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Permanent URL to this publication: http://dx.doi.org/10.5167/uzh-19309

Dours-Zimmermann, M; Maurer, K; Rauch, U; Fässler, R; Zimmermann, D R (2009). Versican V2 assembles the extracellular matrix surrounding the nodes of ranvier in the CNS. Journal of Neuroscience, 29(24):7731-7742.

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Abstract

The CNS-restricted versican splice-variant V2 is a large chondroitin sulfate proteoglycan incorporated in the extracellular matrix surrounding myelinated fibers and particularly accumulating at nodes of Ranvier. In vitro, it is a potent inhibitor of axonal growth and therefore considered to participate in the reduction of structural plasticity connected to myelination. To study the role of versican V2 during postnatal development, we designed a novel isoform-specific gene inactivation approach circumventing early embryonic lethality of the complete knock-out and preventing compensation by the remaining versican splice variants. These mice are viable and fertile; however, they display major molecular alterations at the nodes of Ranvier. While the clustering of nodal sodium channels and paranodal structures appear in versican V2-deficient mice unaffected, the formation of the extracellular matrix surrounding the nodes is largely impaired. The conjoint loss of tenascin-R and phosphacan from the perinodal matrix provide strong evidence that versican V2, possibly controlled by a nodal receptor, organizes the extracellular matrix assembly in vivo.

Item Type:Journal Article, refereed, original work
Communities & Collections:04 Faculty of Medicine > University Hospital Zurich > Institute of Surgical Pathology
04 Faculty of Medicine > University Hospital Zurich > Institute of Anesthesiology
DDC:610 Medicine & health
Language:English
Date:June 2009
Deposited On:22 Jun 2009 08:30
Last Modified:28 Nov 2013 01:05
Publisher:Society for Neuroscience
ISSN:0270-6474
Additional Information:Holder of copyright: The Society for Neuroscience
Publisher DOI:10.1523/JNEUROSCI.4158-08.2009
PubMed ID:19535585
Citations:Web of Science®. Times Cited: 35
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Scopus®. Citation Count: 35

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