Glycoconjugate Journal

, Volume 1, Issue 1, pp 51–61 | Cite as

Decreased UDP-GlcNAc:Glycopeptideβ-2-N-Acetylglucosaminyltransferase II activity in a ricin-resistant mutant of baby hamster kidney (BHK) cells

  • Saroja Narasimhan
  • Stephen Allen
  • R Colin Hughes
  • Harry Schachter
Article

Abstract

The ricin-resistant mutant baby hamster kidney (BHK) cell line RICR21 is unable to make the sialylated bi- or triantennary complexN-glycans found in wild type cells and accumulates instead non-bisected hybrid structures containing three Man residues and one or two sialylated antennae (Hugheset al 1983, Carbohydr Res 120215-34). Specific assays forN-acetylglucosaminyltransferases I, II, III and IV were applied to Triton X-100 extracts of wild type BHK, RICR14 and RICR21 cells. It was shown that RICR21 cell extracts had a decreasedN-acetylglucosaminyltransferase II specific activity (17 to 27% of wild type values). It is suggested that in wild type cellsN-acetylglucosaminyltransferase II action proceeds quickly, leading to complexN-glycan synthesis, while in RICR21 cells potential substrates forN-acetylglucosaminyltransferase II move into the trans-Golgi compartment before the transferase can act, thereby leading to hybrid structures.

Key words

N-acetylglucosaminyltransferase lectin hybrid oligosaccharides ricin-resistant mutants 

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Copyright information

© Glycoconjugate Journal 1984

Authors and Affiliations

  • Saroja Narasimhan
    • 1
  • Stephen Allen
    • 1
  • R Colin Hughes
    • 2
  • Harry Schachter
    • 1
  1. 1.Research Institute, Hospital for Sick Children and Dept. of BiochemistryUniv. of TorontoTorontoCanada
  2. 2.National Institute for Medical ResearchLondonUK

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