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Isolation and characterization of low sulfated heparan sulfate sequences with affinity for lipoprotein lipase
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Medical Biochemistry and Microbiology.
2006 (English)In: Journal of Biological Chemistry, ISSN 0021-9258, E-ISSN 1083-351X, Vol. 281, no 33, 23405-23413 p.Article in journal (Refereed) Published
Abstract [en]

Lipoprotein lipase (LPL), which is an important enzyme in lipid metabolism, binds to heparan sulfate (HS) proteoglycans. This interaction is crucial for several aspects of LPL function, such as intracellular/ extracellular transport and high capacity attachment to cell surfaces. Retention of LPL on the capillary walls, and elsewhere, via HS chains is most likely affected by the quality and quantity of HS present. Earlier studies have demonstrated that LPL interacts with highly sulfated HS and heparin oligosaccharides. Since such structures are relatively rare in endothelial HS, we have re-addressed the question of physiological ligand structures for LPL by affinity purification of endlabeled oligosaccharides originating from heparin and HS on immobilized LPL. By a combination of chemical modification and fragmentation of the bound material we identified that the bound fraction contained modestly sulfated oligosaccharides with an average sulfation of one O-sulfate per disaccharide unit and tolerates N-acetylated glucosamine residues. Therefore LPL, containing several clusters of positive charges on each subunit, may constitute an ideal structure for a protein that needs to bind with reasonable affinity to a variety of modestly sulfated sequences of the type that is abundant in HS chains.

Place, publisher, year, edition, pages
2006. Vol. 281, no 33, 23405-23413 p.
National Category
Medical and Health Sciences
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URN: urn:nbn:se:uu:diva-22420DOI: 10.1074/jbc.M604702200ISI: 000239702900015PubMedID: 16782967OAI: oai:DiVA.org:uu-22420DiVA: diva2:50193
Available from: 2007-01-17 Created: 2007-01-17 Last updated: 2017-12-07Bibliographically approved

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Spillmann, Dorothe

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