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Mapping of 3 carbohydrate attachment sites in embryonic and adult forms of the neural cell-adhesion molecule

Academic Article
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Overview

authors

  • Crossin, Kathryn
  • Edelman, Gerald
  • Cunningham, Bruce

publication date

  • 1984

journal

  • Journal of Cell Biology  Journal

abstract

  • The sialic-rich carbohydrate moiety of the neural cell adhesion molecule (N-CAM) undergoes major structural changes during development and plays a significant role in altering the homophilic binding of the molecule. In order to understand the mechanism of these changes, a cyanogen bromide (CNBr) fragment that contained 90% of the sialic acid of N-CAM was isolated and characterized according to the number of carbohydrate attachment sites and reactivity with specific monoclonal antibodies. The CNBr sialopeptide migrated on SDS PAGE as a broad zone of Mr 42,000-60,000. Upon treatment with neuraminidase, it was converted to a single component of Mr 42,000, and subsequent, limited treatment with endoglycosidase F gave four evenly spaced components of Mr 35,000-42,000, suggesting that it contained three attachment sites for N-linked oligosaccharides. The fragment reacted with monoclonal antibody 15G8, which detects the sialic acid in embryonic N-CAM, and with a monoclonal antibody, anti-(N-CAM) No. 2. Treatment with neuraminidase or with endoglycosidase F destroyed reactivity with 15G8 but not with anti-(N-CAM) No. 2. A similar CNBr sialopeptide was obtained from adult N-CAM; it contained sialic acid, had three N-linked oligosaccharides and reacted with anti-(N-CAM) No. 2 but not with 15G8 monoclonal antibodies. A peptide fragment, Fr2, comprising the NH2 terminal and middle regions of the molecule yielded a CNBr fragment closely similar to the fragment obtained from the whole molecule. The CNBr fragment from Fr2 reacted with monoclonal antibody anti-(N-CAM) No. 2. Fr1, comprising the NH2 terminal region alone, failed to react. These data confirm that the majority of the sialic acid is localized in the middle region of the N-CAM molecule and support the hypothesis that embryonic to adult conversion of N-CAM is the result of differences in sialidase or sialytransferase activity.

subject areas

  • Aging
  • Amino Acids
  • Animals
  • Antibodies, Monoclonal
  • Antigens, Surface
  • Carbohydrate Metabolism
  • Cell Adhesion Molecules
  • Chick Embryo
  • Chickens
  • Cyanogen Bromide
  • Immunologic Techniques
  • Molecular Weight
  • N-Acetylneuraminic Acid
  • Neuraminidase
  • Peptide Fragments
  • Sialic Acids
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Identity

International Standard Serial Number (ISSN)

  • 0021-9525

Digital Object Identifier (DOI)

  • 10.1083/jcb.99.5.1848

PubMed ID

  • 6386828
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Additional Document Info

start page

  • 1848

end page

  • 1855

volume

  • 99

issue

  • 5

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