The anti-angiogenic peptide anginex greatly enhances galectin-1 binding affinity for glycoproteins

J Biol Chem. 2011 Apr 22;286(16):13801-4. doi: 10.1074/jbc.C111.229096. Epub 2011 Mar 3.

Abstract

Angiogenesis is a key event in cancer progression and therefore a promising target in cancer treatment. Galectin-1, a β-galactoside binding lectin, is up-regulated in the endothelium of tumors of different origin and has been shown to be the target for anginex, a powerful anti-angiogenic peptide with anti-tumor activity. Here we show that when bound to anginex, galectin-1 binds various glycoproteins with hundred- to thousand-fold higher affinity. Anginex also interacts with galectin-2, -7, -8N, and -9N but not with galectin-3, -4, or -9C.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Angiogenesis Inhibitors / chemistry
  • Angiogenesis Inhibitors / pharmacology*
  • Disaccharides / chemistry
  • Fluorescence Polarization / methods
  • Galectin 1 / biosynthesis*
  • Galectins / chemistry
  • Glycoconjugates / chemistry
  • Glycoproteins / chemistry*
  • Haptoglobins / chemistry
  • Humans
  • Kinetics
  • Lectins / chemistry
  • Microscopy, Fluorescence / methods
  • Neoplasms / metabolism
  • Peptides / chemistry
  • Peptides / pharmacology*
  • Protein Binding
  • alpha-Fetoproteins / chemistry

Substances

  • Angiogenesis Inhibitors
  • Disaccharides
  • Galectin 1
  • Galectins
  • Glycoconjugates
  • Glycoproteins
  • Haptoglobins
  • Lectins
  • Peptides
  • alpha-Fetoproteins
  • anginex peptide