The presence of N-glycosylated proteins in cell nuclei

Biochem Biophys Res Commun. 1991 Aug 15;178(3):1365-70. doi: 10.1016/0006-291x(91)91044-d.

Abstract

The protein-DNA crosslinking capability of cis-dichloro diammineplatinum has been exploited to check the intranuclear location of N-glycosylated proteins. When intact liver cells were treated with this reagent, a number of glycoproteins, recognized by Concanavalin A, have been shown to become crosslinked to DNA; many of them have been recognized as nuclear matrix components. The recognition by this lectin was abolished by treatment with N-glycosidase F, showing the presence of N-glycosidic bonds between the sugar moiety and the protein. Most of the glycoproteins appeared to have high mannose oligosaccharide chains, but sialic acid containing oligosaccharides were also identified.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Cattle
  • Cell Nucleus / metabolism*
  • Chickens
  • Cisplatin / pharmacology*
  • Concanavalin A
  • Cross-Linking Reagents
  • DNA / isolation & purification
  • DNA / metabolism*
  • Glycoproteins / isolation & purification
  • Glycoproteins / metabolism*
  • Glycosylation
  • Liver / metabolism*
  • Protein Binding
  • Swine

Substances

  • Cross-Linking Reagents
  • Glycoproteins
  • Concanavalin A
  • DNA
  • Cisplatin