Cargando…
Keratan sulfate, a complex glycosaminoglycan with unique functional capability
From an evolutionary perspective keratan sulfate (KS) is the newest glycosaminoglycan (GAG) but the least understood. KS is a sophisticated molecule with a diverse structure, and unique functional roles continue to be uncovered for this GAG. The cornea is the richest tissue source of KS in the human...
Autores principales: | , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2018
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5993099/ https://www.ncbi.nlm.nih.gov/pubmed/29340594 http://dx.doi.org/10.1093/glycob/cwy003 |
_version_ | 1783330171623833600 |
---|---|
author | Caterson, Bruce Melrose, James |
author_facet | Caterson, Bruce Melrose, James |
author_sort | Caterson, Bruce |
collection | PubMed |
description | From an evolutionary perspective keratan sulfate (KS) is the newest glycosaminoglycan (GAG) but the least understood. KS is a sophisticated molecule with a diverse structure, and unique functional roles continue to be uncovered for this GAG. The cornea is the richest tissue source of KS in the human body but the central and peripheral nervous systems also contain significant levels of KS and a diverse range of KS-proteoglycans with essential functional roles. KS also displays important cell regulatory properties in epithelial and mesenchymal tissues and in bone and in tumor development of diagnostic and prognostic utility. Corneal KS-I displays variable degrees of sulfation along the KS chain ranging from non-sulfated polylactosamine, mono-sulfated and disulfated disaccharide regions. Skeletal KS-II is almost completely sulfated consisting of disulfated disaccharides interrupted by occasional mono-sulfated N-acetyllactosamine residues. KS-III also contains highly sulfated KS disaccharides but differs from KS-I and KS-II through 2-O-mannose linkage to serine or threonine core protein residues on proteoglycans such as phosphacan and abakan in brain tissue. Historically, the major emphasis on the biology of KS has focused on its sulfated regions for good reason. The sulfation motifs on KS convey important molecular recognition information and direct cell behavior through a number of interactive proteins. Emerging evidence also suggest functional roles for the poly-N-acetyllactosamine regions of KS requiring further investigation. Thus further research is warranted to better understand the complexities of KS. |
format | Online Article Text |
id | pubmed-5993099 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2018 |
publisher | Oxford University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-59930992018-06-13 Keratan sulfate, a complex glycosaminoglycan with unique functional capability Caterson, Bruce Melrose, James Glycobiology Review From an evolutionary perspective keratan sulfate (KS) is the newest glycosaminoglycan (GAG) but the least understood. KS is a sophisticated molecule with a diverse structure, and unique functional roles continue to be uncovered for this GAG. The cornea is the richest tissue source of KS in the human body but the central and peripheral nervous systems also contain significant levels of KS and a diverse range of KS-proteoglycans with essential functional roles. KS also displays important cell regulatory properties in epithelial and mesenchymal tissues and in bone and in tumor development of diagnostic and prognostic utility. Corneal KS-I displays variable degrees of sulfation along the KS chain ranging from non-sulfated polylactosamine, mono-sulfated and disulfated disaccharide regions. Skeletal KS-II is almost completely sulfated consisting of disulfated disaccharides interrupted by occasional mono-sulfated N-acetyllactosamine residues. KS-III also contains highly sulfated KS disaccharides but differs from KS-I and KS-II through 2-O-mannose linkage to serine or threonine core protein residues on proteoglycans such as phosphacan and abakan in brain tissue. Historically, the major emphasis on the biology of KS has focused on its sulfated regions for good reason. The sulfation motifs on KS convey important molecular recognition information and direct cell behavior through a number of interactive proteins. Emerging evidence also suggest functional roles for the poly-N-acetyllactosamine regions of KS requiring further investigation. Thus further research is warranted to better understand the complexities of KS. Oxford University Press 2018-01-11 /pmc/articles/PMC5993099/ /pubmed/29340594 http://dx.doi.org/10.1093/glycob/cwy003 Text en © The Author(s) 2018. Published by Oxford University Press. http://creativecommons.org/licenses/by-nc/4.0/ This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/4.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited. For commercial re-use, please contact journals.permissions@oup.com |
spellingShingle | Review Caterson, Bruce Melrose, James Keratan sulfate, a complex glycosaminoglycan with unique functional capability |
title | Keratan sulfate, a complex glycosaminoglycan with unique functional capability |
title_full | Keratan sulfate, a complex glycosaminoglycan with unique functional capability |
title_fullStr | Keratan sulfate, a complex glycosaminoglycan with unique functional capability |
title_full_unstemmed | Keratan sulfate, a complex glycosaminoglycan with unique functional capability |
title_short | Keratan sulfate, a complex glycosaminoglycan with unique functional capability |
title_sort | keratan sulfate, a complex glycosaminoglycan with unique functional capability |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5993099/ https://www.ncbi.nlm.nih.gov/pubmed/29340594 http://dx.doi.org/10.1093/glycob/cwy003 |
work_keys_str_mv | AT catersonbruce keratansulfateacomplexglycosaminoglycanwithuniquefunctionalcapability AT melrosejames keratansulfateacomplexglycosaminoglycanwithuniquefunctionalcapability |