Issue 32, 2017

Insights into the role of 3-O-sulfotransferase in heparan sulfate biosynthesis

Abstract

3-O-Sulfotransferase enzyme (sHS) from Litopenaeus vannamei was cloned and its substrate specificity was investigated against a number of GAG structures, including modified heparin polysaccharides and model oligosaccharides. For the heparin polysaccharides, derived from porcine intestinal mucosa heparin, sulfate groups were incorporated into glucosamine residues containing both N-sulfated and N-acetylated substitution within the regions of the predominant repeating disaccharide, either I–ANS or I–ANAc. However, the resulting polysaccharides did not stabilize antithrombin, which is correlated with anticoagulant activity. It was also shown that the enzyme was able to sulfate disaccharides, I2S–ANS and G–ANAc. The results further illustrate that 3-O-sulfation can be induced outside of the classical heparin-binding pentasaccharide sequence, show that 3-O-sulfation of glucosamine is not a sufficient condition for antithrombin stabilization and suggest that the use of this enzyme during HS biosynthesis may not occur as the final enzymatic step.

Graphical abstract: Insights into the role of 3-O-sulfotransferase in heparan sulfate biosynthesis

Supplementary files

Article information

Article type
Paper
Submitted
23 jun 2017
Accepted
27 jul 2017
First published
27 jul 2017

Org. Biomol. Chem., 2017,15, 6792-6799

Insights into the role of 3-O-sulfotransferase in heparan sulfate biosynthesis

M. C. Z. Meneghetti, T. Gesteira Ferreira, A. K. Tashima, S. F. Chavante, E. A. Yates, J. Liu, H. B. Nader and M. A. Lima, Org. Biomol. Chem., 2017, 15, 6792 DOI: 10.1039/C7OB01533J

To request permission to reproduce material from this article, please go to the Copyright Clearance Center request page.

If you are an author contributing to an RSC publication, you do not need to request permission provided correct acknowledgement is given.

If you are the author of this article, you do not need to request permission to reproduce figures and diagrams provided correct acknowledgement is given. If you want to reproduce the whole article in a third-party publication (excluding your thesis/dissertation for which permission is not required) please go to the Copyright Clearance Center request page.

Read more about how to correctly acknowledge RSC content.

Social activity

Spotlight

Advertisements