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Physicochemical bin...
Physicochemical binding properties of the proteoglycan receptor for serum lipoproteins
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Siegel, G (författare)
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- Malmsten, M (författare)
- RISE,YKI – Ytkemiska institutet
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Klüssendorf, D (författare)
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visa fler...
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Leonhardt, W (författare)
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visa färre...
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(creator_code:org_t)
- 1999
- 1999
- Engelska.
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Ingår i: Atherosclerosis. - 0021-9150 .- 1879-1484. ; 144, s. 59-67
- Relaterad länk:
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https://urn.kb.se/re...
Abstract
Ämnesord
Stäng
- 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.
Nyckelord
- Ellipsometry
- methylated silica surface
- heparan sulfate proteoglycan
- scavenger receptor
- lipoprotein binding
- calcification
Publikations- och innehållstyp
- ref (ämneskategori)
- art (ämneskategori)
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