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Brevican distinctively assembles extracellular components at the large diameter nodes of Ranvier in the CNS

Bekku, Yoko ; Rauch, Uwe LU ; Ninomiya, Yoshifumi and Oohashi, Toshitaka (2009) In Journal of Neurochemistry 108(5). p.1266-1276
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... (More)
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. (Less)
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author
; ; and
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
tenascin-R, scaffolding proteins, proteoglycan, node of Ranvier, action potential, extracellular matrix
in
Journal of Neurochemistry
volume
108
issue
5
pages
1266 - 1276
publisher
Wiley-Blackwell
external identifiers
  • wos:000263044800016
  • scopus:59449103926
  • pmid:19141078
ISSN
1471-4159
DOI
10.1111/j.1471-4159.2009.05873.x
language
English
LU publication?
yes
id
6db3cfc1-16d5-4753-81d2-aa3319127a33 (old id 1311411)
date added to LUP
2016-04-01 14:04:19
date last changed
2022-04-22 01:11:53
@article{6db3cfc1-16d5-4753-81d2-aa3319127a33,
  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.}},
  author       = {{Bekku, Yoko and Rauch, Uwe and Ninomiya, Yoshifumi and Oohashi, Toshitaka}},
  issn         = {{1471-4159}},
  keywords     = {{tenascin-R; scaffolding proteins; proteoglycan; node of Ranvier; action potential; extracellular matrix}},
  language     = {{eng}},
  number       = {{5}},
  pages        = {{1266--1276}},
  publisher    = {{Wiley-Blackwell}},
  series       = {{Journal of Neurochemistry}},
  title        = {{Brevican distinctively assembles extracellular components at the large diameter nodes of Ranvier in the CNS}},
  url          = {{http://dx.doi.org/10.1111/j.1471-4159.2009.05873.x}},
  doi          = {{10.1111/j.1471-4159.2009.05873.x}},
  volume       = {{108}},
  year         = {{2009}},
}