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The Journal of Neuroscience, June 17, 2009, 29(24):7731-7742; doi:10.1523/JNEUROSCI.4158-08.2009

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Cellular/Molecular
Versican V2 Assembles the Extracellular Matrix Surrounding the Nodes of Ranvier in the CNS

María T. Dours-Zimmermann,1 Konrad Maurer,2 Uwe Rauch,3 Wilhelm Stoffel,4 Reinhard Fässler,5 and Dieter R. Zimmermann1

Institutes of 1Surgical Pathology and 2Anesthesiology, University Hospital Zurich, CH-8091 Zurich, Switzerland, 3Vascular Wall Biology, Department of Experimental Medical Science, University of Lund, S-221 00 Lund, Sweden, 4Center for Biochemistry, Medical Faculty, University of Cologne, D-50931 Cologne, Germany, and 5Department of Molecular Medicine, Max Planck Institute of Biochemistry, D-82152 Martinsried, Germany

Correspondence should be addressed to Dieter R. Zimmermann, Institute of Surgical Pathology, University Hospital Zurich, Schmelzbergstrasse 12, CH-8091 Zürich, Switzerland. Email: dieterzi{at}pathol.uzh.ch

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.

Received Sept. 1, 2008; revised March 27, 2009; accepted April 23, 2009.

Correspondence should be addressed to Dieter R. Zimmermann, Institute of Surgical Pathology, University Hospital Zurich, Schmelzbergstrasse 12, CH-8091 Zürich, Switzerland. Email: dieterzi{at}pathol.uzh.ch
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