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. 1987 Jun;84(12):4337–4341. doi: 10.1073/pnas.84.12.4337

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

C Lai, M A Brow, K A Nave, A B Noronha, R H Quarles, F E Bloom, R J Milner, J G Sutcliffe
PMCID: PMC305080  PMID: 2438699

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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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