Brevican distinctively assembles extracellular components at the large diameter nodes of Ranvier in the CNS
Yoko Bekku, Uwe Rauch, Yoshifumi Ninomiya, Toshitaka Oohashi
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.
Node of Ranvier
Proteoglycan
Scaffolding proteins
Tenascin-R
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Brevican Medicine & Life Sciences 100%
Ranvier's Nodes Medicine & Life Sciences 82%
tenascin R Medicine & Life Sciences 42%
Class 5 Receptor-Like Protein Tyrosine Phosphatases Medicine & Life Sciences 40%
Versicans Medicine & Life Sciences 23%
Hyaluronic Acid Medicine & Life Sciences 16%
Immunoprecipitation Medicine & Life Sciences 7%
Bekku, Y., Rauch, U., Ninomiya, Y., & Oohashi, T. (2009). Brevican distinctively assembles extracellular components at the large diameter nodes of Ranvier in the CNS. Journal of Neurochemistry, 108(5), 1266-1276. https://doi.org/10.1111/j.1471-4159.2009.05873.x
Brevican distinctively assembles extracellular components at the large diameter nodes of Ranvier in the CNS. / Bekku, Yoko; Rauch, Uwe; Ninomiya, Yoshifumi; Oohashi, Toshitaka.
In: Journal of Neurochemistry, Vol. 108, No. 5, 03.2009, p. 1266-1276.
Bekku, Y, Rauch, U, Ninomiya, Y & Oohashi, T 2009, 'Brevican distinctively assembles extracellular components at the large diameter nodes of Ranvier in the CNS', Journal of Neurochemistry, vol. 108, no. 5, pp. 1266-1276. https://doi.org/10.1111/j.1471-4159.2009.05873.x
Bekku Y, Rauch U, Ninomiya Y, Oohashi T. Brevican distinctively assembles extracellular components at the large diameter nodes of Ranvier in the CNS. Journal of Neurochemistry. 2009 Mar;108(5):1266-1276. https://doi.org/10.1111/j.1471-4159.2009.05873.x
Bekku, Yoko ; Rauch, Uwe ; Ninomiya, Yoshifumi ; Oohashi, Toshitaka. / Brevican distinctively assembles extracellular components at the large diameter nodes of Ranvier in the CNS. In: Journal of Neurochemistry. 2009 ; Vol. 108, No. 5. pp. 1266-1276.
@article{a265e33d9f544647a06d74d66ba937e5,
title = "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.",
keywords = "Action potential, Extracellular matrix, Node of Ranvier, Proteoglycan, Scaffolding proteins, Tenascin-R",
author = "Yoko Bekku and Uwe Rauch and Yoshifumi Ninomiya and Toshitaka Oohashi",
journal = "Journal of Neurochemistry",
T1 - Brevican distinctively assembles extracellular components at the large diameter nodes of Ranvier in the CNS
AU - Bekku, Yoko
AU - Rauch, Uwe
AU - Ninomiya, Yoshifumi
AU - Oohashi, Toshitaka
N2 - 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.
AB - 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.
KW - Action potential
KW - Extracellular matrix
KW - Node of Ranvier
KW - Proteoglycan
KW - Scaffolding proteins
KW - Tenascin-R
JO - Journal of Neurochemistry
JF - Journal of Neurochemistry