Analysis of the glycosaminoglycan chains of proteoglycans

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Authors
Song, Yuefan
Zhang, Fuming
Linhardt, Robert J.
Issue Date
2021-02-01
Type
Article
Language
ENG
Keywords
Biology , Chemistry and chemical biology , Chemical and biological engineering , Biomedical engineering
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Abstract
Glycosaminoglycans (GAGs) are heterogeneous, negatively charged, macromolecules that are found in animal tissues. Based on the form of component sugar, GAGs have been categorized into four different families: heparin/heparan sulfate, chondroitin/dermatan sulfate, keratan sulfate, and hyaluronan. GAGs engage in biological pathway regulation through their interaction with protein ligands. Detailed structural information on GAG chains is required to further understanding of GAG–ligand interactions. However, polysaccharide sequencing has lagged behind protein and DNA sequencing due to the non-template-driven biosynthesis of glycans. In this review, we summarize recent progress in the analysis of GAG chains, specifically focusing on techniques related to mass spectroscopy (MS), including separation techniques coupled to MS, tandem MS, and bioinformatics software for MS spectrum interpretation. Progress in the use of other structural analysis tools, such as nuclear magnetic resonance (NMR) and hyphenated techniques, is included to provide a comprehensive perspective.
Description
Journal of Histochemistry & Cytochemistry, 69, 121 –135
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Full Citation
Analysis of the glycosaminoglycan chains of proteoglycans, Y. Song, F. Zhang, R. J. Linhardt, Journal of Histochemistry & Cytochemistry, 69, 121 –135, 2021.
Publisher
Sage
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Volume
Issue
PubMed ID
DOI
ISSN
15515044
221554
EISSN