Investigating the effect of VEGF glycosylation on glycosaminoglycan binding and protein unfolding

Biochem Biophys Res Commun. 2006 Feb 17;340(3):836-9. doi: 10.1016/j.bbrc.2005.12.079. Epub 2005 Dec 21.

Abstract

VEGF165 binding to endothelial cells is potentiated by glycosaminoglycans (GAGs). Here, we have investigated the impact of VEGF165 N-glycosylation on GAG binding. Although glycosylated VEGF165 bound to heparin with only slightly higher affinity than non-glycosylated VEGF165, the natural ligand heparan sulfate induced a conformational change only in the glycosylated protein. Unfolding studies of the VEGF proteins indicated a stabilising effect of heparin on the growth factor structure.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Calorimetry
  • Cell Line
  • Circular Dichroism
  • Cloning, Molecular
  • DNA, Complementary / metabolism
  • Dose-Response Relationship, Drug
  • Endothelium, Vascular / metabolism
  • Glycosaminoglycans / chemistry*
  • Glycosylation
  • Growth Substances
  • Heparin / chemistry
  • Heparitin Sulfate / chemistry
  • Humans
  • Insecta
  • Kinetics
  • Ligands
  • Protein Binding
  • Protein Conformation
  • Protein Denaturation
  • Protein Folding
  • Protein Structure, Secondary
  • Temperature
  • Time Factors
  • Ultraviolet Rays
  • Vascular Endothelial Growth Factor A / chemistry*
  • Vascular Endothelial Growth Factor A / metabolism

Substances

  • DNA, Complementary
  • Glycosaminoglycans
  • Growth Substances
  • Ligands
  • Vascular Endothelial Growth Factor A
  • Heparin
  • Heparitin Sulfate