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

J Roth, D J Taatjes, J M Lucocq, J Weinstein, J C Paulson

Research output: Contribution to journalArticlepeer-review

349 Citations (Scopus)

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.
Original languageEnglish
Pages (from-to)287-95
Number of pages9
JournalCell
Volume43
Issue number1
Publication statusPublished - Nov 1985

Keywords

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

Fingerprint

Dive into the research topics of 'Demonstration of an extensive trans-tubular network continuous with the Golgi apparatus stack that may function in glycosylation'. Together they form a unique fingerprint.

Cite this