The DOI matches its Crossref record; 47 of the 47 references it cites were found in a registry or an index.
Alternative splicing in the aggrecan G3 domain influences binding interactions with tenascin-C and other extracellular matrix proteins.
Open accessAbstract
The proteoglycans aggrecan, versican, neurocan, and brevican bind hyaluronan through their N-terminal G1 domains, and other extracellular matrix proteins through the C-type lectin repeat in their C-terminal G3 domains. Here we identify tenascin-C as a ligand for the lectins of all these proteoglycans and map the binding site on the tenascin molecule to fibronectin type III repeats, which corresponds to the proteoglycan lectin-binding site on tenascin-R. In the G3 domain, the C-type lectin is flanked by epidermal growth factor (EGF) repeats and a complement regulatory protein-like motif. In aggrecan, these are subject to alternative splicing. To investigate if these flanking modules affect the C-type lectin ligand interactions, we produced recombinant proteins corresponding to aggrecan G3 splice variants. The G3 variant proteins containing the C-type lectin showed different affinities for various ligands, including tenascin-C, tenascin-R, fibulin-1, and fibulin-2. The presence of an EGF motif enhanced the affinity of interaction, and in particular the splice variant containing both EGF motifs had significantly higher affinity for ligands, such as tenascin-R and fibulin-2. The mRNA for this splice variant was shown by reverse transcriptase-PCR to be expressed in human chondrocytes. Our findings suggest that alternative splicing in the aggrecan G3 domain may be a mechanism for modulating interactions and extracellular matrix assembly.
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“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 Day et al., 2004
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Galtrey, C. M., & Fawcett, J. W. (2007) · Brain Research Reviews · doi:10.1016/j.brainresrev.2006.09.006 · Cited by 575
The role of tenascin-C in tissue injury and tumorigenesis
Midwood, K. S., & Orend, G. (2009) · Journal of Cell Communication and Signaling · doi:10.1007/s12079-009-0075-1 · Cited by 453
“Tenascin-C also interacts with ECM-resident proteoglycans, including members of the lectican family; versican, neurocan, aggrecan and brevican (Day et al. 2004).”
Tenascin-C induced signaling in cancer
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Tissue mechanics regulate brain development, homeostasis and disease
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“3A) stiffens the tumor tissue relative to normal brain by limiting the flexibility of the ECM (Mouw et al., 2014; Day et al., 2004; Kim and Kumar, 2014).”
BackgroundFell‐Muir Lecture: Proteoglycans and more – from molecules to biology
Heinegård, D. K. (2009) · International Journal of Experimental Pathology · doi:10.1111/j.1365-2613.2009.00695.x · Cited by 326
“These include the fibrillins, the fibulins as well as tenascins (Day et al. 2004).”
Background
Metadata
- Authors
- Day, J. M., Olin, A. I., Murdoch, A. D., Canfield, A., Sasaki, T., Timpl, R., Hardingham, T. E., & Aspberg, A.
- Affiliations
- Wellcome Centre for Cell-Matrix Research (GB)
- Lund University (SE)
- Max Planck Institute of Biochemistry (DE)
- Corresponding author
- Aspberg, Anders
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2004-03
- Volume
- 279
- Issue
- 13
- Pages
- 12511-12518
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2157467821
- Cited by
- 127
- References
- 47
- Citations by year
- 2026: 1 · 2025: 2 · 2024: 5 · 2023: 6 · 2022: 8 · 2021: 7 · 2020: 1 · 2019: 5 · 2018: 7 · 2017: 5 · 2016: 5 · 2015: 2 · 2014: 2 · 2013: 10 · 2012: 9
- FWCI
- 2.83
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Research Explorer (The University of Manchester) (publishedVersion)
- Max Planck Institute for Plasma Physics (submittedVersion)
- Lund University Publications (Lund University) (submittedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Proteoglycans and glycosaminoglycans research
- Health Sciences › Medicine › Rheumatology › Osteoarthritis Treatment and Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Protease and Inhibitor Mechanisms
- Keywords
- aggrecan, alternative splicing, tenascin-C, tenascin-R, C-type lectin, EGF-like repeats, fibulin-1, fibulin-2, extracellular matrix assembly, chondrocytes, hyaluronan binding, fibronectin type III repeats
- MeSH terms
- Amino Acid Sequence, Base Sequence, Binding Sites, Binding, Competitive, Dose-Response Relationship, Drug, Electrophoresis, Polyacrylamide Gel, Epidermal Growth Factor, Extracellular Matrix, Fibronectins, Humans, Kinetics, Ligands, Molecular Sequence Data, Protein Binding, Proteoglycans, Recombinant Proteins, RNA, Messenger, Time Factors, Extracellular Matrix Proteins, Alternative Splicing, Protein Structure, Tertiary, Tenascin, Chondrocytes, Reverse Transcriptase Polymerase Chain Reaction, Surface Plasmon Resonance, Amino Acid Motifs, Lectins, Lectins, C-Type, Aggrecans
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