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Titolo:
The conformation of apolipoprotein A-I in high-density lipoproteins is influenced by core lipid composition and particle size: A surface plasmon resonance study
Autore:
Curtiss, LK; Bonnet, DJ; Rye, KA;
Indirizzi:
Scripps Clin & Res Inst, Dept Immunol, La Jolla, CA 92037 USA Scripps Clin& Res Inst La Jolla CA USA 92037 nol, La Jolla, CA 92037 USA Scripps Clin & Res Inst, Dept Vasc Biol, La Jolla, CA 92037 USA Scripps Clin & Res Inst La Jolla CA USA 92037 iol, La Jolla, CA 92037 USA Hanson Ctr, Lipid Res Lab, Adelaide, SA 5000, Australia Hanson Ctr Adelaide SA Australia 5000 s Lab, Adelaide, SA 5000, Australia
Titolo Testata:
BIOCHEMISTRY
fascicolo: 19, volume: 39, anno: 2000,
pagine: 5712 - 5721
SICI:
0006-2960(20000516)39:19<5712:TCOAAI>2.0.ZU;2-G
Fonte:
ISI
Lingua:
ENG
Soggetto:
LECITHIN-CHOLESTEROL ACYLTRANSFERASE; ESTER TRANSFER PROTEIN; MONOCLONAL-ANTIBODIES; BINDING-KINETICS; LOCALIZATION; IDENTIFICATION; HETEROGENEITY; SUBFRACTIONS; ASSOCIATION; ACTIVATION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
33
Recensione:
Indirizzi per estratti:
Indirizzo: Curtiss, LK Scripps Clin & Res Inst, Dept Immunol, 10550 N Torrey Pines Rd, La Jolla, CA 92037 USA Scripps Clin & Res Inst 10550 N Torrey Pines Rd LaJolla CA USA 92037
Citazione:
L.K. Curtiss et al., "The conformation of apolipoprotein A-I in high-density lipoproteins is influenced by core lipid composition and particle size: A surface plasmon resonance study", BIOCHEM, 39(19), 2000, pp. 5712-5721

Abstract

Plasma high-density lipoproteins (HDL) are a heterogeneous group of particles that vary in size as well as lipid and apoprotein composition. The effect of HDL core lipid composition and particle site on apolipoprotein (apo) A-I structure was studied using surface plasmon resonance (SPR) analysis ofthe binding of epitope-defined monoclonal antibodies. The association and dissociation rate constants of 12 unique apo A-I-specific monoclonal antibodies for isolated plasma HDL were calculated. In addition, the association rate constants of the antibodies were determined for homogeneous preparations of spherical reconstituted HDL (rHDL) that contained apo A-I as the soleapolipoprotein and differed either in their size or in their core lipid composition. This analysis showed that lipoprotein size affected the conformation of domains dispersed throughout the apo A-I molecule, but the conformation of the central domain between residues 121 and 165 was most consistently modified. In contrast, replacement of core cholesteryl esters with triglyceride in small HDL modified almost the entire molecule, with only two keyN-terminal domains of apo A-I being unaffected. This finding suggested that the central and C-terminal domains of apo A-I are in direct contact with rHDL core lipids. This immunochemical analysis has provided valuable insight into how core lipid composition and particle size affect the structure ofspecific domains of apo A-I on HDL.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 28/03/20 alle ore 13:43:59