Abstract
Cell surface molecules have been implicated in cell interactions which underlie formation of the nervous system. The analysis of the functional properties of such molecules has profited from the combined use of antibodies and cell culture systems. It has been suggested that the interplay between these molecules modulates cell-to-cell interaction at critical developmental stages1,2. In the mouse, N-CAM1,3 and L1 antigen4 have been shown to mediate Ca2+-independent adhesion among neural cells. N-CAM plays a role in fasciculation of neurites and formation of neuromuscular junction. L1 is apparently not involved in synaptogenesis, but in migration of granule cell neurones in the developing mouse cerebellar cortex5. The two antigens are distinct molecular and functional entities which act synergistically in aggregation of neuroblastoma6 and early postnatal cerebellar cells7. In view of a certain similarity in function between the two groups of molecules, it was not surprising to find that structural similarities are detectable by the monoclonal antibody L2. We show here that a carbohydrate moiety recognized by L2 and HNK-1 monoclonal antibodies, is present in mouse N-CAM and LI. The L2 epitope appears on all major neural cell types but not all N-CAM molecules express it. This heterogeneity points to a previously undetected molecular diversity which may have functional implications for modulating cell adhesion during development.
This is a preview of subscription content, access via your institution
Access options
Subscribe to this journal
Receive 51 print issues and online access
$199.00 per year
only $3.90 per issue
Buy this article
- Purchase on Springer Link
- Instant access to full article PDF
Prices may be subject to local taxes which are calculated during checkout
Similar content being viewed by others
References
Edelman, G. M. et al. Cold Spring Harb. Symp. quant. Biol. 48, 515–526 (1983).
Schachner, M. et al. Cold Spring Harb. Symp. quant. Biol. 48, 557–568 (1983).
Goridis, C. et al. Cold Spring Harb. Symp. quant. Biol. 48, 527–538 (1983).
Rathjen, F. G. & Schachner, M. EMBO J. 3, 1–10 (1984).
Lindner, J., Rathjen, F. G. & Schachner, M. Nature 305, 427–430 (1983).
Rathjen, F. G. & Rutishauser, U. EMBO J. 3, 461–465 (1984).
Faissner, A., Kruse, J., Goridis, C., Bock, E. & Schachner, M. EMBO J. 3, 733–737 (1984).
Hirn, M., Pierres, M., Deagostini-Bazin, H., Hirsch, M. & Goridis, C. Brain Res. 214, 433–439 (1981).
Hirn, M., Ghandour, M. S., Deagostini-Bazin, H. & Goridis, C. Brain Res. 265, 87–100 (1983).
Abo, T. & Balch, C. M. J. Immun. 127, 1024–1029 (1981).
McGarry, R. C., Helfand, S. L., Quarles, R. H. & Roder, J. C. Nature 306, 376–378 (1983).
Schuller-Petrovic, S., Gebhart, W., Lassmann, H., Rumpold, H. & Kraft, D. Nature 306, 179–181 (1983).
Quartes, R. H., Johnson, D., Brady, R. O. & Sternberger, N. H. Neurochem. Res. 6, 1115–1127 (1981).
Spiro, R. G. Meth. Enzym. 8, 26–52 (1966).
Elder, J. H. & Alexander, S. Proc. natn. Acad. Sci. U.S.A. 79, 4540–4544 (1982).
Schnitzer, J. & Schachner, M. J. Neuroimmun. 1, 429–456 (1981).
Schnitzer, J., Franke, W. W. & Schachner, M. J. Cell Biol. 90, 447–475 (1981).
Sommer, I. & Schachner, M. Devl Biol. 83, 311–327 (1981).
Schachner, M., Kim, S. U. & Zehnle, R. Devl. Biol. 83, 328–338 (1981).
Sommer, I. & Schachner, M. Neurosci. Lett. 29, 183–188 (1982).
Schachner, M., Schoonmaker, G. & Hynes, R. O. Brain Res. 158, 149–158 (1978).
Itoyama, Y. et al. Ann. Neurol. 7, 167–177 (1980).
Sadoul, R., Hirn, M., Deagostini-Bazin, H., Rougon, G. & Goridis, C. Nature 304, 347–349 (1983).
Hoffman, S. & Edelman, G. M. Proc. natn. Acad. Sci. U.S.A. 80, 5762–5766 (1983).
Reutter, W., Köttgen, E., Bauer, C. & Gehrock, W., in Sialic acids; Chemistry, Metabolism and Function (ed. Schauer, R.) 263–305 (Springer, Berlin, 1982).
Latov, N. et al. Proc. natn. Acad. Sci. U.S.A. 75, 7139–7142 (1981).
Steck, A. J., Murray, N., Vandevelde, M. & Zurbriggen, A. J. Neuroimmunology 5, 145–156 (1983).
Stefansson, K. et al. Acta neuropath. (Berl.) 59, 255–261 (1983).
Palfree, R. G. E. & Elliot, B. E. J. immun. Meth. 52, 395–408 (1982).
Holmes, E. W. & O'Brien, J. S. Analyt. Biochem. 93, 167–170 (1979).
Neuhoff, V., Phillipp, K., Zimmer, H. G. & Mesecke, S. Hoppe-Seyler's Z. physiol. Chem. 360, 1657–1670 (1979).
Hirs, C. H. N. Meth. Enzym. 11, 411–413 (1967).
Gennarini, G., Hirn, M., Deagostini-Bazin, H. & Goridis, C. Eur. J. Biochem. (in the press).
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Kruse, J., Mailhammer, R., Wernecke, H. et al. Neural cell adhesion molecules and myelin-associated glycoprotein share a common carbohydrate moiety recognized by monoclonal antibodies L2 and HNK-1. Nature 311, 153–155 (1984). https://doi.org/10.1038/311153a0
Received:
Accepted:
Issue Date:
DOI: https://doi.org/10.1038/311153a0
This article is cited by
-
The dynamic brain N-glycome
Glycoconjugate Journal (2022)
-
Neural glycomics: the sweet side of nervous system functions
Cellular and Molecular Life Sciences (2021)
-
Anti-MAG IgM: differences in antibody tests and correlation with clinical findings
Neurological Sciences (2020)
-
The Adhesion Molecule-Characteristic HNK-1 Carbohydrate Contributes to Functional Recovery After Spinal Cord Injury in Adult Zebrafish
Molecular Neurobiology (2017)
-
HNK-1 Carrier Glycoproteins Are Decreased in the Alzheimer’s Disease Brain
Molecular Neurobiology (2017)
Comments
By submitting a comment you agree to abide by our Terms and Community Guidelines. If you find something abusive or that does not comply with our terms or guidelines please flag it as inappropriate.