Analysis of the Glycosaminoglycan Chains of Proteoglycans.
NMR
glycosaminoglycans
mass spectroscopy
sequencing
structural analysis
Journal
The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society
ISSN: 1551-5044
Titre abrégé: J Histochem Cytochem
Pays: United States
ID NLM: 9815334
Informations de publication
Date de publication:
02 2021
02 2021
Historique:
pubmed:
7
7
2020
medline:
25
8
2021
entrez:
7
7
2020
Statut:
ppublish
Résumé
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.
Identifiants
pubmed: 32623943
doi: 10.1369/0022155420937154
pmc: PMC7841699
doi:
Substances chimiques
Glycosaminoglycans
0
Proteoglycans
0
Types de publication
Journal Article
Review
Langues
eng
Sous-ensembles de citation
IM
Pagination
121-135Subventions
Organisme : NIDDK NIH HHS
ID : R01 DK111958
Pays : United States
Organisme : NCI NIH HHS
ID : U01 CA231074
Pays : United States
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