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

Academic Article
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Overview

authors

  • Bloom, Floyd
  • Brow, M. A.
  • Lai, C.
  • Milner, R, J.
  • Nave, K. A.
  • Noronha, A. B.
  • Quarles, R. H.
  • Sutcliffe, J. Gregor

publication date

  • 1987

journal

  • Proceedings of the National Academy of Sciences of the United States of America  Journal

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.

subject areas

  • Aging
  • Amino Acid Sequence
  • Animals
  • Antigens, Surface
  • Base Sequence
  • Brain
  • Cell Adhesion
  • Cell Adhesion Molecules
  • Cloning, Molecular
  • DNA
  • Genes
  • Myelin Proteins
  • Myelin-Associated Glycoprotein
  • RNA Splicing
  • RNA, Messenger
  • Rats
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Identity

PubMed Central ID

  • PMC305080

International Standard Serial Number (ISSN)

  • 0027-8424

Digital Object Identifier (DOI)

  • 10.1073/pnas.84.12.4337

PubMed ID

  • 2438699
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Additional Document Info

start page

  • 4337

end page

  • 4341

volume

  • 84

issue

  • 12

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