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Demonstration of an extensive tras-tubular network continuous with the golgi-apparatus stack that may function in glycosylation

Academic Article
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Overview

authors

  • Roth, J.
  • Taatjes, D. J.
  • Lucocq, J. M.
  • Weinstein, J.
  • Paulson, James

publication date

  • 1985

journal

  • Cell  Journal

abstract

  • Sialyltransferase (Gal beta 1,4GlcNAc alpha 2,6 sialyltransferase) was localized by immunoelectron microscopy in rat liver hepatocytes using affinity-purified antibodies. Immunoreactivity for sialyltransferase was found in the Golgi apparatus, where it was restricted to an interconnected system consisting of the trans-cisternae and the trans-tubular network. This region of the Golgi apparatus exhibited both TPPase and CMPase activity and was the intracellular site where sialic acid residues bound to glycoprotein were detected using the Limax flavus lectin. Sialyltransferase and sialic acid residues were not detected in medial and cis-cisternae of the Golgi apparatus. These findings suggest that in rat hepatocytes sialylation of N-linked glycoproteins occurs in the complex formed by the trans-cisternae and the trans-tubular network of Golgi apparatus.

subject areas

  • Animals
  • Glycoproteins
  • Golgi Apparatus
  • Immunologic Techniques
  • Liver
  • Microscopy, Electron
  • Nucleotidases
  • Rats
  • Sialic Acids
  • Sialyltransferases
  • Thiamine Pyrophosphatase
  • Transferases
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Identity

International Standard Serial Number (ISSN)

  • 0092-8674

Digital Object Identifier (DOI)

  • 10.1016/0092-8674(85)90034-0

PubMed ID

  • 3000603
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Additional Document Info

start page

  • 287

end page

  • 295

volume

  • 43

issue

  • 1

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