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  • Long-term maintenance of Na+ channels at nodes of Ranvier depends on glial contact mediated by gliomedin and NrCAM.

Long-term maintenance of Na+ channels at nodes of Ranvier depends on glial contact mediated by gliomedin and NrCAM.

The Journal of neuroscience : the official journal of the Society for Neuroscience (2014-04-11)
Veronique Amor, Konstantin Feinberg, Yael Eshed-Eisenbach, Anya Vainshtein, Shahar Frechter, Martin Grumet, Jack Rosenbluth, Elior Peles
ABSTRACT

Clustering of Na(+) channels at the nodes of Ranvier is coordinated by myelinating glia. In the peripheral nervous system, axoglial contact at the nodes is mediated by the binding of gliomedin and glial NrCAM to axonal neurofascin 186 (NF186). This interaction is crucial for the initial clustering of Na(+) channels at heminodes. As a result, it is not clear whether continued axon-glial contact at nodes of Ranvier is required to maintain these channels at the nodal axolemma. Here, we report that, in contrast to mice that lack either gliomedin or NrCAM, absence of both molecules (and hence the glial clustering signal) resulted in a gradual loss of Na(+) channels and other axonal components from the nodes, the formation of binary nodes, and dysregulation of nodal gap length. Therefore, these mice exhibit neurological abnormalities and slower nerve conduction. Disintegration of the nodes occurred in an orderly manner, starting with the disappearance of neurofascin 186, followed by the loss of Na(+) channels and ankyrin G, and then βIV spectrin, a sequence that reflects the assembly of nodes during development. Finally, the absence of gliomedin and NrCAM led to the invasion of the outermost layer of the Schwann cell membrane beyond the nodal area and the formation of paranodal-like junctions at the nodal gap. Our results reveal that axon-glial contact mediated by gliomedin, NrCAM, and NF186 not only plays a role in Na(+) channel clustering during development, but also contributes to the long-term maintenance of Na(+) channels at nodes of Ranvier.

MATERIALS
Product Number
Brand
Product Description

Sigma-Aldrich
Anti-Neurofilament NF-H Antibody, clone TA51, culture supernatant, clone TA51, Chemicon®
Sigma-Aldrich
Spectrin from human erythrocytes, buffered aqueous glycerol solution
Sigma-Aldrich
Monoclonal Anti-Sodium Channel, Pan antibody produced in mouse, ~1 mg/mL, clone K58/35, purified immunoglobulin