| pubmed-article:11060345 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11060345 | lifeskim:mentions | umls-concept:C0023816 | lld:lifeskim |
| pubmed-article:11060345 | lifeskim:mentions | umls-concept:C0052191 | lld:lifeskim |
| pubmed-article:11060345 | lifeskim:mentions | umls-concept:C0021467 | lld:lifeskim |
| pubmed-article:11060345 | lifeskim:mentions | umls-concept:C0205419 | lld:lifeskim |
| pubmed-article:11060345 | lifeskim:mentions | umls-concept:C0021469 | lld:lifeskim |
| pubmed-article:11060345 | lifeskim:mentions | umls-concept:C0679622 | lld:lifeskim |
| pubmed-article:11060345 | lifeskim:mentions | umls-concept:C1880022 | lld:lifeskim |
| pubmed-article:11060345 | lifeskim:mentions | umls-concept:C0205314 | lld:lifeskim |
| pubmed-article:11060345 | lifeskim:mentions | umls-concept:C0871161 | lld:lifeskim |
| pubmed-article:11060345 | pubmed:issue | 11 | lld:pubmed |
| pubmed-article:11060345 | pubmed:dateCreated | 2000-11-29 | lld:pubmed |
| pubmed-article:11060345 | pubmed:abstractText | We have identified a G-to-A transition in exon 3 of the APOC3 gene resulting in a novel Ala23Thr apolipoprotein (apo) C-III variant, associated with apoC-III deficiency in three unrelated Yucatan Indians. The Ala23Thr substitution modifies the hydrophobic/hydrophilic repartition of the helical N-terminal peptide and hence could disturb the lipid association. In vitro expression in Escherichia coli of wild-type and mutant apoC-III enabled the characterization of the variant. Compared with wild-type apoC-III-Ala23, the mutant apoC-III-Thr23 showed reduced affinity for dimyristoylphosphatidylcholine (DMPC) multilamellar vesicles with higher amounts of free apoC-III. Displacement of apoE from discoidal apoE:dipalmitoylphosphatidycholine (DPPC) complex by apoC-III-Thr23 was comparable to wild type but the less efficient binding of the apoC-III-Thr23 to the discoidal complex resulted in a higher apoE/apoC-III (mol/mol) ratio (34%) than with wild-type/apoE:DPPC mixtures. The inhibition of lipoprotein lipase (LPL) by apoC-III-Thr23 was comparable to that of wild type, and therefore effects on LPL activity could not explain the lower triglyceride (Tg) levels in Thr-23 carriers. Thus, these in vitro results suggest that in vivo the less efficient lipid binding of apoC-III-Thr23 might lead to a faster catabolism of free apoC-III, reflected in the reduced plasma apoC-III levels identified in Thr-23 carriers, and poorer competition with apoE, which might enhance clearance of Tg-rich lipoproteins and lower plasma Tg levels seen in Thr-23 carriers. | lld:pubmed |
| pubmed-article:11060345 | pubmed:language | eng | lld:pubmed |
| pubmed-article:11060345 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11060345 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:11060345 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:11060345 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11060345 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11060345 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11060345 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11060345 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11060345 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11060345 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11060345 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:11060345 | pubmed:issn | 0022-2275 | lld:pubmed |
| pubmed-article:11060345 | pubmed:author | pubmed-author:RosseneuMM | lld:pubmed |
| pubmed-article:11060345 | pubmed:author | pubmed-author:LiuHH | lld:pubmed |
| pubmed-article:11060345 | pubmed:author | pubmed-author:WeissK MKM | lld:pubmed |
| pubmed-article:11060345 | pubmed:author | pubmed-author:BrasseurRR | lld:pubmed |
| pubmed-article:11060345 | pubmed:author | pubmed-author:FerrellRR | lld:pubmed |
| pubmed-article:11060345 | pubmed:author | pubmed-author:HumphriesS... | lld:pubmed |
| pubmed-article:11060345 | pubmed:author | pubmed-author:LinzGG | lld:pubmed |
| pubmed-article:11060345 | pubmed:author | pubmed-author:TalmudP JPJ | lld:pubmed |
| pubmed-article:11060345 | pubmed:author | pubmed-author:XuC FCF | lld:pubmed |
| pubmed-article:11060345 | pubmed:author | pubmed-author:LabeurCC | lld:pubmed |
| pubmed-article:11060345 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11060345 | pubmed:volume | 41 | lld:pubmed |
| pubmed-article:11060345 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11060345 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11060345 | pubmed:pagination | 1760-71 | lld:pubmed |
| pubmed-article:11060345 | pubmed:dateRevised | 2008-11-21 | lld:pubmed |
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| pubmed-article:11060345 | pubmed:meshHeading | pubmed-meshheading:11060345... | lld:pubmed |
| pubmed-article:11060345 | pubmed:year | 2000 | lld:pubmed |
| pubmed-article:11060345 | pubmed:articleTitle | Characterization of the lipid-binding properties and lipoprotein lipase inhibition of a novel apolipoprotein C-III variant Ala23Thr. | lld:pubmed |
| pubmed-article:11060345 | pubmed:affiliation | Cardiovascular Genetics Division, Department of Medicine, Royal Free and University College London Medical School, London WC1E 6JJ, UK. | lld:pubmed |
| pubmed-article:11060345 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:11060345 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| entrez-gene:345 | entrezgene:pubmed | pubmed-article:11060345 | lld:entrezgene |
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