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  • 1. Siegel, G
    et al.
    Malmsten, M
    YKI – Ytkemiska institutet.
    Klüssendorf, D
    Leonhardt, W
    Physicochemical binding properties of the proteoglycan receptor for serum lipoproteins1999In: Atherosclerosis, ISSN 0021-9150, E-ISSN 1879-1484, Vol. 144, p. 59-67Article in journal (Refereed)
    Abstract [en]

    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 polysugar side chains are stretched out into the blood substitute solution representing a co-receptor for specific lipoprotein binding through basic amino acid-rich residues within their apolipoproteins. The binding process was studied by ellipsometric techniques showing that oxLDL had a deleterious effect on heparan sulfate proteoglycan binding and conformation. Ca2+ binding to and storage on the proteoheparan sulfate/LDL compound formed a 'heterotrimeric' HS-PG/LDL/Ca2+ complex of high stability, aggregability and deposit coating. On the other hand, HDL bound to heparan sulfate proteoglycan protected against LDL docking and completely suppressed calcification of the proteoglycan/lipoprotein complex.

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