Link protein interactions with hyaluronate and proteoglycans. Characterization of two distinct domains in bovine cartilage link proteins
Open accessAbstract
Hyaluronic acid-binding region and trypsin-link protein were prepared from bovine nasal cartilage proteoglycan complex after trypsin digestion. Binary complexes were reformed between trypsin-link protein and hyaluronic acid-binding region or hyaluronate. Upon trypsin treatment of these complexes, two fragments deriving from trypsin-link protein were characterized. One of them, of 20 kDa, corresponds in fact to a 140-amino acid long fragment and bears the glycosylated site of trypsin-link protein; it appears to be involved in proteoglycan/link protein interaction. The other, of 22 kDa, corresponds to the 200 C-terminal amino acids of trypsin-link protein; it appears to be involved in the binding of link protein with hyaluronic acid. A structural model of bovine trypsin-like protein depicting two distinct domains involved in hyaluronate and proteoglycan subunit interactions is proposed.
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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 Perin et al., 1987
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- Authors
- Périn, J. P., Bonnet, F., Thurieau, C., & Jollès, P.
- Affiliations
- Université Paris Cité (FR)
- ORCID
- Jollès, P
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1987-09
- Volume
- 262
- Issue
- 27
- Pages
- 13269-13272
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1486162627
- Cited by
- 59
- References
- 30
- Citations by year
- 2026: 1 · 2025: 1 · 2024: 1 · 2023: 1 · 2022: 1 · 2017: 1 · 2016: 1 · 2015: 1
- FWCI
- 1.66
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Proteoglycans and glycosaminoglycans research
- Health Sciences › Medicine › Rheumatology › Osteoarthritis Treatment and Mechanisms
- Health Sciences › Medicine › Rheumatology › Bone and Dental Protein Studies
- Keywords
- link protein, hyaluronic acid, proteoglycans, nasal cartilage, protein domains, glycosylation sites, protein-protein interaction, structural model
- MeSH terms
- Proteoglycan Link Protein, Animals, Cartilage, Cattle, Chromatography, Gel, Hyaluronic Acid, Peptide Fragments, Proteins, Proteoglycans, Trypsin, Extracellular Matrix Proteins, Macromolecular Substances
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