http://www.cnr.it/ontology/cnr/individuo/prodotto/ID167761
Estradiol binding prevents ApoB-100 misfolding in electronegative LDL(-) (Articolo in rivista)
- Type
- Label
- Estradiol binding prevents ApoB-100 misfolding in electronegative LDL(-) (Articolo in rivista) (literal)
- Anno
- 2010-01-01T00:00:00+01:00 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
- 10.1021/bi100715f (literal)
- Alternative label
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
- Roberto Brunelli 1; Gabor Balogh 2; Graziella Costa 3; Marco De Spirito 4; Giulia Greco 3; Giampiero Mei 5; Eleonora Nicolai 5; Laszlo Vigh 2; Fulvio Ursini 6; Tiziana Parasassi 3 (literal)
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- ISI Web of Science (WOS) (literal)
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- 1 Dipartimento di Ostetricia e Ginecologia, Università di Roma Sapienza, Roma, Italy;
2 Institute of Biochemistry, Biological Research Center, Hungarian Academy of Sciences, Szeged, Hungary;
3 Istituto di Neurobiologia e Medicina Molecolare, CNR, Roma, Italy;
4 Istituto di Fisica, Facoltà di Medicina e Chirurgia, Università Cattolica del Sacro Cuore, Roma, Italy;
5 Dipartimento di Medicina Sperimentale e Scienze Biochimiche, Università di Roma Tor Vergata, Roma, Italy;
6 Dipartimento di Chimica Biologica, Università di Padova, Padova, Italy. (literal)
- Titolo
- Estradiol binding prevents ApoB-100 misfolding in electronegative LDL(-) (literal)
- Abstract
- Seeking for a modified lipoprotein present in plasma that could account for the atherogenic effect of high cholesterol, several years ago electronegative LDL(-) was identified. The peculiar feature of LDL(-) is an apoprotein misfolding that triggers the formation of aggregates, perfectly fitting in size the subendothelial droplets observed in early phases of atherogenesis. Apoprotein misfolding was therefore proposed as a possible atherogenic modification. LDL(-) can be spontaneously produced in vitro by plasma incubation through phospholipid hydrolysis catalyzed by the activity of endogenous phospholipases. As a consequence, apoprotein is misfolded. 17beta-Estradiol (E2), a specific ligand to apoB-100, was used to unravel the relationship between negative charge of the lipoprotein and apoprotein structural/conformational shift. Although E2 addition to plasma does not prevent LDL(-) generation nor phospholipase activity, it deeply stabilizes apoB-100 structure, thus preventing its structural and conformational shift. Apoprotein stabilization extends to lipids. Indeed, while a loosening of lipid packing is observed together with apoprotein misfolding, conversely, when E2 stabilizes apoprotein, lipid structure is preserved. Finally, even in the presence of LDL(-), the E2-stabilized LDL is resistant to aggregation, unambiguously demonstrating that misfolding, but not negative charge, primes aggregation. In conclusion, electronegative charge and misfolding are independent and distinct features of LDL(-), and apoprotein misfolding rather than the increase in the negative charge emerges both as a valid biomarker and as an appealing pharmacological and nutritional target. (literal)
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