Source:http://linkedlifedata.com/resource/pubmed/id/19635584
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
12
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pubmed:dateCreated |
2009-11-3
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pubmed:abstractText |
Whereas hepatocytes secrete the major human plasma high density lipoproteins (HDL)-protein, apo A-I, as lipid-free and lipidated species, the biogenic itineraries of apo A-II and apo E are unknown. Human plasma and HepG2 cell-derived apo A-II and apo E occur as monomers, homodimers and heterodimers. Dimerization of apo A-II, which is more lipophilic than apo A-I, is catalyzed by lipid surfaces. Thus, we hypothesized that lipidation of intracellular and secreted apo A-II exceeds that of apo A-I, and once lipidated, apo A-II dimerizes. Fractionation of HepG2 cell lysate and media by size exclusion chromatography showed that intracellular apo A-II and apo E are fully lipidated and occur on nascent HDL and VLDL respectively, while only 45% of intracellular apo A-I is lipidated. Secreted apo A-II and apo E occur on small HDL and on LDL and large HDL respectively. HDL particles containing both apo A-II and apo A-I form only after secretion from both HepG2 and Huh7 hepatoma cells. Apo A-II dimerizes intracellularly while intracellular apo E is monomeric but after secretion associates with HDL and subsequently dimerizes. Thus, HDL apolipoproteins A-I, A-II and E have distinct intracellular and post-secretory pathways of hepatic lipidation and dimerization in the process of HDL formation. These early forms of HDL are expected to follow different apolipoprotein-specific pathways through plasma remodeling and reverse cholesterol transport.
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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/APOA1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/APOA2 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Apolipoprotein A-I,
http://linkedlifedata.com/resource/pubmed/chemical/Apolipoprotein A-II,
http://linkedlifedata.com/resource/pubmed/chemical/Apolipoproteins E,
http://linkedlifedata.com/resource/pubmed/chemical/Lipoproteins, HDL,
http://linkedlifedata.com/resource/pubmed/chemical/Sepharose,
http://linkedlifedata.com/resource/pubmed/chemical/thiopropyl-sepharose
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0006-3002
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
1791
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1125-32
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pubmed:dateRevised |
2011-9-26
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pubmed:meshHeading |
pubmed-meshheading:19635584-Apolipoprotein A-I,
pubmed-meshheading:19635584-Apolipoprotein A-II,
pubmed-meshheading:19635584-Apolipoproteins E,
pubmed-meshheading:19635584-Carcinoma, Hepatocellular,
pubmed-meshheading:19635584-Chromatography, Gel,
pubmed-meshheading:19635584-Hep G2 Cells,
pubmed-meshheading:19635584-Humans,
pubmed-meshheading:19635584-Intracellular Space,
pubmed-meshheading:19635584-Lipoproteins, HDL,
pubmed-meshheading:19635584-Liver Neoplasms,
pubmed-meshheading:19635584-Models, Biological,
pubmed-meshheading:19635584-Protein Binding,
pubmed-meshheading:19635584-Protein Multimerization,
pubmed-meshheading:19635584-Sepharose,
pubmed-meshheading:19635584-Time Factors,
pubmed-meshheading:19635584-Ultracentrifugation
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pubmed:year |
2009
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pubmed:articleTitle |
Apolipoproteins A-I, A-II and E are independently distributed among intracellular and newly secreted HDL of human hepatoma cells.
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pubmed:affiliation |
Section of Atherosclerosis and Vascular Medicine, Department of Medicine, Baylor College of Medicine, One Baylor Plaza, MS-A601, Houston, TX 77030, USA. baibag@bcm.tmc.edu
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pubmed:publicationType |
Journal Article,
Research Support, N.I.H., Extramural
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