/CMV) containing either the complete or the first 474 base pairs of the human apoE cDNA inserted in an antisense orientation, for apoE gene inactivation, or the full-length human apoE cDNA inserted in a sense orientation for overexpression of apoE. Stable transformants were obtained that expressed 15, 24, 226, and 287% the apoE level of control HepG2 cells. The metabolism of low-density lipoprotein (LDL) and high-density lipoprotein-3 (HDL(3)), two lipoprotein classes following both holoparticle and cholesteryl esters (CE)-selective uptake pathways, was compared between all these cells. LDL-protein degradation, an indicator of the holoparticle uptake, was greater in low apoE expressing cells than in control or high expressing cells, while HDL(3)-protein degradation paralleled the apoE levels of the cells (r(2) = 0.989). LDL- and HDL(3)-protein association was higher in low apoE expressing cells compared to control cells. In opposition, LDL- and HDL(3)-CE association was not different from control cells in low apoE expressing cells but rose in high apoE expressing cells. In consequence, the CE-selective uptake (CE/protein association ratio) was positively correlated with the level of apoE expression in all cells for both LDL (r(2) = 0.977) and HDL(3) (r(2) = 0.998). We also show that, although in normal and low apoE expressor cells, 92% of LDL- and 80% HDL(3)-CE hydrolysis is sensitive to chloroquine suggesting a pathway linked to lysosomes for both lipoproteins, cells overexpressing apoE lost 60% of chloroquine-sensitive HDL(3)-CE hydrolysis without affecting that of LDL-CE. Thus, the level of apoE expression in HepG2 cells determines the fate of LDL and HDL(3).
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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/Apolipoproteins E,
http://linkedlifedata.com/resource/pubmed/chemical/Chloroquine,
http://linkedlifedata.com/resource/pubmed/chemical/Cholesterol, HDL,
http://linkedlifedata.com/resource/pubmed/chemical/Cholesterol Esters,
http://linkedlifedata.com/resource/pubmed/chemical/Lipoproteins, HDL,
http://linkedlifedata.com/resource/pubmed/chemical/Lipoproteins, LDL,
http://linkedlifedata.com/resource/pubmed/chemical/Tritium
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0006-2960
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
26
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pubmed:volume |
39
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
16084-91
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:11123936-Apolipoproteins E,
pubmed-meshheading:11123936-Carcinoma, Hepatocellular,
pubmed-meshheading:11123936-Chloroquine,
pubmed-meshheading:11123936-Cholesterol, HDL,
pubmed-meshheading:11123936-Cholesterol Esters,
pubmed-meshheading:11123936-Genetic Vectors,
pubmed-meshheading:11123936-Humans,
pubmed-meshheading:11123936-Hydrolysis,
pubmed-meshheading:11123936-Intracellular Fluid,
pubmed-meshheading:11123936-Lipoproteins, HDL,
pubmed-meshheading:11123936-Lipoproteins, LDL,
pubmed-meshheading:11123936-Protein Binding,
pubmed-meshheading:11123936-Temperature,
pubmed-meshheading:11123936-Transfection,
pubmed-meshheading:11123936-Tritium,
pubmed-meshheading:11123936-Tumor Cells, Cultured
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pubmed:year |
2000
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pubmed:articleTitle |
Low- and high-density lipoprotein metabolism in HepG2 cells expressing various levels of apolipoprotein E.
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pubmed:affiliation |
Département des Sciences Biologiques, Université du Québec à Montréal, C.P. 8888, Succ. Centre-ville, Montréal, Québec, Canada.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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