| pubmed-article:18507396 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:18507396 | lifeskim:mentions | umls-concept:C0035820 | lld:lifeskim |
| pubmed-article:18507396 | lifeskim:mentions | umls-concept:C0019143 | lld:lifeskim |
| pubmed-article:18507396 | lifeskim:mentions | umls-concept:C0011602 | lld:lifeskim |
| pubmed-article:18507396 | lifeskim:mentions | umls-concept:C0003595 | lld:lifeskim |
| pubmed-article:18507396 | lifeskim:mentions | umls-concept:C0597298 | lld:lifeskim |
| pubmed-article:18507396 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
| pubmed-article:18507396 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
| pubmed-article:18507396 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
| pubmed-article:18507396 | lifeskim:mentions | umls-concept:C0597731 | lld:lifeskim |
| pubmed-article:18507396 | lifeskim:mentions | umls-concept:C2603343 | lld:lifeskim |
| pubmed-article:18507396 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
| pubmed-article:18507396 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
| pubmed-article:18507396 | lifeskim:mentions | umls-concept:C1707271 | lld:lifeskim |
| pubmed-article:18507396 | pubmed:issue | 25 | lld:pubmed |
| pubmed-article:18507396 | pubmed:dateCreated | 2010-3-24 | lld:pubmed |
| pubmed-article:18507396 | pubmed:abstractText | 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. | lld:pubmed |
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| pubmed-article:18507396 | pubmed:language | eng | lld:pubmed |
| pubmed-article:18507396 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18507396 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:18507396 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:18507396 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:18507396 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:18507396 | pubmed:issn | 1520-4995 | lld:pubmed |
| pubmed-article:18507396 | pubmed:author | pubmed-author:Lund-KatzSiss... | lld:pubmed |
| pubmed-article:18507396 | pubmed:author | pubmed-author:PhillipsMicha... | lld:pubmed |
| pubmed-article:18507396 | pubmed:author | pubmed-author:TanakaMasafum... | lld:pubmed |
| pubmed-article:18507396 | pubmed:author | pubmed-author:SaitoHiroyuki... | lld:pubmed |
| pubmed-article:18507396 | pubmed:author | pubmed-author:NakanoMinoruM | lld:pubmed |
| pubmed-article:18507396 | pubmed:author | pubmed-author:HandaTetsurou... | lld:pubmed |
| pubmed-article:18507396 | pubmed:author | pubmed-author:YamauchiYukoY | lld:pubmed |
| pubmed-article:18507396 | pubmed:author | pubmed-author:DhanasekaranP... | lld:pubmed |
| pubmed-article:18507396 | pubmed:author | pubmed-author:TakagiChikaC | lld:pubmed |
| pubmed-article:18507396 | pubmed:author | pubmed-author:DeguchiNoriko... | lld:pubmed |
| pubmed-article:18507396 | pubmed:issnType | Electronic | lld:pubmed |
