Cited by 144Proteoglycans and glycosaminoglycans researchOsteoarthritis Treatment and MechanismsLysosomal Storage Disorders Research

Chondroitin sulfates and their binding molecules in the central nervous system

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Djerbal, L, Lortat-Jacob, H, Kwok, JCF·2017·Glycoconjugate Journal

Abstract

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.

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Crossref · 10.1007/s10719-017-9761-z

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  • CS-GAGs are comprised of repeating units of glucuronic acid and N-acetylgalactosamine isomers that are uniquely modified by the addition of sulfates to the disaccharide unit, including non-sulfated (0S-CS), mono-sulfated (4S-CS and 6S-CS), and di-sulfated (2S6S-CS and 4S6S-CS) variants.

    “These CS-GAGs are comprised of repeating units of glucuronic acid and N-acetylgalatosamine isomers that are uniquely modified by the addition of sulfates to the disaccharide unit, including non-sulfated (0S-CS), mono-sulfated (4S-CS and 6S-CS), and di-sulfated (2S6S-CS and 4S6S-CS) variants (Fig. 4A) (Djerbal et al. 2017).”

    From Perineuronal net deglycosylation associates with tauopathy‐induced gliosis and neurodegeneration (2024) · cites this paper as Djerbal et al. 2017

    The Introduction and Fig. 1 caption describe repeating glucuronic acid–N-acetylgalactosamine disaccharides and identify the sulfation positions corresponding to the listed mono- and di-sulfated variants. They do not identify a non-sulfated 0S-CS variant, so that part of the list is not directly supported by our copy. (LLM, conf=0.86)

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Research works printed but not linked: 2

  1. [85]Fox GM Clark RAF Henson PM The role of growth factors in tissue repair III The molecular and cellular biology of wound repair 1988 Boston Springer US 265 271
  2. [126]Lodish, H., Berk, A., Zipursky, S.L., Matsudaira, P., Baltimore, D., Darnell, J.: Cell-cell adhesion and communication. In: Lodish, H.e.a. (ed.) Molecular Cell Biology. W.H. Freeman, New York (2000)

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Authors
Djerbal, L., Lortat-Jacob, H., & Kwok, J.
Affiliations
  • Centre National de la Recherche Scientifique (FR)
  • University of Leeds (GB)
Corresponding author
Kwok, JCF
Venue
Glycoconjugate Journal
Published
2017-01-18
Volume
34
Issue
3
Pages
363-376
ISSN
  • 0282-0080 (ISSN-L)
  • 1573-4986
OpenAlex
W2577967191
Cited by
144
References
179
Citations by year
2026: 8 · 2025: 17 · 2024: 20 · 2023: 10 · 2022: 16 · 2021: 29 · 2020: 15 · 2019: 14 · 2018: 10 · 2017: 4
FWCI
1.37
Type
journal article
Language
en
Open access
Locations
  • Glycoconjugate Journal (publishedVersion, cc-by)
  • Europe PMC (PubMed Central) (publishedVersion, cc-by)
  • PubMed Central (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • White Rose Research Online (University of Leeds, The University of Sheffield, University of York) (acceptedVersion)
  • HAL (submittedVersion)
Funders
University Grenoble Alpes
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Proteoglycans and glycosaminoglycans research
  • Health Sciences › Medicine › Rheumatology › Osteoarthritis Treatment and Mechanisms
  • Health Sciences › Medicine › Physiology › Lysosomal Storage Disorders Research
Keywords
chondroitin sulfate, glycosaminoglycans, sulfation patterns, epimerization, growth factor binding, receptor binding, guidance molecules, central nervous system development
MeSH terms
Midkine, Animals, Carbohydrate Conformation, Carrier Proteins, Central Nervous System, Chondroitin Sulfates, Extracellular Matrix, Humans, Neurons, Protein Binding, Proteoglycans, Cytokines, Extracellular Matrix Proteins, Neural Cell Adhesion Molecules, Intercellular Signaling Peptides and Proteins, Receptor-Like Protein Tyrosine Phosphatases

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