The C-type lectin domains of lecticans, a family of aggregating chondroitin sulfate proteoglycans, bind tenascin-R by protein– protein interactions independent of carbohydrate moiety
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The lecticans are a family of chondroitin sulfate proteoglycans including aggrecan, versican, neurocan, and brevican. The C-terminal globular domains of lecticans are structurally related to selectins, consisting of a C-type lectin domain flanked by epidermal growth factor and complement regulatory protein domains. The C-type lectin domain of versican has been shown to bind tenascin-R, an extracellular matrix protein specifically expressed in the nervous system, and the interaction was presumed to be mediated by a carbohydrate–protein interaction. In this paper, we show that the C-type lectin domain of brevican, another lectican that is specifically expressed in the nervous system, also binds tenascin-R. Surprisingly, this interaction is mediated by a protein–protein interaction through the fibronectin type III domains 3–5 of tenascin-R, independent of any carbohydrates or sulfated amino acids. The lectin domains of versican and other lecticans also bind the same domain of tenascin-R by protein–protein interactions. Surface plasmon resonance analysis revealed that brevican lectin has at least a 10-fold higher affinity than the other lectican lectins. Tenascin-R is coprecipitated with brevican from adult rat brain extracts, suggesting that tenascin-R and brevican form complexes in vivo . These results demonstrate that the C-type lectin domain can interact with fibronectin type III domains through protein–protein interactions, and suggest that brevican is a physiological tenascin-R ligand in the adult brain.
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Binding of the N-terminal of CSPG to hyaluronan chains is stabilised by Hapln, and the C-terminals of three CSPG molecules link with trimeric tenascin-R.
“While binding of the N-terminal of CSPG to hyaluronan chains is stabilised by Hapln, the C-terminals of three CSPG molecules will link with the trimeric tenascin-R [19–21].”
From The extracellular matrix and perineuronal nets in memory (2022) · cites this paper as [19]
Tenascins are fibrous, matricellular proteins that bind to the C-terminal domain of lecticans.
“Tenascins are fibrous, matricellular proteins, which bind to the C-terminal domain of lecticans (Aspberg et al., 1997; Day et al., 2004).”
From The Perineuronal ‘Safety’ Net? Perineuronal Net Abnormalities in Neurological Disorders (2018) · cites this paper as Aspberg et al., 1997
The C-type lectin subdomain of lecticans binds to fibronectin type III repeats 3-5 of tenascin-R.
“The C-type lectin subdomain of lecticans binds to the fibronectin type III repeats 3-5 of TN-R, which was demonstrated by the crystal structure of the recombinant complex (Aspberg et al., 1997;Lundell et al., 2004).”
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 Aspberg et al., 1997
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 Aspberg et al., 1997
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- Authors
- Aspberg, A., Miura, R., Bourdoulous, S., Shimonaka, M., Heinegård, D., Schachner, M., Ruoslahti, E., & Yamaguchi, Y.
- Affiliations
- Universität Hamburg (DE)
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 1997-09-16
- Volume
- 94
- Issue
- 19
- Pages
- 10116-10121
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC23322
- OpenAlex
- W1978514720
- Cited by
- 275
- References
- 1
- Citations by year
- 2026: 1 · 2025: 5 · 2024: 4 · 2023: 7 · 2022: 8 · 2021: 5 · 2020: 7 · 2019: 5 · 2018: 3 · 2017: 7 · 2016: 7 · 2015: 6 · 2014: 8 · 2013: 6 · 2012: 12
- FWCI
- 6.80
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Rutgers University Community Repository (Rutgers University) (submittedVersion)
- Lund University Publications (Lund University) (submittedVersion)
- Funders
- U.S. Department of Health and Human Services
- National Institutes of Health (5p01ca028896-15, 5r01ns032717-08)
- National Cancer Institute (CA30199, CA 28896, P30CA030199)
- National Institute of Neurological Disorders and Stroke (NS 32717)
- 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, brevican, versican, tenascin-R, C-type lectin domain, protein-protein interaction, fibronectin type III domain, chondroitin sulfate proteoglycans, extracellular matrix, brain, ligand binding
- MeSH terms
- Animals, Carbohydrates, Cell Line, Ligands, Protein Binding, Chondroitin Sulfate Proteoglycans, Tenascin, Lectins, Carbohydrate Metabolism, Rats
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