Cartilage link protein interacts with neurocan, which shows hyaluronan binding characteristics different from CD44 and TSG-6
Abstract
The interaction of neurocan with hyaluronan was qualitatively characterized with alkaline phosphatase fusion proteins secreted by mammalian cells. The wild type neurocan hyaluronan binding domain fused to alkaline phosphatase bound to immobilized hyaluronan under physiological as well as moderately hypertonic conditions, whereas its ability to bind to immobilized chondroitin sulfate dropped rapidly with increasing salt concentration. Strong hyaluronan binding ability was still evident when in both link modules within the hyaluronan binding domain a basic amino acid was mutated, which is well conserved among link modules of hyaluronan binding proteins. A strong enhancement of the binding of neurocan to immobilized hyaluronan was observed after preincubation of the immobilized hyaluronan with cartilage link protein. Moreover, this preincubation mediated also the binding of a fusion protein representing only the immunoglobulin module of neurocan linked to alkaline phosphatase, which showed no binding to immobilized hyaluronan alone. The interaction of the neurocan immunoglobulin module with link protein could also be shown by overlay blot analysis. These observations suggest that the hyaluronan binding characteristics of paired link modules are different from those of single link modules, and that the reported temporal co-expression of cartilage link protein and of neurocan in developing brain implicates the possibility of a cooperative function of these molecules.
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Hapln1/Crtl1 binding with neurocan G1 is mediated by the immunoglobulin module of neurocan G1, indicating a hyaluronan-independent interaction.
“Hapln1/Crtl1 binding with neurocan G1 interaction was demonstrated to be mediated by the Ig module of neurocan G1 on overlay blot analysis, indicating hyaluronan independent interaction (Rauch 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 Rauch et al., 2004
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- Authors
- Rauch, U., Hirakawa, S., Oohashi, T., Kappler, J., & Roos, G.
- Affiliations
- Lund University (SE)
- Okayama University (JP)
- University of Bonn (DE)
- Corresponding author
- Rauch, Uwe
- Venue
- Matrix Biology
- Publisher
- Elsevier BV
- Published
- 2004-02
- Volume
- 22
- Issue
- 8
- Pages
- 629-639
- ISSN
- 0945-053X (ISSN-L)
- OpenAlex
- W1963481111
- Cited by
- 42
- References
- 34
- Citations by year
- 2024: 3 · 2023: 1 · 2022: 1 · 2020: 1 · 2019: 1 · 2018: 1 · 2017: 2 · 2016: 1 · 2015: 3 · 2014: 1 · 2012: 2
- FWCI
- 1.78
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Matrix Biology (publishedVersion)
- PubMed (publishedVersion)
- Lund University Publications (Lund University) (submittedVersion)
- Funders
- Deutsche Forschungsgemeinschaft
- Greta och Johan Kocks stiftelser
- 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
- neurocan, hyaluronan binding, hyaluronan-binding domain, CD44, TSG-6, chondroitin sulfate, Link module, extracellular matrix, brain development, salt effects
- MeSH terms
- Proteoglycan Link Protein, Alanine, Alkaline Phosphatase, Amino Acid Sequence, Animals, Cell Line, Humans, Hyaluronic Acid, Molecular Sequence Data, Nerve Tissue Proteins, Protein Binding, Chondroitin Sulfate Proteoglycans, Proteoglycans, Recombinant Fusion Proteins, Cell Adhesion Molecules, Extracellular Matrix Proteins, Sequence Alignment, Culture Media, Conditioned, Point Mutation, Protein Structure, Tertiary, Hyaluronan Receptors, Lectins, C-Type, Mice, Rats, Neurocan
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