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Physicochemical binding properties of the proteoglycan receptor for serum lipoproteins
YKI – Ytkemiska institutet.
1999 (English)In: Atherosclerosis, ISSN 0021-9150, E-ISSN 1879-1484, Vol. 144, 59-67 p.Article 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.

Place, publisher, year, edition, pages
1999. Vol. 144, 59-67 p.
Keyword [en]
Ellipsometry, methylated silica surface, heparan sulfate proteoglycan, scavenger receptor, lipoprotein binding, calcification
National Category
Natural Sciences
Identifiers
URN: urn:nbn:se:ri:diva-26304OAI: oai:DiVA.org:ri-26304DiVA: diva2:1053306
Note
A1313Available from: 2016-12-08 Created: 2016-12-08Bibliographically approved

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