Two forms of 1B236/myelin-associated glycoprotein, a cell adhesion molecule for 
postnatal neural development, are produced by alternative splicing

Lai, C; Brow, M A; Nave, K.-A.; Noronha, A B; Quarles, R H; Bloom, F E; Milner, R J; Sutcliffe, J G

doi:10.1073/pnas.84.12.4337

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Two forms of 1B236/myelin-associated glycoprotein, a cell adhesion molecule for postnatal neural development, are produced by alternative splicing

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Nave, K.-A.
Neurogenetics, Max Planck Institute of Experimental Medicine, Max Planck Society;

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Citation

Lai, C., Brow, M. A., Nave, K.-A., Noronha, A. B., Quarles, R. H., Bloom, F. E., et al. (1987). Two forms of 1B236/myelin-associated glycoprotein, a cell adhesion molecule for postnatal neural development, are produced by alternative splicing. Proceedings of the National Academy of Sciences of the United States of America, 84(12), 4337-4341. doi:10.1073/pnas.84.12.4337.

Cite as: https://hdl.handle.net/21.11116/0000-000D-2BF4-0

Abstract

The structures of two rat brain-specific 1B236 mRNAs, alternative splice products from a single gene regulated differently during postnatal brain development, were deduced from full-length cDNA clones. The 626- and 582-amino acid-long encoded proteins are indistinguishable from two forms of myelin-associated glycoprotein, a cell adhesion molecule involved in axonal-glial and glial-glial interactions in postnatal brain development, particularly in myelination. The two proteins share a single membrane-spanning domain and a glycosylated N terminus but differ in the structures of their C termini. The N terminus consists of five domains related in sequence to each other and to immunoglobulin-like molecules, especially the neural cell adhesion molecule N-CAM, suggesting a common structure for cell adhesion molecules.