دورية أكاديمية
Estradiol enhances the resistance of LDL to oxidation by stabilizing apoB-100 conformation.
| العنوان: | Estradiol enhances the resistance of LDL to oxidation by stabilizing apoB-100 conformation. |
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| المؤلفون: | Brunelli R; I and II Clinica Ostetrica e Ginecologica, Universitá di Roma La Sapienza, Viale del Policlinico 155, 00185 Roma, Italy., Mei G, Krasnowska EK, Pierucci F, Zichella L, Ursini F, Parasassi T |
| المصدر: | Biochemistry [Biochemistry] 2000 Nov 14; Vol. 39 (45), pp. 13897-903. |
| نوع المنشور: | Journal Article; Research Support, Non-U.S. Gov't |
| اللغة: | English |
| بيانات الدورية: | Publisher: American Chemical Society Country of Publication: United States NLM ID: 0370623 Publication Model: Print Cited Medium: Print ISSN: 0006-2960 (Print) Linking ISSN: 00062960 NLM ISO Abbreviation: Biochemistry Subsets: MEDLINE |
| أسماء مطبوعة: | Original Publication: Washington, American Chemical Society. |
| مواضيع طبية MeSH: | Lipid Peroxidation*/drug effects, 2-Naphthylamine/*analogs & derivatives , Apolipoproteins B/*chemistry , Estradiol/*chemistry , Lipoproteins, LDL/*chemistry , Lipoproteins, LDL/*metabolism, 2-Naphthylamine/chemistry ; Antioxidants/chemistry ; Antioxidants/metabolism ; Antioxidants/pharmacology ; Apolipoprotein B-100 ; Apolipoproteins B/metabolism ; Circular Dichroism ; Estradiol/metabolism ; Estradiol/pharmacology ; Fluorescence Polarization ; Fluorescent Dyes/chemistry ; Free Radical Scavengers/chemistry ; Free Radical Scavengers/metabolism ; Humans ; Laurates/chemistry ; Protein Conformation ; Spectrometry, Fluorescence ; Tryptophan/chemistry |
| مستخلص: | 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. |
| المشرفين على المادة: | 0 (Antioxidants) 0 (Apolipoprotein B-100) 0 (Apolipoproteins B) 0 (Fluorescent Dyes) 0 (Free Radical Scavengers) 0 (Laurates) 0 (Lipoproteins, LDL) 4TI98Z838E (Estradiol) 8DUH1N11BX (Tryptophan) CKR7XL41N4 (2-Naphthylamine) Y97FBL93VW (laurdan) |
| تواريخ الأحداث: | Date Created: 20001115 Date Completed: 20001228 Latest Revision: 20190613 |
| رمز التحديث: | 20240627 |
| DOI: | 10.1021/bi000341p |
| PMID: | 11076531 |
| قاعدة البيانات: | MEDLINE |
Find this issue from the American Chemical Society | تدمد: | 0006-2960 |
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| DOI: | 10.1021/bi000341p |