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Review
. 2020 Nov;53(10):491-499.
doi: 10.5483/BMBRep.2020.53.10.156.

Extracellular matrixes and neuroinflammation

Dong Gil Jang  1 , Hyo Jung Sim  1 , Eun Kyung Song  1 , Taejoon Kwon  2 , Tae Joo Park  2
Affiliations
Review

Extracellular matrixes and neuroinflammation

Dong Gil Jang et al. BMB Rep. 2020 Nov.

Abstract

The extracellular matrix is a critical component of every human tissue. ECM not only functions as a structural component but also regulates a variety of cellular processes such as cell migration, differentiation, proliferation, and cell death. In addition, current studies suggest that ECM is critical for the pathophysiology of various human diseases. ECM is composed of diverse components including several proteins and polysaccharide chains such as chondroitin sulfate, heparan sulfate, and hyaluronic acid. Each component of ECM exerts its own functions in cellular and pathophysiological processes. One of the interesting recent findings is that ECM is involved in inflammatory responses in various human tissues. In this review, we summarized the known functions of ECM in neuroinflammation after acute injury and chronic inflammatory diseases of the central nerve systems. [BMB Reports 2020; 53(10): 491-499].

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Conflict of interest statement

CONFLICTS OF INTEREST

The authors have no conflicting interests.

Figures

Fig. 1
Fig. 1
The extracellular matrices in central nervous systems. Interstitial ECM is loosely distributed in the CNS and neuronal cell bodies and are tightly associated and covered by PNN. Neural ECMs are mainly composed of proteoglycans and hyaluronic acid with a small amount of fibrous matrix.
Fig. 2
Fig. 2
Hyalectan in neuronal ECMs. Neural ECMs are mainly composed of hyalectans which are the meshwork of interconnected hyaluronans and chondroitin sulfate proteoglycans such as aggrecan, brevican, neurocan, and versican.
Fig. 3
Fig. 3
Lectican family of chondroitin sulfate proteoglycan. Lecticans are a class of chondroitin sulfate proteoglycan (CSPG) including Aggrecan, Versican, Neurocan, and Brevican. All lecticans have a G1-domain which is a conserved binding site to hyaluronan, the central GAG attachment domain, and a lectin-containing G3 domain mediating the binding to glycoproteins such as tenascins.
Fig. 4
Fig. 4
Structure of Tenascins. (A) The domain structure of major tenascin, Tenascin-C and Tenascin-R. (B) Tenascins form oligomers and the N-terminus of tenascin meditates oligomerization.
See this image and copyright information in PMC

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