Identification of Keratan Sulfate Disaccharide Unit at the C-3 position of Glucuronic Acid of Chondroitin Sulfate from Mactra chinensis

Authors
Higashi, K.
Takeda, Keita
Mukuno, A.
Okamoto, Y.
Masuko, S.
Linhardt, Robert J.
Toida, T.
ORCID
https://orcid.org/0000-0003-2219-5833
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Issue Date
2016
Keywords
Biology , Chemistry and chemical biology , Chemical and biological engineering , Biomedical engineering
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Terms of Use
Attribution-NonCommercial-NoDerivs 3.0 United States
CC BY-NC-ND : this license allows reusers to copy and distribute the material in any medium or format in unadapted form only, for noncommercial purposes only, and only so long as attribution is given to the creator.
Full Citation
Identification of Keratan Sulfate Disaccharide Unit at the C-3 position of Glucuronic Acid of Chondroitin Sulfate from Mactra chinensis, K. Higashi, K. Takeda, A. Mukuno, Y. Okamoto, S. Masuko, R. J. Linhardt, T. Toida, Biochemical Journal, 473 4145–4158, 2016.
Abstract
Glycosaminoglycans (GAGs), including chondroitin sulfate (CS), dermatan sulfate, heparin, heparan sulfate and keratan sulfate (KS) are linear sulfated repeating disaccharide sequences containing hexosamine and uronic acid [or galactose (Gal) in the case of KS]. Among the GAGs, CS shows structural variations, such as sulfation patterns and fucosylation, which are responsible for their physiological functions through CS interaction with CS-binding proteins. Here, we solved the structure of KS-branched CS-E derived from a clam, Mactra chinensis. KS disaccharide [d-GlcNAc6S-(1→3)-β-d-Gal-(1→] was attached to the C-3 position of GlcA, and consecutive KS-branched disaccharide sequences were found in a CS chain. KS-branched polysaccharides clearly exhibited resistance to degradation by chondroitinase ABC or ACII (at low concentrations) compared with typical CS structures. Furthermore, KS-branched polysaccharides stimulated neurite outgrowth of hippocampal neurons. These results strongly suggest that M. chinensis is a rich source of KS-branched CS, and it has important biological activities.
Description
Biochemical Journal, 473 4145–4158
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Department
The Linhardt Research Labs.
The Shirley Ann Jackson, Ph.D. Center for Biotechnology and Interdisciplinary Studies (CBIS)
Publisher
Portland Press Limited
Relationships
The Linhardt Research Labs Online Collection
Rensselaer Polytechnic Institute, Troy, NY
https://harc.rpi.edu/
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A full text version is available in DSpace@RPI
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CC BY-NC-ND — Creative Commons Attribution-NonCommercial-NoDerivatives