Heparan Sulfate Structure: Methods to Study N-Sulfation and NDST ActionShow others and affiliations
2015 (English)In: Methods in Molecular Biology, ISSN 1064-3745, E-ISSN 1940-6029, Vol. 1229, p. 189-200Article in journal (Refereed) Published
Abstract [en]
Heparan sulfate proteoglycans are important modulators of cellular processes where the negatively charged polysaccharide chains interact with target proteins. The sulfation pattern of the heparan sulfate chains will determine the proteins that will bind and the affinity of the interactions. The N-deacetylase/N-sulfotransferase (NDST) enzymes are of key importance during heparan sulfate biosynthesis when the sulfation pattern is determined. In this chapter, metabolic labeling of heparan sulfate with [35S]sulfate or [3H]glucosamine in cell cultures is described, in addition to characterization of polysaccharide chain length and degree of N-sulfation. Methods to measure NDST enzyme activity are also presented.
Place, publisher, year, edition, pages
New York, NY: Humana Press, 2015. Vol. 1229, p. 189-200
National Category
Molecular Biology
Identifiers
URN: urn:nbn:se:his:diva-25810DOI: 10.1007/978-1-4939-1714-3_17ISI: 000344016200018PubMedID: 25325954Scopus ID: 2-s2.0-84921823681OAI: oai:DiVA.org:his-25810DiVA, id: diva2:1995600
Note
Artikel/Article; Kapitel i bok/Book Chapter
Glycosaminoglycans: Chemistry and Biology
Editors: Kuberan Balagurunathan, Hiroshi Nakato, Umesh R. Desai
Part of the book series: Methods in Molecular Biology (MIMB, volume 1229)
Hardcover ISBN 978-1-4939-1713-6
Softcover ISBN 978-1-4939-4696-9
eBook ISBN 978-1-4939-1714-3
2025-09-052025-09-052025-11-12Bibliographically approved