Bral1, a brain-specific link protein, colocalizing with the versican V2 isoform at the nodes of Ranvier in developing and adult mouse central nervous systems
Abstract
Bral1, a brain-specific hyaluronan-binding protein, has been cloned recently. To gain insight into the role of Bral1, we generated a specific antibody against this protein. We have examined the detailed localization pattern of Bral1 protein and compared it with that of other members of the lectican proteoglycan family, such as brevican and versican, with which Bral1 is predicted to interact. The immunoreactivity of Bral1 antibody was predominantly observed in myelinated fiber tracts in the adult brain and could be detected at P20 in the white matter of the developing cerebellum, suggesting that expression starts when axonal myelination takes place. Furthermore, immunostaining demonstrated that Bral1 colocalized with the versican V2 isoform at the nodes of Ranvier. The present data suggest that Bral1 may play a pivotal role in the formation of the hyaluronan-associated matrix in the CNS that facilitates neuronal conduction by forming an ion diffusion barrier at the nodes.
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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 Oohashi et al., 2002
Versican V2 and Hapln2/Bral1 are most ubiquitously located at the nodes.
“Versican V2 and Hapln2/Bral1 are most ubiquitously located at the nodes (Schmalfeldt et al., 2000;Oohashi et al., 2002).”
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 Oohashi et al., 2002
Cites
MATRIX PROTEOGLYCANS: From Molecular Design to Cellular Function
Iozzo, R. V. (1998) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.67.1.609 · Cited by 1,639 · see citing works
Lecticans: organizers of the brain extracellular matrix
Yamaguchi, Y. (2000) · Cellular and Molecular Life Sciences · doi:10.1007/pl00000690 · Cited by 642 · see citing works
Ruoslahti, E. (1996) · Glycobiology · doi:10.1093/glycob/6.5.489 · Cited by 467 · see citing works
Dependence of nodal sodium channel clustering on paranodal axoglial contact in the developing CNS
Rasband, M. N., Peles, E., Trimmer, J. S., Levinson, S. R., Lux, S. E., & Shrager, P. (1999) · The Journal of Neuroscience · doi:10.1523/jneurosci.19-17-07516.1999 · Cited by 325 · see citing works
Hyaluronate binding properties of versican.
LeBaron, R. G., Zimmermann, D., & Ruoslahti, E. I. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)50191-0 · Cited by 317 · see citing works
Self-citationRauch, U., Gao, P., Janetzko, A., Flaccus, A., Hilgenberg, L., Tekotte, H., Margolis, R. K., & Margolis, R. U. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)98755-7 · Cited by 267 · see citing works
Self-citationProperties of the extracellular calcium binding module of the proteoglycan testican
Kohfeldt, E., Maurer, P., Vannahme, C., & Timpl, R. (1997) · FEBS Letters · doi:10.1016/s0014-5793(97)01070-3 · Cited by 246 · see citing works
Molecular domains of myelinated axons.
Peles, E., & Salzer, J. (2000) · Current Opinion in Neurobiology · doi:10.1016/s0959-4388(00)00122-7 · Cited by 242 · see citing works
Milev, P., Maurel, P., Chiba, A., Mevissen, M., Popp, S., Yamaguchi, Y., Margolis, R. K., & Margolis, R. U. (1998) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1998.8759 · Cited by 219 · see citing works
Brain derived versican V2 is a potent inhibitor of axonal growth
Schmalfeldt, M., Bandtlow, C. E., Dours-Zimmermann, M. T., Winterhalter, K. H., & Zimmermann, D. R. (2000) · Journal of Cell Science · doi:10.1242/jcs.113.5.807 · Cited by 197 · see citing works
Self-citationMice lacking link protein develop dwarfism and craniofacial abnormalities
Watanabe, H., & Yamada, Y. (1999) · Nature Genetics · doi:10.1038/6016 · Cited by 190 · see citing works
Giltay, R., Timpl, R., & Kostka, G. (1999) · Matrix Biology · doi:10.1016/s0945-053x(99)00038-4 · Cited by 167 · see citing works
Perissinotto, D., Iacopetti, P., Bellina, I., Doliana, R., Colombatti, A., Unno, Z. P., Bronner-Fraser, M. E., Shinomura, T., Kimata, K., Mörgelin, M., et al. (2000) · Development · doi:10.1242/dev.127.13.2823 · Cited by 149 · see citing works
Neame, P. J., & Barry, F. (1993) · Cellular and Molecular Life Sciences · doi:10.1007/bf01923584 · Cited by 146 · see citing works
Mörgelin, M., Paulsson, M., Hardingham, T., Heinegård, D. K., & Engel, J. (1988) · Biochemical Journal · doi:10.1042/bj2530175 · Cited by 144 · see citing works
Asher, R., Perides, G., Vanderhaeghen, J., & Bignami, A. (1991) · Journal of Neuroscience Research · doi:10.1002/jnr.490280314 · Cited by 120 · see citing works
Binette, F., Cravens, J. L., Kahoussi, B., Haudenschild, D. R., & Goetinck, P. F. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)32282-2 · Cited by 106 · see citing works
Thon, N., Haas, C. A., Rauch, U., Merten, T., Fässler, R., Frotscher, M., & Deller, T. (2000) · European Journal of Neuroscience · doi:10.1046/j.1460-9568.2000.00109.x · Cited by 104 · see citing works
Self-citationThe structure and regulation of hyaluronan-binding proteins
Day, A. J. (1999) · Biochemical Society Transactions · doi:10.1042/bst0270115 · Cited by 86 · see citing works
Link protein and a hyaluronic acid-binding region as components of aorta proteoglycan
Gardell, S., Baker, J., Caterson, B., Heinegård, D. K., & Rodén, L. (1980) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(80)80111-2 · Cited by 86 · see citing works
Glial hyaluronate-binding protein: a product of metalloproteinase digestion of versican?
Perides, G., Asher, R. A., Lark, M. W., Lane, W. S., Robinson, R. A., & Bignami, A. (1995) · Biochemical Journal · doi:10.1042/bj3120377 · Cited by 74 · see citing works
Analysis of Neurocan Structures Interacting with the Neural Cell Adhesion Molecule N-CAM
Retzler, C., Göhring, W., & Rauch, U. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.44.27304 · Cited by 71 · see citing works
Self-citationHirakawa, S., Oohashi, T., Su, W.-D., Yoshioka, H., MURAKAMI, T., Arata, J., & Ninomiya, Y. (2000) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2000.3583 · Cited by 70 · see citing works
Self-citationHyaluronan and Hyaluronectin in the Nervous System
Delpech, B., DELPECH, A., Brückner, G., Girard, N., & Maingonnat, C. (2007) · Novartis Foundation symposium · doi:10.1002/9780470513774.ch13 · Cited by 69 · see citing works
An amino acid sequence common to both cartilage proteoglycan and link protein.
Neame, P. J., Périn, J.-P., Bonnet, F., Christner, J. E., Jollès, P., & Baker, J. R. (1985) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)38887-7 · Cited by 46 · see citing works
Neurons with Intensely Negatively Charged Extracellular Matrix in the Human Visual Cortex.
MURAKAMI, T., Ohtsuka, A., & TAGUCHI, T. (1994) · Archivum histologicum japonicum · doi:10.1679/aohc.57.509 · Cited by 38 · see citing works
Self-citationImmunochemical Characterization of the Hyaluronic Acid‐Hyaluronectin Interaction
Delpech, B. (1982) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1982.tb05338.x · Cited by 37 · see citing works
Choi, H. U., Tang, L. H., Johnson, T. L., & Rosenberg, L. (1985) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)38879-8 · Cited by 36 · see citing works
Mörgelin, M., Engel, J., Heinegård, D. K., & Paulsson, M. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)49709-3 · Cited by 33 · see citing works
Sado, Y., Kagawa, M., Naito, I., & Okigaki, T. (1991) · Virchows Archiv B Cell Pathology Including Molecular Pathology · doi:10.1007/bf02899566 · Cited by 32 · see citing works
Isolation and characterization of a link protein from bovine aorta proteoglycan aggregate
Vijayagopal, P., Radhakrishnamurthy, B., Srinivasan, S. R., & Berenson, G. S. (1985) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/0304-4165(85)90188-6 · Cited by 28 · see citing works
Rosenberg, L., Choi, H. U., Tang, L. H., Pal, S., Johnson, T., Lyons, D. A., & Laue, T. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(20)89603-3 · Cited by 27 · see citing works
Shimada, A., Ota, Y., Sugiyama, Y., Inoue, S., Sato, S., Kume, K., & Shimizu, T. (1998) · Journal of Investigative Dermatology · doi:10.1046/j.1523-1747.1998.00202.x · Cited by 23 · see citing works
Interaction of a brain extracellular matrix protein with hyaluronic acid
Perides, G., Biviano, F., & Bignami, A. (1991) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/0304-4165(91)90273-j · Cited by 20 · see citing works
Stirpe, N. S., Dickerson, K., & Goetinck, P. F. (1990) · Developmental Biology · doi:10.1016/0012-1606(90)90266-l · Cited by 17 · see citing works
Flagged first, then by citations
1 of the 36 references couldn’t be matched to a known paper.
Cited by
Sorted by citations
The local differentiation of myelinated axons at nodes of Ranvier
Poliak, S., & Peles, E. (2003) · Nature Reviews Neuroscience · doi:10.1038/nrn1253 · Cited by 673 · see citing works
The roles of perineuronal nets and the perinodal extracellular matrix in neuronal function
Fawcett, J. W., Oohashi, T., & Pizzorusso, T. (2019) · Nature Reviews Neuroscience · doi:10.1038/s41583-019-0196-3 · Cited by 589 · see citing works
Self-citationGaltrey, C. M., & Fawcett, J. W. (2007) · Brain Research Reviews · doi:10.1016/j.brainresrev.2006.09.006 · Cited by 575 · see citing works
Extracellular matrix of the central nervous system: from neglect to challenge
Zimmermann, D. R., & Dours-Zimmermann, M. T. (2008) · Histochemistry and Cell Biology · doi:10.1007/s00418-008-0485-9 · Cited by 465 · see citing works
Self-citationPolarized Domains of Myelinated Axons
Salzer, J. L. (2003) · Neuron · doi:10.1016/s0896-6273(03)00628-7 · Cited by 399 · see citing works
Extracellular matrix and perineuronal nets in CNS repair
Kwok, J. C. F., Dick, G., Wang, D., & Fawcett, J. W. (2011) · Developmental Neurobiology · doi:10.1002/dneu.20974 · Cited by 395 · see citing works
The perineuronal net and the control of CNS plasticity
Wang, D., & Fawcett, J. (2012) · Cell and Tissue Research · doi:10.1007/s00441-012-1375-y · Cited by 373 · see citing works
Composition of Perineuronal Net Extracellular Matrix in Rat Brain
Deepa, S. S., Carulli, D., Galtrey, C., Rhodes, K., Fukuda, J., Mikami, T., Sugahara, K., & Fawcett, J. W. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m600544200 · Cited by 367 · see citing works
Carulli, D., Rhodes, K. E., Brown, D. J., Bonnert, T. P., Pollack, S. J., Oliver, K., Strata, P., & Fawcett, J. W. (2006) · Journal of Comparative Neurology · doi:10.1002/cne.20822 · Cited by 341 · see citing works
Dityatev, A. E., Seidenbecher, C. I., & Schachner, M. (2010) · Trends in Neurosciences · doi:10.1016/j.tins.2010.08.003 · Cited by 229 · see citing works
Molecular domains of myelinated axons in the peripheral nervous system
Salzer, J., Brophy, P., & Peles, E. (2008) · Glia · doi:10.1002/glia.20750 · Cited by 240 · see citing works
Galtrey, C. M., Kwok, J. C. F., Carulli, D., Rhodes, K. E., & Fawcett, J. W. (2008) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2008.06108.x · Cited by 203 · see citing works
Spicer, A. P., Joo, A., & Bowling, R. A. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m213100200 · Cited by 201 · see citing works
Three mechanisms assemble central nervous system nodes of Ranvier
Susuki, K., Chang, K.-J., Zollinger, D. R., Liu, Y., Ogawa, Y., Eshed-Eisenbach, Y., Dours-Zimmermann, M. T., Oses-Prieto, J. A., Burlingame, A. L., Seidenbecher, C. I., et al. (2013) · Neuron · doi:10.1016/j.neuron.2013.03.005 · Cited by 186 · see citing works
Self-citationExtracellular matrix components associated with remodeling processes in brain
Rauch, U. (2004) · Cellular and Molecular Life Sciences (CMLS) · doi:10.1007/s00018-004-4043-x · Cited by 205 · see citing works
Self-citationMiyata, S., & Kitagawa, H. (2017) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2017.06.010 · Cited by 171 · see citing works
Mechanisms of node of Ranvier assembly
Rasband, M. N., & Peles, E. (2020) · Nature reviews. Neuroscience · doi:10.1038/s41583-020-00406-8 · Cited by 168 · see citing works
Glial Membranes at the Node of Ranvier Prevent Neurite Outgrowth
Huang, J. K., Phillips, G. R., Roth, A. D., Pedraza, L., Shan, W., Belkaïd, W., Mi, S., Svenningsen, Å. F., Florens, L. A., Yates, J. R., et al. (2005) · Science · doi:10.1126/science.1118313 · Cited by 160 · see citing works
Burnside, E. R., & Bradbury, E. J. (2013) · Neuropathology and Applied Neurobiology · doi:10.1111/nan.12114 · Cited by 153 · see citing works
Mechanisms of sodium channel clustering and its influence on axonal impulse conduction
Freeman, S. A., Desmazières, A., Fricker, D., Lubetzki, C., & Sol‐Foulon, N. (2015) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-015-2081-1 · Cited by 133 · see citing works
Molecular mechanisms of node of Ranvier formation
Susuki, K., & Rasband, M. N. (2008) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2008.09.007 · Cited by 135 · see citing works
Oohashi, T., Edamatsu, M., Bekku, Y., & Carulli, D. (2015) · Experimental Neurology · doi:10.1016/j.expneurol.2015.09.010 · Cited by 131 · see citing works
Self-citationVersican V2 Assembles the Extracellular Matrix Surrounding the Nodes of Ranvier in the CNS
Dours-Zimmermann, M. T., Maurer, K., Rauch, U., Stoffel, W., Fassler, R., & Zimmermann, D. R. (2009) · Journal of Neuroscience · doi:10.1523/jneurosci.4158-08.2009 · Cited by 123 · see citing works
Self-citationBral1: its role in diffusion barrier formation and conduction velocity in the CNS
Bekku, Y., Vargová, L., Goto, Y., Vorísek, I., Dmytrenko, L., Narasaki, M., Ohtsuka, A., Fässler, R., Ninomiya, Y., Syková, E., et al. (2010) · The Journal of Neuroscience · doi:10.1523/jneurosci.5598-09.2010 · Cited by 123 · see citing works
Self-citationArnaud, E., Zenker, J., Charles, A.-S. D. P., Stendel, C., Roos, A., Médard, J., Tricaud, N., Kleine, H. O., Lüscher, B., Weis, J., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0905523106 · Cited by 121 · see citing works
Axon initial segment ensheathed by extracellular matrix in perineuronal nets
Brückner, G., Szeöke, S., Pavlica, S., Grosche, J., & Kacza, J. (2006) · Neuroscience · doi:10.1016/j.neuroscience.2005.11.068 · Cited by 114 · see citing works
Nelson, A. D., & Jenkins, P. M. (2017) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2017.00136 · Cited by 120 · see citing works
Development of nodes of Ranvier.
Girault, J., & Peles, E. (2002) · Current Opinion in Neurobiology · doi:10.1016/s0959-4388(02)00370-7 · Cited by 110 · see citing works
Bekku, Y., Su, W.-D., Hirakawa, S., Fässler, R., Ohtsuka, A., Kang, J. S., Sanders, J., Murakami, T., Ninomiya, Y., & Oohashi, T. (2003) · Molecular and Cellular Neuroscience · doi:10.1016/s1044-7431(03)00133-7 · Cited by 114 · see citing works
Self-citationMolecular control of brain plasticity and repair
Fawcett, J. (2009) · Progress in Brain Research · doi:10.1016/s0079-6123(09)17534-9 · Cited by 105 · see citing works
Bekku, Y., Rauch, U., Ninomiya, Y., & Oohashi, T. (2009) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2009.05873.x · Cited by 104 · see citing works
Self-citationWestling, J., Gottschall, P. E., Thompson, V. P., Cockburn, A., Perides, G., Zimmermann, D. R., & Sandy, J. D. (2004) · Biochemical Journal · doi:10.1042/bj20030896 · Cited by 104 · see citing works
Self-citationKrishnaswamy, V. R., Benbenishty, A., Blinder, P., & Sagi, I. (2019) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-019-03182-6 · Cited by 92 · see citing works
Seyfried, N. T., McVey, G. F., Almond, A., Mahoney, D. J., Dudhia, J., & Day, A. J. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m411297200 · Cited by 94 · see citing works
Neural ECM molecules in synaptic plasticity, learning, and memory
Senkov, O., Anđjus, P. R., Radenović, L., Soriano, E., & Dityatev, A. E. (2014) · Progress in brain research · doi:10.1016/b978-0-444-63486-3.00003-7 · Cited by 94 · see citing works
Brain matrix: structure, turnover and necessity
Rauch, U. (2007) · Biochemical Society Transactions · doi:10.1042/bst0350656 · Cited by 88 · see citing works
Self-citationMolecular signature of extracellular matrix pathology in schizophrenia
Pantazopoulos, H., Katsel, P., Haroutunian, V. H., Chelini, G., Klengel, T., & Berretta, S. (2020) · European Journal of Neuroscience · doi:10.1111/ejn.15009 · Cited by 79 · see citing works
Liu, Y., Zhou, Q., Tang, M., Fu, N., Shao, W., Zhang, S., Yin, Y., Zeng, R., Wang, X., Hu, G., et al. (2015) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2015.01.015 · Cited by 81 · see citing works
Extracellular Matrix in Neural Plasticity and Regeneration
Chelyshev, Y. A., Kabdesh, I. M., & Mukhamedshina, Y. O. (2020) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-020-00986-0 · Cited by 76 · see citing works
Yeom, M., Shim, I., Lee, H., & Hahm, D. (2004) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2004.11.034 · Cited by 69 · see citing works
Shibata, S., Fukada, K., Harujiro, I. M. A. I., Abe, T., & Yamashita, Y. (2003) · Journal of Anatomy · doi:10.1046/j.1469-7580.2003.00226.x · Cited by 68 · see citing works
Bekku, Y., Saito, M., Moser, M., Fuchigami, M., Maehara, A., Nakayama, M., Kusachi, S., Ninomiya, Y., & Oohashi, T. (2012) · Journal of Comparative Neurology · doi:10.1002/cne.23009 · Cited by 65 · see citing works
Self-citationBeggah, A., Dours-Zimmermann, M. T., Barras, F. M., Brosius, A., Zimmermann, D., & Zurn, A. D. (2005) · Neuroscience · doi:10.1016/j.neuroscience.2005.03.005 · Cited by 61 · see citing works
Self-citationNaughton, B. J., Duncan, F. J., Murrey, D. A., Meadows, A. S., Newsom, D. E., Stoicea, N., White, P., Scharre, D. W., McCarty, D. M., & Fu, H. (2014) · Journal of Alzheimer s Disease · doi:10.3233/jad-140606 · Cited by 61 · see citing works
A canine BCAN microdeletion associated with episodic falling syndrome
Gill, J. L., Tsai, K. L., Krey, C., Noorai, R. E., Vanbellinghen, J.-F., GAROSI, L. S., Shelton, G. D., Clark, L. A., & Harvey, R. J. (2011) · Neurobiology of Disease · doi:10.1016/j.nbd.2011.07.014 · Cited by 59 · see citing works
Collateral Sprouting as a Target for Improved Function after Spinal Cord Injury
Hagg, T. (2006) · Journal of Neurotrauma · doi:10.1089/neu.2006.23.281 · Cited by 59 · see citing works
Differential expression of proteoglycans at central and peripheral nodes of Ranvier
Melendez‐Vasquez, C. V., Carey, D. J., Zanazzi, G. J., Reizes, O., Maurel, P., & Salzer, J. L. (2005) · Glia · doi:10.1002/glia.20245 · Cited by 56 · see citing works
Localization of aggrecan and versican in the developing rat central nervous system.
Popp, S., Andersen, J. S., Maurel, P., & Margolis, R. U. (2003) · Developmental Dynamics · doi:10.1002/dvdy.10282 · Cited by 55 · see citing works
Brevican isoforms associate with neural membranes
Seidenbecher, C. I., Smalla, K., Fischer, N., Gundelfinger, E. D., & Kreutz, M. R. (2002) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2002.01183.x · Cited by 55 · see citing works
Neural ECM molecules in axonal and synaptic homeostatic plasticity
Frischknecht, R., Chang, K.-J., Rasband, M. N., & Seidenbecher, C. I. (2014) · Progress in brain research · doi:10.1016/b978-0-444-63486-3.00004-9 · Cited by 53 · see citing works
Perisynaptic barrier of proteoglycans in the mature brain and spinal cord
MURAKAMI, T., & Ohtsuka, A. (2003) · Archivum histologicum japonicum · doi:10.1679/aohc.66.195 · Cited by 53 · see citing works
Self-citationAggrecan and versican: two brothers close or apart
Watanabe, H. (2022) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00081.2022 · Cited by 51 · see citing works
The making of a node: a co-production of neurons and glia
Eshed‐Eisenbach, Y., & Peles, E. (2013) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2013.06.003 · Cited by 48 · see citing works
Czipri, M., Otto, J. M., Cs-Szabó, G., Kamath, R. V., Vermes, C., Firneisz, G., Kolman, K. J., Watanabe, H., Li, Y., Roughley, P. J., et al. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m303329200 · Cited by 46 · see citing works
Rauch, U., Hirakawa, S., Oohashi, T., Kappler, J., & Roos, G. (2004) · Matrix Biology · doi:10.1016/j.matbio.2003.11.007 · Cited by 42 · see citing works
Self-citationNew Insights into ADAMTS Metalloproteases in the Central Nervous System
Mohamedi, Y., Fontanil, T., Cobo, T., Cal, S., & Obaya, Á. J. (2020) · Biomolecules · doi:10.3390/biom10030403 · Cited by 39 · see citing works
Levy, C., Brooks, J. M., Chen, J., Su, J., & Fox, M. A. (2014) · The Journal of Comparative Neurology · doi:10.1002/cne.23701 · Cited by 38 · see citing works
Reduced Expression of the Hyaluronan and Proteoglycan Link Proteins in Malignant Gliomas
Sim, H., Hu, B., & Viapiano, M. S. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.013185 · Cited by 38 · see citing works
Abaskharoun, M., Bellemare, M., Lau, E., & Margolis, R. U. (2010) · Brain Research · doi:10.1016/j.brainres.2010.02.048 · Cited by 37 · see citing works
Snyder, J. M., Smoak, I. W., Birkland, T. P., Chang, M. Y., & Frevert, C. W. (2015) · Journal of Histochemistry & Cytochemistry · doi:10.1369/0022155415610383 · Cited by 37 · see citing works
Characterization of dermacan, a novel zebrafish lectican gene, expressed in dermal bones
Kang, J. S., Oohashi, T., Kawakami, Y., Bekku, Y., Belmonte, J. C. I., & Ninomiya, Y. (2004) · Mechanisms of Development · doi:10.1016/j.mod.2004.01.007 · Cited by 37 · see citing works
Self-citationLim, J. P., Devaux, J. J., & Yuki, N. (2014) · Autoimmunity Reviews · doi:10.1016/j.autrev.2014.08.005 · Cited by 35 · see citing works
Zacharias, U., & Rauch, U. (2006) · Journal of Cell Science · doi:10.1242/jcs.03094 · Cited by 35 · see citing works
Self-citationNeurocan contributes to the molecular heterogeneity of the perinodal ECM
Bekku, Y., & Oohashi, T. (2010) · Archivum histologicum japonicum · doi:10.1679/aohc.73.95 · Cited by 34 · see citing works
Self-citationOgawa, H., Oohashi, T., Sata, M., Bekku, Y., Hirohata, S., Nakamura, K., Yonezawa, T., Kusachi, S., Shiratori, Y., & Ninomiya, Y. (2004) · Matrix Biology · doi:10.1016/j.matbio.2004.07.001 · Cited by 33 · see citing works
Self-citationZhang, H., Baader, S. L., Sixt, M., Kappler, J., & Rauch, U. (2004) · Journal of Histochemistry & Cytochemistry · doi:10.1369/jhc.3a6221.2004 · Cited by 33 · see citing works
Self-citationLy, L., Barnett, M. H., Zheng, Y. Z., Gulati, T., Prineas, J. W., & Crossett, B. (2011) · Journal of Proteome Research · doi:10.1021/pr200672n · Cited by 31 · see citing works
Suzuki, A., Hoshi, T., Ishibashi, T., Hayashi, A., Yamaguchi, Y., & Baba, H. (2004) · Glia · doi:10.1002/glia.20008 · Cited by 29 · see citing works
Bucher, E., Collins, J. M., King, A. E., Vickers, J. C., & Kirkcaldie, M. (2021) · Brain Structure and Function · doi:10.1007/s00429-021-02327-3 · Cited by 29 · see citing works
Oligodendrocyte Myelin Glycoprotein Does Not Influence Node of Ranvier Structure or Assembly
Chang, K.-J., Susuki, K., Dours-Zimmermann, M. T., Zimmermann, D. R., & Rasband, M. N. (2010) · Journal of Neuroscience · doi:10.1523/jneurosci.1698-10.2010 · Cited by 29 · see citing works
Self-citationOligodendrocytes regulate formation of nodes of Ranvier via the recognition molecule OMgp
Nie, D. A., Ma, Q., Law, J. W. S., Chia, C., Dhingra, N. K., Shimoda, Y., Yang, W.-L., Gong, N., CHEN, Q.-W., Xu, G., et al. (2006) · Neuron Glia Biology · doi:10.1017/s1740925x06000251 · Cited by 29 · see citing works
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Wang, Q., Wang, C., Ji, B., Zhou, J., Yang, C., & Chen, J. (2019) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2019.00060 · Cited by 25 · see citing works
A view of the genetic and proteomic profile of extracellular matrix molecules in aging and stroke
Chmelová, M., Androvic, P., Kirdajová, D., Turečková, J., Kriška, J., Valihrach, L., Anděrová, M., & Vargová, L. (2023) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2023.1296455 · Cited by 23 · see citing works
ADAMTS‐4 in oligodendrocytes contributes to myelination with an impact on motor function
Pruvost, M., Lépine, M., Leonetti, C., Etard, O., Naveau, M., Agin, V., Docagne, F., Maubert, E., Ali, C., Emery, É., et al. (2017) · Glia · doi:10.1002/glia.23207 · Cited by 22 · see citing works
Kang, J. S., Kawakami, Y., Bekku, Y., Ninomiya, Y., Belmonte, J. C. I., & Oohashi, T. (2008) · ZOOLOGICAL SCIENCE · doi:10.2108/zsj.25.912 · Cited by 22 · see citing works
Self-citationStructural and Functional Diversity of Hyaluronan-Binding Proteins
Blundell, C. D., Seyfried, N. T., & Day, A. J. (2004) · Elsevier eBooks · doi:10.1016/b978-008044382-9/50039-x · Cited by 21 · see citing works
Wang, Q., Zhou, Q., Zhang, S., Shao, W., Yin, Y., Li, Y., Hou, J., Zhang, X., Guo, Y.-S., Wang, X., et al. (2016) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2016.00197 · Cited by 21 · see citing works
Horii‐Hayashi, N., Okuda, H., Tatsumi, K., Ishizaka, S., Yoshikawa, M., & Wanaka, A. (2008) · Cell and Tissue Research · doi:10.1007/s00441-008-0698-1 · Cited by 20 · see citing works
Regeneration Failure in the CNS
Zurn, A. D., & Bandtlow, C. E. (2007) · Springer eBooks · doi:10.1007/0-387-30128-3_4 · Cited by 19 · see citing works
Rozhnova, M. A., Pankratova, E. V., Викторович, С. С., & Kazantsev, V. (2021) · Chaos Solitons & Fractals · doi:10.1016/j.chaos.2021.111253 · Cited by 18 · see citing works
Elbaz, B., Darwish, A., Vardy, M., Isaac, S., Tokars, H. M., Dzhashiashvili, Y., Korshunov, K. S., Prakriya, M., Eden, A., & Popko, B. (2023) · Neuron · doi:10.1016/j.neuron.2023.10.008 · Cited by 21 · see citing works
Functional Organization of the Nodes of Ranvier
Scherer, S., Arroyo, E., & Peles, E. (2004) · Elsevier eBooks · doi:10.1016/b978-012439510-7/50057-7 · Cited by 16 · see citing works
Molecular composition of extracellular matrix in the vestibular nuclei of the rat
Rácz, É., Gaál, B., Kecskés, S., & Matesz, C. (2013) · Brain Structure and Function · doi:10.1007/s00429-013-0575-x · Cited by 18 · see citing works
Cicanic, M., Edamatsu, M., Bekku, Y., Voříšek, I., Oohashi, T., & Vargová, L. (2017) · Journal of Neuroscience Research · doi:10.1002/jnr.24136 · Cited by 17 · see citing works
Self-citationMartá-Ariza, M., Leitner, D. F., Kanshin, E., Suazo, J., Giusti Pedrosa, A., Thierry, M., Lee, E. B., Devinsky, O., Drummond, E., Fortea, J., et al. (2025) · Acta Neuropathologica · doi:10.1007/s00401-025-02844-z · Cited by 15 · see citing works
Accumulation of Neurofascin at Nodes of Ranvier Is Regulated by a Paranodal Switch
Zhang, Y., Yuen, S. K., Peles, E., & Salzer, J. L. (2020) · Journal of Neuroscience · doi:10.1523/jneurosci.0830-19.2020 · Cited by 15 · see citing works
Combinatorial identification of DNA methylation patterns over age in the human brain
Moghadam, B. T., Dąbrowski, M., Kaminska, B., Grabherr, M., & Komorowski, J. (2016) · BMC Bioinformatics · doi:10.1186/s12859-016-1259-3 · Cited by 14 · see citing works
Popelář, J., GÓMEZ, M. D., Lindovský, J., Rybalko, N., Burianova, J. S., Oohashi, T., & Syka, J. (2017) · Physiological Research · doi:10.33549/physiolres.933605 · Cited by 14 · see citing works
Self-citationV3: an enigmatic isoform of the proteoglycan versican
Wight, T. N., Day, A. J., Kang, I., Harten, I. A., Kaber, G., Briggs, D. C., Braun, K. R., Lemire, J. M., Kinsella, M. G., Hinek, A., et al. (2023) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00059.2023 · Cited by 13 · see citing works
Lamprey lecticans link new vertebrate genes to the origin and elaboration of vertebrate tissues
Root, Z. D., Jandzík, D., Allen, C., Brewer, M., Romášek, M., Square, T. A., & Medeiros, D. M. (2021) · Developmental Biology · doi:10.1016/j.ydbio.2021.03.020 · Cited by 12 · see citing works
Identifying loci for behavioral traits using genome‐tagged mice
Liu, D., Singh, R. P., Khan, A. H., Bhavsar, K., Lusis, A. J., Davis, R. C., & Smith, D. (2003) · Journal of Neuroscience Research · doi:10.1002/jnr.10765 · Cited by 13 · see citing works
Gaál, B., Rácz, É., Juhász, T., Holló, K., & Matesz, C. (2013) · Neuroscience · doi:10.1016/j.neuroscience.2013.10.080 · Cited by 11 · see citing works
Bral1: “Superglue” for the extracellular matrix in the brain white matter
Cicanic, M., Syková, E., & Vargová, L. (2012) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2012.01.009 · Cited by 11 · see citing works
The Molecular and Morphologic Structures That Make Saltatory Conduction Possible in Peripheral Nerve
Carroll, S. L. (2017) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/nlx013 · Cited by 10 · see citing works
Mukhina, I. V., Александровна, К. С., & Dityatev, A. E. (2012) · Neurochemical Journal · doi:10.1134/s1819712412020055 · Cited by 8 · see citing works
The extracellular matrix composition of the optic nerve subarachnoid space
Hao, J., Kohler, C., van den Dorpel, H., Scholl, H. P. N., Meyer, P., Killer, H. E., & Neutzner, A. (2020) · Experimental Eye Research · doi:10.1016/j.exer.2020.108250 · Cited by 8 · see citing works
Bekku, Y., & Oohashi, T. (2019) · Advances in experimental medicine and biology · doi:10.1007/978-981-32-9636-7_8 · Cited by 8 · see citing works
Self-citationProteomics analysis of periplaque and chronic inactive multiple sclerosis lesions
Wilkins, J. M., Mangalaparthi, K. K., Netzel, B. C., Sherman, W. A., Guo, Y. X., Kalinowska, A., Pandey, A., & Lucchinetti, C. F. (2024) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2024.1448215 · Cited by 7 · see citing works
Heterogeneous expression of extracellular matrix molecules in the red nucleus of the rat
Rácz, É., Gaál, B., & Matesz, C. (2016) · Neuroscience · doi:10.1016/j.neuroscience.2016.02.005 · Cited by 6 · see citing works
Chondroitin Sulfate Proteoglycans in the Brain
Aono, S., & Oohira, A. (2006) · Advances in pharmacology · doi:10.1016/s1054-3589(05)53015-1 · Cited by 6 · see citing works
- Authors
- Oohashi, T., Hirakawa, S., Bekku, Y., Rauch, U., Zimmermann, D. R., Su, W.-D., Ohtsuka, A., Murakami, T., & Ninomiya, Y.
- Affiliations
- Okayama University (JP)
- Lund University (SE)
- University of Zurich (CH)
- Venue
- Molecular and Cellular Neuroscience
- Publisher
- Elsevier BV
- Published
- 2002-01
- Volume
- 19
- Issue
- 1
- Pages
- 43-57
- ISSN
- 1044-7431 (ISSN-L)
- OpenAlex
- W1980283213
- Cited by
- 124
- References
- 36
- Citations by year
- 2026: 1 · 2025: 3 · 2024: 2 · 2023: 4 · 2022: 2 · 2021: 3 · 2020: 8 · 2019: 6 · 2018: 3 · 2017: 6 · 2016: 4 · 2015: 6 · 2014: 6 · 2013: 5 · 2012: 5
- FWCI
- 3.29
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Molecular and Cellular Neuroscience (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 › Neurology › Barrier Structure and Function Studies
- Keywords
- nodes of Ranvier, hyaluronan-binding protein, brevican, axonal myelination, white matter development, cerebellum, ion diffusion barrier, central nervous system development
- MeSH terms
- Proteoglycan Link Protein, Amino Acid Sequence, Animals, Antibodies, Central Nervous System, Extracellular Matrix, Hyaluronic Acid, Immunohistochemistry, Isomerism, Mice, Inbred Strains, Molecular Sequence Data, Nerve Tissue Proteins, Neurons, Peptide Fragments, Chondroitin Sulfate Proteoglycans, Proteoglycans, Rabbits, Ranvier's Nodes, Gene Expression Regulation, Developmental, Lectins, C-Type, Mice, Versicans
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