Glycosylated forms of nuclear lamins

FEBS Lett. 1989 Nov 6;257(2):241-6. doi: 10.1016/0014-5793(89)81543-1.

Abstract

Chromatin and pore complex-lamina preparations were obtained from pig and chicken tissues, and their proteins were analysed by mono- and bidimensional electrophoresis. A glycosylated form of lamin A, recognized by concanavalin A, was shown to be present in at least 3 of the tissues examined. Glycosylation is suggested to be a further postsynthetic modification, besides phosphorylation and methylation, which can modify the properties of lamins.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Cell Nucleus / metabolism*
  • Chickens
  • Chromatin / metabolism
  • Concanavalin A / metabolism
  • Electrophoresis, Gel, Two-Dimensional
  • Glycosylation
  • Lamin Type A
  • Lamins
  • Molecular Weight
  • Nuclear Proteins / metabolism*
  • Swine

Substances

  • Chromatin
  • Lamin Type A
  • Lamins
  • Nuclear Proteins
  • Concanavalin A