Source:http://linkedlifedata.com/resource/pubmed/id/15878877
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
27
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| pubmed:dateCreated |
2005-7-4
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| pubmed:abstractText |
Transgenic and gene disruption experiments in mice have revealed that apolipoprotein (apo) A-V is a potent regulator of plasma triglyceride (TG) levels. To investigate the molecular basis of apoA-V function, the ability of isolated recombinant apoA-V to modulate lipoprotein lipase (LPL) activity was examined in vitro. With three distinct lipid substrate particles, including very low-density lipoprotein (VLDL), a TG/phospholipid emulsion, or dimyristoylphosphatidylcholine liposomes, apoA-V had little effect on LPL activity. In the absence or presence apolipoprotein C-II, apoA-V marginally inhibited LPL activity. On the other hand, apoA-V-dimyristoylphosphatidylcholine disc particles bound to heparin-Sepharose and were specifically eluted upon application of a linear gradient of NaCl. The interaction of apoA-V with sulfated glycosaminoglycans was further studied by surface plasmon resonance spectroscopy. ApoA-V showed strong binding to heparin-coated chips, and binding was competed by free heparin. ApoA-V enrichment enhanced binding of apoC-II-deficient chylomicrons and VLDL to heparin-coated chips. When LPL was first bound to the heparin-coated chip, apoA-V-enriched chylomicrons showed binding. Finally, human pre- and post-heparin plasma samples were subjected to immunoblot analysis with anti-apoA-V IgG. No differences in the amount of apoA-V present were detected. Taken together, the results show that apoA-V lipid complexes bind heparin and, when present on TG-rich lipoprotein particles, may promote their association with cell surface heparan sulfate proteoglycans. Through such interactions, apoA-V may indirectly affect LPL activity, possibly explaining its inverse correlation with plasma TG levels.
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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/APOA5 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Apolipoprotein C-III,
http://linkedlifedata.com/resource/pubmed/chemical/Apolipoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Apolipoproteins A,
http://linkedlifedata.com/resource/pubmed/chemical/Apolipoproteins C,
http://linkedlifedata.com/resource/pubmed/chemical/Blood Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Cholesterol, VLDL,
http://linkedlifedata.com/resource/pubmed/chemical/Dimyristoylphosphatidylcholine,
http://linkedlifedata.com/resource/pubmed/chemical/Heparin,
http://linkedlifedata.com/resource/pubmed/chemical/Lipoprotein Lipase,
http://linkedlifedata.com/resource/pubmed/chemical/Liposomes,
http://linkedlifedata.com/resource/pubmed/chemical/Sepharose,
http://linkedlifedata.com/resource/pubmed/chemical/Triglycerides
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| pubmed:status |
MEDLINE
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| pubmed:month |
Jul
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| pubmed:issn |
0021-9258
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| pubmed:author | |
| pubmed:issnType |
Print
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| pubmed:day |
8
|
| pubmed:volume |
280
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| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
25383-7
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| pubmed:dateRevised |
2007-11-14
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| pubmed:meshHeading |
pubmed-meshheading:15878877-Animals,
pubmed-meshheading:15878877-Apolipoprotein C-III,
pubmed-meshheading:15878877-Apolipoproteins,
pubmed-meshheading:15878877-Apolipoproteins A,
pubmed-meshheading:15878877-Apolipoproteins C,
pubmed-meshheading:15878877-Blood Proteins,
pubmed-meshheading:15878877-Cattle,
pubmed-meshheading:15878877-Cholesterol, VLDL,
pubmed-meshheading:15878877-Chromatography, Affinity,
pubmed-meshheading:15878877-Dimyristoylphosphatidylcholine,
pubmed-meshheading:15878877-Enzyme Activation,
pubmed-meshheading:15878877-Heparin,
pubmed-meshheading:15878877-Humans,
pubmed-meshheading:15878877-Lipoprotein Lipase,
pubmed-meshheading:15878877-Liposomes,
pubmed-meshheading:15878877-Sepharose,
pubmed-meshheading:15878877-Surface Plasmon Resonance,
pubmed-meshheading:15878877-Triglycerides
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| pubmed:year |
2005
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| pubmed:articleTitle |
Apolipoprotein A-V-heparin interactions: implications for plasma lipoprotein metabolism.
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| pubmed:affiliation |
Department of Medical Biosciences/Physiological Chemistry, Umeå University, SE-901 87 Umeå, Sweden.
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| pubmed:publicationType |
Journal Article,
In Vitro,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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