Source:http://linkedlifedata.com/resource/pubmed/id/11076531
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
45
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pubmed:dateCreated |
2000-11-30
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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.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/2-Naphthylamine,
http://linkedlifedata.com/resource/pubmed/chemical/Antioxidants,
http://linkedlifedata.com/resource/pubmed/chemical/Apolipoprotein B-100,
http://linkedlifedata.com/resource/pubmed/chemical/Apolipoproteins B,
http://linkedlifedata.com/resource/pubmed/chemical/Estradiol,
http://linkedlifedata.com/resource/pubmed/chemical/Fluorescent Dyes,
http://linkedlifedata.com/resource/pubmed/chemical/Free Radical Scavengers,
http://linkedlifedata.com/resource/pubmed/chemical/Laurates,
http://linkedlifedata.com/resource/pubmed/chemical/Lipoproteins, LDL,
http://linkedlifedata.com/resource/pubmed/chemical/Tryptophan,
http://linkedlifedata.com/resource/pubmed/chemical/laurdan
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0006-2960
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
14
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pubmed:volume |
39
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pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
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pubmed:pagination |
13897-903
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:11076531-2-Naphthylamine,
pubmed-meshheading:11076531-Antioxidants,
pubmed-meshheading:11076531-Apolipoprotein B-100,
pubmed-meshheading:11076531-Apolipoproteins B,
pubmed-meshheading:11076531-Circular Dichroism,
pubmed-meshheading:11076531-Estradiol,
pubmed-meshheading:11076531-Fluorescence Polarization,
pubmed-meshheading:11076531-Fluorescent Dyes,
pubmed-meshheading:11076531-Free Radical Scavengers,
pubmed-meshheading:11076531-Humans,
pubmed-meshheading:11076531-Laurates,
pubmed-meshheading:11076531-Lipid Peroxidation,
pubmed-meshheading:11076531-Lipoproteins, LDL,
pubmed-meshheading:11076531-Protein Conformation,
pubmed-meshheading:11076531-Spectrometry, Fluorescence,
pubmed-meshheading:11076531-Tryptophan
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pubmed:year |
2000
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pubmed:articleTitle |
Estradiol enhances the resistance of LDL to oxidation by stabilizing apoB-100 conformation.
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pubmed:affiliation |
I and II Clinica Ostetrica e Ginecologica, Universitá di Roma La Sapienza, Viale del Policlinico 155, 00185 Roma, Italy.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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