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J. Biol. Chem., Vol. 281, Issue 33, 23405-23413, August 18, 2006

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Isolation and Characterization of Low Sulfated Heparan Sulfate Sequences with Affinity for Lipoprotein Lipase^*

Dorothe Spillmann¹, Aivar Lookene^¶, and Gunilla Olivecrona

From the Department of Medical Biochemistry and Microbiology, University of Uppsala, SE-751 23 Uppsala, Sweden, the Department of Medical Biosciences/Physiological Chemistry, Umeå University, SE-901 87 Umeå, Sweden, and the ^¶Department of Gene Technology, Tallinn Technical University, Tallinn 12618, Estonia

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 end-labeled 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.

Received for publication, May 16, 2006 , and in revised form, June 16, 2006.

^* This work was supported by The Swedish Research Council (Grants 15023 and 12203), The Swedish Foundation for Strategic Research (A303:156e), the Swedish Cancer Society (4708-B02-01XAA), and Polysackaridforskning AB. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

¹ To whom correspondence should be addressed: Dept. of Medical Biochemistry and Microbiology, The Biomedical Centre, University of Uppsala, Box 582, SE-751 23 Uppsala, Sweden. Tel.: 46-18-471-4367; Fax: 46-471-4209; E-mail: Dorothe.Spillmann{at}imbim.uu.se.

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