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Titolo:
A receptor-based biosensor for lipoprotein docking at the endothelial surface and vascular matrix
Autore:
Siegel, G; Malmsten, M; Klussendorf, D; Michel, F;
Indirizzi:
Free Univ Berlin, Inst Physiol, Biophys Res Grp, D-14195 Berlin, Germany Free Univ Berlin Berlin Germany D-14195 Res Grp, D-14195 Berlin, Germany Inst Surface Chem, SE-11486 Stockholm, Sweden Inst Surface Chem Stockholm Sweden SE-11486 , SE-11486 Stockholm, Sweden
Titolo Testata:
BIOSENSORS & BIOELECTRONICS
fascicolo: 9-12, volume: 16, anno: 2001,
pagine: 895 - 904
SICI:
0956-5663(200112)16:9-12<895:ARBFLD>2.0.ZU;2-L
Fonte:
ISI
Lingua:
ENG
Soggetto:
HEPARAN-SULFATE PROTEOGLYCANS; SILICA WATER INTERFACE; PROTEOHEPARAN SULFATE; ANIONIC BIOPOLYMERS; DENSITY-LIPOPROTEINS; HYDROPHOBIC SURFACES; PLASMA-LIPOPROTEINS; PROTEIN ADSORPTION; BLOOD INTERFACE; ELLIPSOMETRY;
Keywords:
proteoglycan receptor; lipoproteins; calcification; drugs; arteriosclerosis model;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Agriculture,Biology & Environmental Sciences
Citazioni:
48
Recensione:
Indirizzi per estratti:
Indirizzo: Siegel, G Free Univ Berlin, Inst Physiol, Biophys Res Grp, Arnimallee 22, D-14195 Berlin, Germany Free Univ Berlin Arnimallee 22 Berlin Germany D-14195 , Germany
Citazione:
G. Siegel et al., "A receptor-based biosensor for lipoprotein docking at the endothelial surface and vascular matrix", BIOSENS BIO, 16(9-12), 2001, pp. 895-904

Abstract

Proteoheparan sulfate can be adsorbed to a methylated silica surface in a monomolecular layer via its transmembrane hydrophobic protein core domain. Due to electrostatic repulsion, its anionic glycosaminoglycan side chains are stretched out into the blood substitute solution, representing a receptor site for specific lipoprotein binding through basic amino acid-rich residues within their apolipoproteins. The binding process was studied by ellipsometric techniques showing that HDL has a high binding affinity to the receptor and a protective effect on interfacial heparan sulfate proteoglycan layers, with respect to LDL and Ca2+ complexation. LDL was found to deposit strongly at the proteoheparan sulfate, particularly in the presence of Ca2+,thus creating the complex formation 'proteoglycan-low density lipoprotein-calcium'. This ternary complex build-up may be interpreted as arteriosclerotic nanoplaque formation on the molecular level responsible for the arteriosclerotic primary lesion. On the other hand. HDL bound to heparan Sulfate proteoglycan protected against LDL docking and completely suppressed calcification of the proteoglycan-lipoprotein complex. In addition, HDL and aqueous garlic extract were able to reduce the ternary complex deposition and to disintegrate HS-PG/LDL/Ca2+ aggregates. Although much remains unclear regarding the mechanism of lipoprotein depositions at proteoglycan-coated surfaces, it seems clear that the use of such systems offers possibilities for investigating lipoprotein deposition at a 'nanoscopic' level under close to physiological conditions. In particular, Ca2+-promoted LDL deposition and the protective effect of HDL, even at high Ca2+ and LDL concentrations, agreewell with previous clinical observations regarding risk and beneficial factors for early stages of atherosclerosis. Therefore, we believe that the system can be of some use in investigations, e.g. of the interplay between different lipoproteins in arteriosclerotic plaque formation, as well as in high throughput screening of candidate drugs to atherosclerosis in a biosensor application. (C) 2001 Elsevier Science B.V. All rights reserved.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 20/09/20 alle ore 06:27:09