Lecticans: organizers of the brain extracellular matrix
Open accessAbstract
Lecticans are a family of chondroitin sulfate proteoglycans, encompassing aggrecan, versican, neurocan and brevican. These proteoglycans are characterized by the presence of a hyaluronan-binding domain and a C-type lectin domain in their core proteins. Through these domains, lecticans interact with carbohydrate and protein ligands in the extracellular matrix and act as linkers of these extracellular matrix molecules. In adult brain, lecticans are thought to interact with hyaluronan and tenascin-R to form a ternary complex. We propose that the hyaluronan-lectican-tenascin-R complex constitutes the core assembly of the adult brain extracellular matrix, which is found mainly in pericellular spaces of neurons as 'perineuronal nets'.
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CSPGs around some classes of neurons interact with other brain ECM molecules, self-assembling into aggregate structures called perineuronal nets (PNNs).
“In addition to being a key inhibitory molecule in the diffuse ECM, CSPGs around some classes of neurons also interact with other brain ECM molecules, self-assembling into aggregate structures called perineuronal nets (PNNs) [12–14].”
From The extracellular matrix and perineuronal nets in memory (2022) · cites this paper as [14]
Aggrecan interacting with hyaluronan mainly contributes to the polyanionic character of the perineuronal net.
“Thus, aggrecan interacting with hyaluronan, also highly negatively charged, mainly contributes to the polyanionic character of the PN.”
From Aggrecan, link protein and tenascin-R are essential components of the perineuronal net to protect neurons against iron-induced oxidative stress (2014) · cites this paper as [45]
PNNs are composed of chondroitin sulfate proteoglycans, tenascin, and link proteins, which facilitate binding to a hyaluronan backbone.
“PNNs are composed of CSPGs, tenascin, and link proteins, which facilitate binding to a hyaluronan backbone (Yamaguchi, 1999) (Figure 2).”
From The Perineuronal ‘Safety’ Net? Perineuronal Net Abnormalities in Neurological Disorders (2018) · cites this paper as Yamaguchi, 1999
The lectican family includes aggrecan, neurocan, versican, and brevican, which vary in core protein size and number of GAG side chains.
“These include aggrecan, neurocan, versican, and brevican, which vary in core protein size and the number of GAG side chains (Yamaguchi, 1999).”
From The Perineuronal ‘Safety’ Net? Perineuronal Net Abnormalities in Neurological Disorders (2018) · cites this paper as Yamaguchi, 1999
CSPGs are organizers of the ECM and are highly represented in PNNs, with aggrecan, neurocan, brevican, versican, and phosphacan among the most abundant.
“CSPGs, the organizers of the ECM, are highly represented in PNNs, with aggrecan, neurocan, brevican, versican and phosphacan among the most abundant (Deepa et al., 2006; Giamanco and Matthews, 2012; Yamaguchi, 2000).”
From Losing the sugar coating: Potential impact of perineuronal net abnormalities on interneurons in schizophrenia (2015) · cites this paper as Yamaguchi, 2000
The HLT model proposes that the supramolecular organization of perineuronal nets consists of hyaluronan, lecticans, and tenascin-R.
“The current concept of supramolecular organization and assembly of PNN was first proposed by Ruoslahti (1996) and designated as “HLT (hyaluronan, lecticans and TN-R)” model by Yamaguchi (2000) (Fig. 2).”
From The hyaluronan and proteoglycan link proteins: Organizers of the brain extracellular matrix and key molecules for neuronal function and plasticity (2015) · cites this paper as Yamaguchi, 2000
A lectican with higher affinity for tenascin-R, such as brevican, might form a more highly cross-linked perineuronal net than those with lower affinity, such as neurocan.
“For instance, a lectican with higher affinity for TN-R (such as brevican) might form a more highly cross-linked PNN than those with lower affinity (e.g.neurocan; Aspberg et al., 1997;Yamaguchi, 2000).”
From The hyaluronan and proteoglycan link proteins: Organizers of the brain extracellular matrix and key molecules for neuronal function and plasticity (2015) · cites this paper as Yamaguchi, 2000
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Pathophysiological function of ADAMTS enzymes on molecular mechanism of Alzheimer’s disease
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- Authors
- Yamaguchi, Y.
- Affiliations
- Sanford Burnham Prebys Medical Discovery Institute (US)
- Corresponding author
- Yamaguchi, Y.
- ORCID
- Yamaguchi, Y.
- Venue
- Cellular and Molecular Life Sciences
- Published
- 2000-02
- Volume
- 57
- Issue
- 2
- Pages
- 276-289
- ISSN
- 1420-682X (ISSN-L)
- PMC
- PMC11146776
- OpenAlex
- W1974815300
- Cited by
- 642
- References
- 5
- Citations by year
- 2026: 10 · 2025: 11 · 2024: 24 · 2023: 17 · 2022: 22 · 2021: 35 · 2020: 24 · 2019: 23 · 2018: 35 · 2017: 21 · 2016: 21 · 2015: 19 · 2014: 46 · 2013: 29 · 2012: 27
- FWCI
- 7.15
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Cellular and Molecular Life Sciences (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health (5r01ns032717-08)
- National Institute of Neurological Disorders and Stroke (NS 32717)
- Eunice Kennedy Shriver National Institute of Child Health and Human Development (HD 25938, P01HD025938)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Proteoglycans and glycosaminoglycans research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glycosylation and Glycoproteins Research
- Health Sciences › Medicine › Rheumatology › Osteoarthritis Treatment and Mechanisms
- Keywords
- lecticans, chondroitin sulfate proteoglycans, aggrecan, versican, neurocan, brevican, hyaluronic acid, tenascin-R, extracellular matrix, perineuronal nets, C-type lectin domain, hyaluronan-binding domain
- MeSH terms
- Amino Acid Sequence, Animals, Brain, Extracellular Matrix, Humans, Models, Biological, Molecular Sequence Data, Organ Specificity, Protein Processing, Post-Translational, Chondroitin Sulfate Proteoglycans, Alternative Splicing, Protein Structure, Tertiary
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