| http://purl.uniprot.org/citations/15878877 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/15878877 | http://www.w3.org/2000/01/rdf-schema#comment | "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."xsd:string |
| http://purl.uniprot.org/citations/15878877 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m501589200"xsd:string |
| http://purl.uniprot.org/citations/15878877 | http://purl.uniprot.org/core/author | "Nilsson S."xsd:string |
| http://purl.uniprot.org/citations/15878877 | http://purl.uniprot.org/core/author | "Olivecrona G."xsd:string |
| http://purl.uniprot.org/citations/15878877 | http://purl.uniprot.org/core/author | "Ryan R.O."xsd:string |
| http://purl.uniprot.org/citations/15878877 | http://purl.uniprot.org/core/author | "Beckstead J.A."xsd:string |
| http://purl.uniprot.org/citations/15878877 | http://purl.uniprot.org/core/author | "Lookene A."xsd:string |
| http://purl.uniprot.org/citations/15878877 | http://purl.uniprot.org/core/date | "2005"xsd:gYear |
| http://purl.uniprot.org/citations/15878877 | http://purl.uniprot.org/core/name | "J Biol Chem"xsd:string |
| http://purl.uniprot.org/citations/15878877 | http://purl.uniprot.org/core/pages | "25383-25387"xsd:string |
| http://purl.uniprot.org/citations/15878877 | http://purl.uniprot.org/core/title | "Apolipoprotein A-V-heparin interactions: implications for plasma lipoprotein metabolism."xsd:string |
| http://purl.uniprot.org/citations/15878877 | http://purl.uniprot.org/core/volume | "280"xsd:string |
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