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http://purl.uniprot.org/citations/18603531http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/18603531http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/18603531http://www.w3.org/2000/01/rdf-schema#comment"Apolipoprotein A-V (apoA-V) is present in low amounts in plasma and has been found to modulate triacylglycerol levels in humans and in animal models. ApoA-V displays affinity for members of the low density lipoprotein receptor (LDL-R) gene family, known as the classical lipoprotein receptors, including LRP1 and SorLA/LR11. In addition to LDL-A binding repeats, the mosaic receptor SorLA/LR11 also possesses a Vps10p domain. Here we show that apoA-V also binds to sortilin, a receptor from the Vsp10p domain gene family that lacks LDL-A repeats. Binding of apoA-V to sortilin was competed by neurotensin, a ligand that binds specifically to the Vps10p domain. To investigate the biological fate of receptor-bound apoA-V, binding experiments were conducted with cultured human embryonic kidney cells transfected with either SorLA/LR11 or sortilin. Compared with nontransfected cells, apoA-V binding to SorLA/LR11- and sortilin-expressing cells was markedly enhanced. Internalization experiments, live imaging studies, and fluorescence resonance energy transfer analyses demonstrated that labeled apoA-V was rapidly internalized, co-localized with receptors in early endosomes, and followed the receptors through endosomes to the trans-Golgi network. The observed decrease of fluorescence signal intensity as a function of time during live imaging experiments suggested ligand uncoupling in endosomes with subsequent delivery to lysosomes for degradation. This interpretation was supported by experiments with (125)I-labeled apoA-V, demonstrating clear differences in degradation between transfected and nontransfected cells. We conclude that apoA-V binds to receptors possessing LDL-A repeats and Vsp10p domains and that apoA-V is internalized into cells via these receptors. This could be a mechanism by which apoA-V modulates lipoprotein metabolism in vivo."xsd:string
http://purl.uniprot.org/citations/18603531http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m802721200"xsd:string
http://purl.uniprot.org/citations/18603531http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m802721200"xsd:string
http://purl.uniprot.org/citations/18603531http://purl.uniprot.org/core/author"Christensen S."xsd:string
http://purl.uniprot.org/citations/18603531http://purl.uniprot.org/core/author"Christensen S."xsd:string
http://purl.uniprot.org/citations/18603531http://purl.uniprot.org/core/author"Nielsen M.S."xsd:string
http://purl.uniprot.org/citations/18603531http://purl.uniprot.org/core/author"Nielsen M.S."xsd:string
http://purl.uniprot.org/citations/18603531http://purl.uniprot.org/core/author"Olivecrona G."xsd:string
http://purl.uniprot.org/citations/18603531http://purl.uniprot.org/core/author"Olivecrona G."xsd:string
http://purl.uniprot.org/citations/18603531http://purl.uniprot.org/core/author"Ryan R.O."xsd:string
http://purl.uniprot.org/citations/18603531http://purl.uniprot.org/core/author"Ryan R.O."xsd:string
http://purl.uniprot.org/citations/18603531http://purl.uniprot.org/core/author"Nilsson S.K."xsd:string
http://purl.uniprot.org/citations/18603531http://purl.uniprot.org/core/author"Nilsson S.K."xsd:string
http://purl.uniprot.org/citations/18603531http://purl.uniprot.org/core/author"Raarup M.K."xsd:string
http://purl.uniprot.org/citations/18603531http://purl.uniprot.org/core/author"Raarup M.K."xsd:string
http://purl.uniprot.org/citations/18603531http://purl.uniprot.org/core/date"2008"xsd:gYear
http://purl.uniprot.org/citations/18603531http://purl.uniprot.org/core/date"2008"xsd:gYear
http://purl.uniprot.org/citations/18603531http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/18603531http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/18603531http://purl.uniprot.org/core/pages"25920-25927"xsd:string
http://purl.uniprot.org/citations/18603531http://purl.uniprot.org/core/pages"25920-25927"xsd:string
http://purl.uniprot.org/citations/18603531http://purl.uniprot.org/core/title"Endocytosis of apolipoprotein A-V by members of the low density lipoprotein receptor and the VPS10p domain receptor families."xsd:string
http://purl.uniprot.org/citations/18603531http://purl.uniprot.org/core/title"Endocytosis of apolipoprotein A-V by members of the low density lipoprotein receptor and the VPS10p domain receptor families."xsd:string
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