Glycosaminoglycans in extracellular matrix organisation: are concepts from soft matter physics key to understanding the formation of perineuronal nets?
Language English Country England, Great Britain Media print-electronic
Document type Journal Article, Research Support, Non-U.S. Gov't, Review
Grant support
G0900538
Medical Research Council - United Kingdom
16539
Arthritis Research UK - United Kingdom
76445
Medical Research Council - United Kingdom
MC_PC_16050
Medical Research Council - United Kingdom
19489
Arthritis Research UK - United Kingdom
PubMed
29275227
DOI
10.1016/j.sbi.2017.12.002
PII: S0959-440X(17)30084-2
Knihovny.cz E-resources
- MeSH
- Extracellular Matrix Proteins metabolism MeSH
- Extracellular Matrix metabolism MeSH
- Glycosaminoglycans chemistry metabolism MeSH
- Hydrophobic and Hydrophilic Interactions MeSH
- Neurons metabolism MeSH
- Protein Binding MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Review MeSH
- Names of Substances
- Extracellular Matrix Proteins MeSH
- Glycosaminoglycans MeSH
Conventional wisdom has it that proteins fold and assemble into definite structures, and that this defines their function. Glycosaminoglycans (GAGs) are different. In most cases the structures they form have a low degree of order, even when interacting with proteins. Here, we discuss how physical features common to all GAGs-hydrophilicity, charge, linearity and semi-flexibility-underpin the overall properties of GAG-rich matrices. By integrating soft matter physics concepts (e.g. polymer brushes and phase separation) with our molecular understanding of GAG-protein interactions, we can better comprehend how GAG-rich matrices assemble, what their properties are, and how they function. Taking perineuronal nets (PNNs)-a GAG-rich matrix enveloping neurons-as a relevant example, we propose that microphase separation determines the holey PNN anatomy that is pivotal to PNN functions.
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