RDF/XMLNTriplesTurtleShow queryShare
SubjectPredicateObject
http://purl.uniprot.org/citations/18507396http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/18507396http://www.w3.org/2000/01/rdf-schema#comment"The ability of apolipoprotein E (apoE) to bind to cell-surface glycosaminoglycans (GAGs) is important for lipoprotein remnant catabolism. Using surface plasmon resonance, we previously showed that the binding of apoE to heparin is a two-step process; the initial binding involves fast electrostatic interaction, followed by a slower hydrophobic interaction. Here we examined the contributions of the N- and C-terminal domains to each step of the binding of apoE isoforms to heparan sulfate (HS) and dermatan sulfate (DS). ApoE3 bound to less sulfated HS and DS with a decreased favorable free energy of binding in the first step compared to heparin, indicating that the degree of sulfation has a major effect on the electrostatic interaction of GAGs with apoE. Mutation of a key Lys residue in the N-terminal heparin binding site of apoE significantly affected this electrostatic interaction. Progressive truncation of the C-terminal alpha-helical regions which favors the monomeric form of apoE3 greatly weakened the ability of apoE3 to bind to HS, with a much reduced favorable free energy of binding of the first step, suggesting that the C-terminal domain contributes to the GAG binding of apoE by the oligomerization effect. In agreement with this, dimerization of the apoE3 N-terminal fragment via disulfide linkage restored the electrostatic interaction of apoE with HS. Significantly, apoE4 exhibited much stronger binding to HS and DS than apoE2 or apoE3 in both lipid-free and lipidated states, perhaps resulting from enhanced electrostatic interaction through the N-terminal domain. This isoform difference in GAG binding of apoE may be physiologically significant such as in the retention of apoE-containing lipoproteins in the arterial wall."xsd:string
http://purl.uniprot.org/citations/18507396http://purl.org/dc/terms/identifier"doi:10.1021/bi8003999"xsd:string
http://purl.uniprot.org/citations/18507396http://purl.uniprot.org/core/author"Nakano M."xsd:string
http://purl.uniprot.org/citations/18507396http://purl.uniprot.org/core/author"Saito H."xsd:string
http://purl.uniprot.org/citations/18507396http://purl.uniprot.org/core/author"Tanaka M."xsd:string
http://purl.uniprot.org/citations/18507396http://purl.uniprot.org/core/author"Yamauchi Y."xsd:string
http://purl.uniprot.org/citations/18507396http://purl.uniprot.org/core/author"Takagi C."xsd:string
http://purl.uniprot.org/citations/18507396http://purl.uniprot.org/core/author"Handa T."xsd:string
http://purl.uniprot.org/citations/18507396http://purl.uniprot.org/core/author"Deguchi N."xsd:string
http://purl.uniprot.org/citations/18507396http://purl.uniprot.org/core/author"Lund-Katz S."xsd:string
http://purl.uniprot.org/citations/18507396http://purl.uniprot.org/core/author"Phillips M.C."xsd:string
http://purl.uniprot.org/citations/18507396http://purl.uniprot.org/core/author"Dhanasekaran P."xsd:string
http://purl.uniprot.org/citations/18507396http://purl.uniprot.org/core/date"2008"xsd:gYear
http://purl.uniprot.org/citations/18507396http://purl.uniprot.org/core/name"Biochemistry"xsd:string
http://purl.uniprot.org/citations/18507396http://purl.uniprot.org/core/pages"6702-6710"xsd:string
http://purl.uniprot.org/citations/18507396http://purl.uniprot.org/core/title"Role of the N- and C-terminal domains in binding of apolipoprotein E isoforms to heparan sulfate and dermatan sulfate: a surface plasmon resonance study."xsd:string
http://purl.uniprot.org/citations/18507396http://purl.uniprot.org/core/volume"47"xsd:string
http://purl.uniprot.org/citations/18507396http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/18507396
http://purl.uniprot.org/citations/18507396http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/18507396
http://purl.uniprot.org/uniprot/#_A0A0S2Z3B1-mappedCitation-18507396http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/18507396
http://purl.uniprot.org/uniprot/#_A0A0S2Z3V0-mappedCitation-18507396http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/18507396
http://purl.uniprot.org/uniprot/#_A0A0S2Z3D5-mappedCitation-18507396http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/18507396
http://purl.uniprot.org/uniprot/#_A0A0S2Z3J5-mappedCitation-18507396http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/18507396
http://purl.uniprot.org/uniprot/#_A0A346DBY2-mappedCitation-18507396http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/18507396