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http://purl.uniprot.org/citations/19542565http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/19542565http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/19542565http://www.w3.org/2000/01/rdf-schema#comment"Glycosylphosphatidylinositol-anchored HDL-binding protein (GPIHBP1) binds both LPL and chylomicrons, suggesting that GPIHBP1 is a platform for LPL-dependent processing of triglyceride (TG)-rich lipoproteins. Here, we investigated whether GPIHBP1 affects LPL activity in the absence and presence of LPL inhibitors angiopoietin-like (ANGPTL)3 and ANGPTL4. Like heparin, GPIHBP1 stabilized but did not activate LPL. ANGPTL4 potently inhibited nonstabilized LPL as well as heparin-stabilized LPL but not GPIHBP1-stabilized LPL. Like ANGPTL4, ANGPTL3 inhibited nonstabilized LPL but not GPIHBP1-stabilized LPL. ANGPTL3 also inhibited heparin-stabilized LPL but with less potency than nonstabilized LPL. Consistent with these in vitro findings, fasting serum TGs of Angptl4(-/-)/Gpihbp1(-/-) mice were lower than those of Gpihbp1(-/-) mice and approached those of wild-type littermates. In contrast, serum TGs of Angptl3(-/-)/Gpihbp1(-/-) mice were only slightly lower than those of Gpihbp1(-/-) mice. Treating Gpihbp1(-/-) mice with ANGPTL4- or ANGPTL3-neutralizing antibodies recapitulated the double knockout phenotypes. These data suggest that GPIHBP1 functions as an LPL stabilizer. Moreover, therapeutic agents that prevent LPL inhibition by ANGPTL4 or, to a lesser extent, ANGPTL3, may benefit individuals with hyperlipidemia caused by gene mutations associated with decreased LPL stability."xsd:string
http://purl.uniprot.org/citations/19542565http://purl.org/dc/terms/identifier"doi:10.1194/jlr.m900145-jlr200"xsd:string
http://purl.uniprot.org/citations/19542565http://purl.org/dc/terms/identifier"doi:10.1194/jlr.m900145-jlr200"xsd:string
http://purl.uniprot.org/citations/19542565http://purl.uniprot.org/core/author"Hu Y."xsd:string
http://purl.uniprot.org/citations/19542565http://purl.uniprot.org/core/author"Hu Y."xsd:string
http://purl.uniprot.org/citations/19542565http://purl.uniprot.org/core/author"Zhao S."xsd:string
http://purl.uniprot.org/citations/19542565http://purl.uniprot.org/core/author"Zhao S."xsd:string
http://purl.uniprot.org/citations/19542565http://purl.uniprot.org/core/author"Xiong W."xsd:string
http://purl.uniprot.org/citations/19542565http://purl.uniprot.org/core/author"Xiong W."xsd:string
http://purl.uniprot.org/citations/19542565http://purl.uniprot.org/core/author"Yu D."xsd:string
http://purl.uniprot.org/citations/19542565http://purl.uniprot.org/core/author"Yu D."xsd:string
http://purl.uniprot.org/citations/19542565http://purl.uniprot.org/core/author"Schneider M."xsd:string
http://purl.uniprot.org/citations/19542565http://purl.uniprot.org/core/author"Schneider M."xsd:string
http://purl.uniprot.org/citations/19542565http://purl.uniprot.org/core/author"Ding Z.M."xsd:string
http://purl.uniprot.org/citations/19542565http://purl.uniprot.org/core/author"Ding Z.M."xsd:string
http://purl.uniprot.org/citations/19542565http://purl.uniprot.org/core/author"Powell D.R."xsd:string
http://purl.uniprot.org/citations/19542565http://purl.uniprot.org/core/author"Powell D.R."xsd:string
http://purl.uniprot.org/citations/19542565http://purl.uniprot.org/core/author"Desai U."xsd:string
http://purl.uniprot.org/citations/19542565http://purl.uniprot.org/core/author"Desai U."xsd:string
http://purl.uniprot.org/citations/19542565http://purl.uniprot.org/core/author"Gay J."xsd:string
http://purl.uniprot.org/citations/19542565http://purl.uniprot.org/core/author"Gay J."xsd:string
http://purl.uniprot.org/citations/19542565http://purl.uniprot.org/core/author"Gololobov G."xsd:string
http://purl.uniprot.org/citations/19542565http://purl.uniprot.org/core/author"Gololobov G."xsd:string