Distinct interaction of versican/PG-M with hyaluronan and link protein
Open accessAbstract
The proteoglycan aggregate is the major structural component of the cartilage matrix, comprising hyaluronan (HA), link protein (LP), and a large chondroitin sulfate (CS) proteoglycan, aggrecan. Here, we found that another member of aggrecan family, versican, biochemically binds to both HA and LP. Functional analyses of recombinant looped domains (subdomains) A, B, and B' of the N-terminal G1 domain revealed that the B-B' segment of versican is adequate for binding to HA and LP, whereas A and B-B' of aggrecan bound to LP and HA, respectively. BIAcore trade mark analyses showed that the A subdomain of versican G1 enhances HA binding but has a negligible effect on LP binding. Overlay sensorgrams demonstrated that versican G1 or its B-B' segment forms a complex with both HA and LP. We generated a molecular model of the B-B' segment, in which a deletion and an insertion of B' and B are critical for stable structure and HA binding. These results provide important insights into the mechanisms of formation of the proteoglycan aggregate and HA binding of molecules containing the link module.
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The interaction between Hapln1/Crtl1 and aggrecan is mediated through association of their N-terminal immunoglobulin modules.
“The interaction between Hapln1/Crtl1 and aggrecan is mediated through association of their N-terminal Ig modules (Grover and Roughley, 1994;Matsumoto et al., 2003;Perin et al., 1987).”
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 Matsumoto et al., 2003
Hapln1/Crtl1 and versican G1 interact via their link modules.
“In contrast, Hapln1/Crtl1 and versican G1 interaction occurred via their link modules (Matsumoto et al., 2003).”
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 Matsumoto et al., 2003
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References 34 · Cited by 153
Research works printed but not linked: 2
- Hascall, V. C., Heinegard, D. K., and Wight, T. N. (1991) in Proteoglycans: Metabolism and Pathology in Cell Biology of Extracellular Matrix (Hay, E. D., ed) pp. 149 -175, Plenum Press, New York
- Kishimoto, J., Ehama, R., Wu, L., Jiang, S., Jiang, N., and Burgeson, R. E. (1999) Proc. Natl. Acad. Sci. U. S. A. 96, 7336 -7341
- Authors
- Matsumoto, K., Shionyu, M., Go, M., Shimizu, K., Shinomura, T., Kimata, K., & Watanabe, H.
- Affiliations
- Aichi Medical University (JP)
- Nagoya University (JP)
- Gifu University (JP)
- Corresponding author
- Watanabe, Hideto
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2003-10
- Volume
- 278
- Issue
- 42
- Pages
- 41205-41212
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1977063541
- Cited by
- 153
- References
- 34
- Citations by year
- 2026: 3 · 2025: 7 · 2024: 11 · 2023: 6 · 2022: 9 · 2021: 2 · 2020: 10 · 2019: 5 · 2018: 1 · 2017: 5 · 2016: 3 · 2015: 5 · 2014: 6 · 2013: 9 · 2012: 6
- FWCI
- 3.52
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- Japan Society for the Promotion of Science
- 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
- versican, hyaluronic acid, link protein, proteoglycan aggregates, aggrecan, chondroitin sulfate proteoglycans, cartilage matrix, hyaluronan binding, Link module, molecular modeling
- MeSH terms
- Amino Acid Sequence, Animals, Cell Line, Chondroitin Sulfates, Genetic Vectors, Humans, Hyaluronic Acid, Kinetics, Models, Molecular, Molecular Sequence Data, Precipitin Tests, Protein Binding, Chondroitin Sulfate Proteoglycans, Recombinant Proteins, Time Factors, Immunoblotting, Cell Adhesion Molecules, Sequence Homology, Amino Acid, Protein Structure, Tertiary, Hyaluronan Receptors, Surface Plasmon Resonance, Lectins, C-Type, Mice, Versicans
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