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
  • 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 (2010)
    Estradiol binding prevents ApoB-100 misfolding in electronegative LDL(-)
    in Biochemistry (Easton)
    (literal)
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)
Pagina inizio
  • 7297 (literal)
Pagina fine
  • 7302 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 49 (literal)
Rivista
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo
  • 34 (literal)
Note
  • ISI Web of Science (WOS) (literal)
  • PubMe (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • 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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