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Chondroitin sulfates and their binding molecules in the central nervous system
Chondroitin sulfate (CS) is the most abundant glycosaminoglycan (GAG) in the central nervous system (CNS) matrix. Its sulfation and epimerization patterns give rise to different forms of CS, which enables it to interact specifically and with a significant affinity with various signalling molecules i...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Springer US
2017
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5487772/ https://www.ncbi.nlm.nih.gov/pubmed/28101734 http://dx.doi.org/10.1007/s10719-017-9761-z |
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author | Djerbal, L Lortat-Jacob, H Kwok, JCF |
author_facet | Djerbal, L Lortat-Jacob, H Kwok, JCF |
author_sort | Djerbal, L |
collection | PubMed |
description | Chondroitin sulfate (CS) is the most abundant glycosaminoglycan (GAG) in the central nervous system (CNS) matrix. Its sulfation and epimerization patterns give rise to different forms of CS, which enables it to interact specifically and with a significant affinity with various signalling molecules in the matrix including growth factors, receptors and guidance molecules. These interactions control numerous biological and pathological processes, during development and in adulthood. In this review, we describe the specific interactions of different families of proteins involved in various physiological and cognitive mechanisms with CSs in CNS matrix. A better understanding of these interactions could promote a development of inhibitors to treat neurodegenerative diseases. |
format | Online Article Text |
id | pubmed-5487772 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | Springer US |
record_format | MEDLINE/PubMed |
spelling | pubmed-54877722017-07-03 Chondroitin sulfates and their binding molecules in the central nervous system Djerbal, L Lortat-Jacob, H Kwok, JCF Glycoconj J Review Chondroitin sulfate (CS) is the most abundant glycosaminoglycan (GAG) in the central nervous system (CNS) matrix. Its sulfation and epimerization patterns give rise to different forms of CS, which enables it to interact specifically and with a significant affinity with various signalling molecules in the matrix including growth factors, receptors and guidance molecules. These interactions control numerous biological and pathological processes, during development and in adulthood. In this review, we describe the specific interactions of different families of proteins involved in various physiological and cognitive mechanisms with CSs in CNS matrix. A better understanding of these interactions could promote a development of inhibitors to treat neurodegenerative diseases. Springer US 2017-01-18 2017 /pmc/articles/PMC5487772/ /pubmed/28101734 http://dx.doi.org/10.1007/s10719-017-9761-z Text en © The Author(s) 2017 Open Access This article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. |
spellingShingle | Review Djerbal, L Lortat-Jacob, H Kwok, JCF Chondroitin sulfates and their binding molecules in the central nervous system |
title | Chondroitin sulfates and their binding molecules in the central nervous system |
title_full | Chondroitin sulfates and their binding molecules in the central nervous system |
title_fullStr | Chondroitin sulfates and their binding molecules in the central nervous system |
title_full_unstemmed | Chondroitin sulfates and their binding molecules in the central nervous system |
title_short | Chondroitin sulfates and their binding molecules in the central nervous system |
title_sort | chondroitin sulfates and their binding molecules in the central nervous system |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5487772/ https://www.ncbi.nlm.nih.gov/pubmed/28101734 http://dx.doi.org/10.1007/s10719-017-9761-z |
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