Brevican distinctively assembles extracellular components at the large diameter nodes of Ranvier in the CNS
Abstract
Brevican is known to be an abundant extracellular matrix component in the adult brain and a structural constituent of perineuronal nets. We herein show that brevican, tenascin‐R (TN‐R) and phosphacan are present at the nodes of Ranvier on myelinated axons with a particularly large diameter in the central nervous system. A brevican deficiency resulted in a reorganization of the nodal matrices, which was characterized by the shift of TN‐R, and concomitantly phosphacan, from an axonal diameter‐dependent association with nodes to an axonal diameter independent association. Supported by the co‐immunoprecipitation results, these observations indicate that the presence of TN‐R and phosphacan at nodes is normally brevican‐dependent, while in the absence of brevican these molecules can also be recruited by versican V2. The versican V2 and Bral1 distribution was not affected, thus indicating a brevican‐independent role of these two molecules for establishing hyaluronan‐binding matrices at the nodes. Our results revealed that brevican plays a crucial role in determining the specialization of the hyaluronan‐binding nodal matrix assemblies in large diameter nodes.
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The HLT model applies not only to perineuronal net molecular organization but also to perinodal extracellular matrix organization.
“The HLT model turn out to be a very far-sighted model not only for the PNN molecular organization but also for the perinodal ECM molecular organization (Bekku et al., 2009).”
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 Bekku et al., 2009
The hyaluronan-associated ECM could serve as an extracellular ion pool at the perinodal extracellular space because both hyaluronan and chondroitin sulfate provide a strong negatively charged environment corresponding to the nodal diameter.
“We thus proposed that the hyaluronan-associated ECM could serve as an”
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 Bekku et al., 2009
Brevican and neurocan localize at the nodes in an axon diameter-dependent manner.
“Brevican and neurocan are also known to localize at the nodes in an axon diameter-dependent manner (Fig. 5; Bekku et al., 2009;Bekku and Oohashi, 2010).”
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 Bekku et al., 2009
The HLT model made from PNN fits the perinodal matrix except that versican V2 is the most common lectican and aggrecan is absent at the node.
“Of particular note is that the HLT model made from PNN fits to this PM except for the differences that vercican V2 is the most common lectican and aggrecan is absent at the node (Bekku et al., 2009;Dours-Zimmermann et al., 2009).”
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 Bekku et al., 2009
Nodes of particularly large diameter have a more elaborate ECM assembly than nodes of smaller axons.
“The nodes of particularly large diameter have a more elaborate ECM assembly than the nodes of smaller axons, as if the ECM could further speed up axonal velocity by a reduction in the resistance of the extracellular medium (Bekku et al., 2009).”
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 Bekku et al., 2009
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- Authors
- Bekku, Y., Rauch, U., Ninomiya, Y., & Oohashi, T.
- Affiliations
- Okayama University (JP)
- Lund University (SE)
- Corresponding author
- Oohashi, Toshitaka
- Venue
- Journal of Neurochemistry
- Publisher
- Wiley
- Published
- 2009-02-09
- Volume
- 108
- Issue
- 5
- Pages
- 1266-1276
- ISSN
- 0022-3042 (ISSN-L)
- 1471-4159
- OpenAlex
- W2015565810
- Cited by
- 104
- References
- 21
- Citations by year
- 2026: 2 · 2025: 3 · 2024: 5 · 2023: 3 · 2022: 7 · 2021: 5 · 2020: 7 · 2019: 6 · 2018: 6 · 2017: 7 · 2016: 3 · 2015: 11 · 2014: 3 · 2013: 9 · 2012: 7
- FWCI
- 4.00
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Journal of Neurochemistry (publishedVersion)
- PubMed (publishedVersion)
- Lund University Publications (Lund University) (submittedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Proteoglycans and glycosaminoglycans research
- Life Sciences › Neuroscience › Developmental Neuroscience › Neurogenesis and neuroplasticity mechanisms
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Nerve injury and regeneration
- Keywords
- brevican, nodes of Ranvier, myelinated axons, axon diameter, extracellular matrix assembly, tenascin-R, phosphacan, perineuronal nets, central nervous system
- MeSH terms
- Age Factors, Animals, Animals, Newborn, Axons, Central Nervous System, Hyaluronic Acid, Nerve Tissue Proteins, Chondroitin Sulfate Proteoglycans, Ranvier's Nodes, Mice, Knockout, Gene Expression Regulation, Developmental, Tenascin, Lectins, C-Type, Immunoprecipitation, Mice, Receptor-Like Protein Tyrosine Phosphatases, Class 5, Brevican
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