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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
11
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pubmed:dateCreated |
1998-4-14
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pubmed:abstractText |
The structural organization and stability of apoB100 in complexes containing triglyceride (TG) and phospholipid have been examined. LDL was delipidated to form aqueous soluble apoB100-TG complexes that retain approximately 70% of LDL TG, but contain no other lipids. The apoB100-TG complexes exhibited reduced amphipathic alpha-helical content (17%) and net negative charge (-2.9 mV) as compared to native LDL-apoB100 (49% and -6 mV, respectively). Of 28 anti-apoB monoclonal antibodies tested, 15 showed partial or full reactivity with apoB100-TG. The immunoreactive epitopes of apoB100-TG were restricted to those situated in either the amino terminal globular domain (4 of 6) or in regions of apoB100 that are predicted to be composed of amphipathic beta-strands (11 of 13). Incubation of the apoB100-TG complex with palmitoyloleoylphosphatidylcholine (POPC) spontaneously (< 10 min) formed homogeneous lipoproteins (20 nm) that contained approximately 300 molecules of POPC per particle (apoB100-PC). Phospholipidation of apoB100-TG complexes partially recovered the alpha-helical content (34%) and net negative charge (-4.9 mV) of the native LDL and restored resistance of apoB100 to denaturation by guanidine HCl (5.8 M). Addition of phospholipids to apoB100-TG also increased the immunoreactivity of specific epitopes that are located primarily in regions of apoB100 that are thought to be constituted of amphipathic beta-strands. The effects of TG and phospholipid on apoB100 conformation appear to be highly domain-specific. On the basis of these results, we propose that the beta-strands of apoB100 may represent a nonflexible lipid-associating backbone, while the amphipathic alpha-helical domains may represent flexible lipid-binding regions that allow the particle to accommodate varying amounts of lipid.
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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/1-palmitoyl-2-oleoylphosphatidylchol...,
http://linkedlifedata.com/resource/pubmed/chemical/Antibodies, Monoclonal,
http://linkedlifedata.com/resource/pubmed/chemical/Apolipoprotein B-100,
http://linkedlifedata.com/resource/pubmed/chemical/Apolipoproteins B,
http://linkedlifedata.com/resource/pubmed/chemical/Deoxycholic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Dimyristoylphosphatidylcholine,
http://linkedlifedata.com/resource/pubmed/chemical/Lipids,
http://linkedlifedata.com/resource/pubmed/chemical/Lipoproteins, LDL,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphatidylcholines,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, LDL,
http://linkedlifedata.com/resource/pubmed/chemical/Triglycerides
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0006-2960
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
17
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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 |
3735-42
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:9521692-Antibodies, Monoclonal,
pubmed-meshheading:9521692-Apolipoprotein B-100,
pubmed-meshheading:9521692-Apolipoproteins B,
pubmed-meshheading:9521692-Cells, Cultured,
pubmed-meshheading:9521692-Deoxycholic Acid,
pubmed-meshheading:9521692-Dimyristoylphosphatidylcholine,
pubmed-meshheading:9521692-Fibroblasts,
pubmed-meshheading:9521692-Humans,
pubmed-meshheading:9521692-Lipid Metabolism,
pubmed-meshheading:9521692-Lipids,
pubmed-meshheading:9521692-Lipoproteins, LDL,
pubmed-meshheading:9521692-Phosphatidylcholines,
pubmed-meshheading:9521692-Protein Binding,
pubmed-meshheading:9521692-Protein Structure, Secondary,
pubmed-meshheading:9521692-Protein Structure, Tertiary,
pubmed-meshheading:9521692-Receptors, LDL,
pubmed-meshheading:9521692-Triglycerides
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pubmed:year |
1998
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pubmed:articleTitle |
Evidence for lipid-dependent structural changes in specific domains of apolipoprotein B100.
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pubmed:affiliation |
Lipoprotein and Atherosclerosis Group, University of Ottawa Heart Institute, Ontario, Canada.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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