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Drosophila heparan sulfate: a novel design
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Medical Biochemistry and Microbiology.
2012 (English)In: Journal of Biological Chemistry, ISSN 0021-9258, E-ISSN 1083-351X, Vol. 287, no 26, 21950-21956 p.Article in journal (Refereed) Published
Abstract [en]

Heparan sulfate (HS) proteoglycans play critical roles in a wide variety of biological processes such as growth factor signaling, cell adhesion, wound healing, and tumor metastasis. Functionally important interactions between HS and a variety of proteins depend on specific structural features within the HS chains. The fruit fly (Drosophila melanogaster) is frequently applied as a model organism to study HS function in development. Previous structural studies of Drosophila HS have been restricted to disaccharide composition, without regard to the arrangement of saccharide domains typically found in vertebrate HS. Here, we biochemically characterized Drosophila HS by selective depolymerization with nitrous acid. Analysis of the generated saccharide products revealed a novel HS design, involving a peripheral, extended, presumably single, N-sulfated domain linked to an N-acetylated sequence contiguous with the linkage to core protein. The N-sulfated domain may be envisaged as a heparin structure of unusually low O-sulfate content.

Place, publisher, year, edition, pages
2012. Vol. 287, no 26, 21950-21956 p.
National Category
Natural Sciences
URN: urn:nbn:se:uu:diva-194282DOI: 10.1074/jbc.M112.350389ISI: 000306418600034PubMedID: 22556423OAI: oai:DiVA.org:uu-194282DiVA: diva2:604793
Available from: 2013-02-12 Created: 2013-02-12 Last updated: 2015-05-26Bibliographically approved

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Lindahl, Ulf
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