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Heparan Sulfate Structure: Methods to Study N-Sulfation and NDST Action

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Glycosaminoglycans

Part of the book series: Methods in Molecular Biology ((MIMB,volume 2303))

Abstract

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 which proteins 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.

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Correspondence to Lena Kjellén .

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Dagälv, A., Lundequist, A., Filipek-Górniok, B., Dierker, T., Eriksson, I., Kjellén, L. (2022). Heparan Sulfate Structure: Methods to Study N-Sulfation and NDST Action. In: Balagurunathan, K., Nakato, H., Desai, U., Saijoh, Y. (eds) Glycosaminoglycans. Methods in Molecular Biology, vol 2303. Humana, New York, NY. https://doi.org/10.1007/978-1-0716-1398-6_12

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  • DOI: https://doi.org/10.1007/978-1-0716-1398-6_12

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  • Publisher Name: Humana, New York, NY

  • Print ISBN: 978-1-0716-1397-9

  • Online ISBN: 978-1-0716-1398-6

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