Two forms of 1B236/myelin-associated glycoprotein, a cell adhesion molecule for postnatal neural development, are produced by alternative splicing.
- 1 June 1987
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 84 (12), 4337-4341
- https://doi.org/10.1073/pnas.84.12.4337
Abstract
The structures of two rat brain-specific 1B236 mRNAs, alternative specific products from a single gene regulated differently during postnatal brain devleopment, were deduced from full-length cDNA clones. The 626- and 582-amino acids-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 structure 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.This publication has 29 references indexed in Scilit:
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