Glycosylation of annexin I and annexin II

Biochem Biophys Res Commun. 1992 Oct 30;188(2):554-8. doi: 10.1016/0006-291x(92)91091-4.

Abstract

Human placental annexin I and annexin II were shown to be glycosylated by one-dimensional affinity blotting with the lectin concanavalin A, which recognizes D-mannose and D-glucose residues. Further evidence that annexin I and annexin II are glycosylated was provided by the finding that these proteins incorporated D-[2,6-3H]mannose and D-[6-3H]glucose when they were biosynthesized by the human squamous carcinoma cell line SqCC/Y1. Annexin I and annexin II could be rapidly purified from a human placental membrane extract by concanavalin A-Sepharose, which indicated that these proteins contain two biantennary mannosyl residues.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Annexin A1 / biosynthesis*
  • Annexin A1 / isolation & purification
  • Annexin A2 / biosynthesis*
  • Annexin A2 / isolation & purification
  • Carcinoma, Squamous Cell
  • Cell Membrane / chemistry
  • Chromatography, Affinity
  • Female
  • Glucose / metabolism
  • Glycosylation
  • Humans
  • Mannose / metabolism
  • Methionine / metabolism
  • Placenta / chemistry
  • Pregnancy
  • Tumor Cells, Cultured

Substances

  • Annexin A1
  • Annexin A2
  • Methionine
  • Glucose
  • Mannose