Binding between the neural cell adhesion molecules axonin-1 and Nr- CAM/Bravo is involved in neuron-glia interaction
Abstract
Neural cell adhesion molecules of the immunoglobulin superfamily mediate cellular interactions via homophilic binding to identical molecules and heterophilic binding to other family members or structurally unrelated cell-surface glycoproteins. Here we report on an interaction between axonin-1 and Nr-CAM/Bravo. In search for novel ligands of axonin-1, fluorescent polystyrene microspheres conjugated with axonin-1 were found to bind to peripheral glial cells from dorsal root ganglia. By antibody blockage experiments an axonin-1 receptor on the glial cells was identified as Nr-CAM. The specificity of the interaction was confirmed with binding studies using purified axonin-1 and Nr-CAM. In cultures of dissociated dorsal root ganglia antibodies against axonin-1 and Nr-CAM perturbed the formation of contacts between neurites and peripheral glial cells. Together, these results implicate a binding between axonin-1 of the neuritic and Nr-CAM of the glial cell membrane in the early phase of axon ensheathment in the peripheral nervous system.
Additional Information
Copyright © 1995 by The Rockefeller University Press. RUP grants the public the non-exclusive right to copy, distribute, or display the Work under a Creative Commons Attribution-Noncommercial-Share Alike 3.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/3.0/ and http://creativecommons.org/licenses/by-nc-sa/3.0/legalcode. Received for publication 16 May 1995 and in revised form 17 August 1995. We thank Eva Niederer for her excellent support of our work with the flow cytometer, Walter Scherle for help with scanning EM, Urs Ziegler for assistance in microscopic analysis, Doris Kemler and Heinz Sonderegger for help with figures, and Gerard Wall for reading the manuscript. Furthermore, we thank E.J. de la Rosa, G. Morales, F.G. Rathjen, N. Ratner, and M. Chiquet for providing antibodies. This work was supported by grants from the Swiss National Science Foundation, the Schweizerische Multiple Sklerose Gesellschaft, the Fonds for medizinische Forschung der Universität Zürich, and the National Institutes of Health (EY07725).Attached Files
Published - SUTjcb95.pdf
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Additional details
- PMCID
- PMC2200008
- Eprint ID
- 12176
- Resolver ID
- CaltechAUTHORS:SUTjcb95
- Swiss National Science Foundation (SNSF)
- Schweizerische Multiple Sklerose Gesellschaft
- Fonds for medizinische Forschung der Universität Zürich
- NIH
- EY07725
- Created
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2008-10-28Created from EPrint's datestamp field
- Updated
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2021-11-08Created from EPrint's last_modified field