pubmed-article:11076531 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:11076531 | lifeskim:mentions | umls-concept:C0023823 | lld:lifeskim |
pubmed-article:11076531 | lifeskim:mentions | umls-concept:C0014912 | lld:lifeskim |
pubmed-article:11076531 | lifeskim:mentions | umls-concept:C0205666 | lld:lifeskim |
pubmed-article:11076531 | lifeskim:mentions | umls-concept:C0030011 | lld:lifeskim |
pubmed-article:11076531 | lifeskim:mentions | umls-concept:C0026377 | lld:lifeskim |
pubmed-article:11076531 | lifeskim:mentions | umls-concept:C0683598 | lld:lifeskim |
pubmed-article:11076531 | lifeskim:mentions | umls-concept:C2349975 | lld:lifeskim |
pubmed-article:11076531 | lifeskim:mentions | umls-concept:C2003913 | lld:lifeskim |
pubmed-article:11076531 | pubmed:issue | 45 | lld:pubmed |
pubmed-article:11076531 | pubmed:dateCreated | 2000-11-30 | lld:pubmed |
pubmed-article:11076531 | pubmed:abstractText | Among different proposed mechanisms to account for the protection exerted by estrogens against cardiovascular diseases, the antioxidant effect has attracted considerable attention. We confirmed that 17-beta-estradiol (E2), when added to human LDL at a 6:1 ratio to apoB-100, markedly delays the phase of massive LDL lipid peroxidation induced by Cu(2+). We also observed an increased oxidative resistance of E2-treated LDL by monitoring the early phase of oxidative degradation on the basis of increased LDL surface polarity by the generalized polarization of the lipophilic fluorescent probe 2-(dimethylamino)-6-lauroylnaphthalene (Laurdan). A scavenging of free radicals by E2 is ruled out since, consistent with its structure, its rate constant for the reduction of peroxy radicals is extremely low, i.e., 0.02% of that of vitamin E. Tryptophan fluorescence lifetime and circular dichroism measurements revealed that (i) apoB-100 undergoes a conformational modification and a progressive loss of secondary structure during lipid peroxidation; (ii) E2 increases apoB-100 secondary structure and modifies its conformation; and (iii) the apoB-100 conformational change induced by E2 makes this protein resistant to modifications brought about by lipid peroxidation. We propose that E2, by affecting apoB-100 secondary structure and conformation, modifies the interaction of this protein with the outer layer of the LDL particle thus increasing its overall oxidative resistance. | lld:pubmed |
pubmed-article:11076531 | pubmed:language | eng | lld:pubmed |
pubmed-article:11076531 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11076531 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:11076531 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11076531 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11076531 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11076531 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11076531 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11076531 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11076531 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11076531 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11076531 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11076531 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11076531 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11076531 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:11076531 | pubmed:month | Nov | lld:pubmed |
pubmed-article:11076531 | pubmed:issn | 0006-2960 | lld:pubmed |
pubmed-article:11076531 | pubmed:author | pubmed-author:ZichellaLL | lld:pubmed |
pubmed-article:11076531 | pubmed:author | pubmed-author:UrsiniFF | lld:pubmed |
pubmed-article:11076531 | pubmed:author | pubmed-author:BrunelliRR | lld:pubmed |
pubmed-article:11076531 | pubmed:author | pubmed-author:ParasassiTT | lld:pubmed |
pubmed-article:11076531 | pubmed:author | pubmed-author:PierucciFF | lld:pubmed |
pubmed-article:11076531 | pubmed:author | pubmed-author:MeoAA | lld:pubmed |
pubmed-article:11076531 | pubmed:author | pubmed-author:KrasnowskaE... | lld:pubmed |
pubmed-article:11076531 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:11076531 | pubmed:day | 14 | lld:pubmed |
pubmed-article:11076531 | pubmed:volume | 39 | lld:pubmed |
pubmed-article:11076531 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:11076531 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:11076531 | pubmed:pagination | 13897-903 | lld:pubmed |
pubmed-article:11076531 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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pubmed-article:11076531 | pubmed:year | 2000 | lld:pubmed |
pubmed-article:11076531 | pubmed:articleTitle | Estradiol enhances the resistance of LDL to oxidation by stabilizing apoB-100 conformation. | lld:pubmed |
pubmed-article:11076531 | pubmed:affiliation | I and II Clinica Ostetrica e Ginecologica, Universitá di Roma La Sapienza, Viale del Policlinico 155, 00185 Roma, Italy. | lld:pubmed |
pubmed-article:11076531 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:11076531 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:11076531 | lld:pubmed |