TSG-6 transfers proteins between glycosaminoglycans via a Ser28-mediated covalent catalytic mechanism

J Biol Chem. 2008 Dec 5;283(49):33919-26. doi: 10.1074/jbc.M804240200. Epub 2008 Sep 26.


Studies of the interaction between Bikunin proteins, tumor necrosis factor-stimulated gene-6 protein (TSG-6), and glycosaminoglycans have revealed a unique catalytic activity where TSG-6/heavy chain 2 transfer heavy chain subunits between glycosaminoglycan chains. The activity is mediated by TSG-6/heavy chain 2 and involves a transient SDS stable interaction between TSG-6 and the heavy chain to be transferred. The focus of this study was to characterize the molecular structure of this cross-link to gain further insight into the catalytic mechanism. The result showed that the C-terminal Asp residue of the heavy chains forms an ester bond to Ser(28) beta-carbon of TSG-6 suggesting that this residue plays a role during catalysis.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Carbon / chemistry
  • Catalysis
  • Cell Adhesion Molecules / chemistry
  • Cell Adhesion Molecules / physiology*
  • Cell Line
  • Cross-Linking Reagents / chemistry
  • Cross-Linking Reagents / pharmacology
  • Glycosaminoglycans / chemistry*
  • Humans
  • Mass Spectrometry / methods
  • Molecular Conformation
  • Peptides / chemistry
  • Protein Binding
  • Recombinant Proteins / chemistry
  • Serine / chemistry*
  • Sodium Dodecyl Sulfate / chemistry
  • Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization


  • Cell Adhesion Molecules
  • Cross-Linking Reagents
  • Glycosaminoglycans
  • Peptides
  • Recombinant Proteins
  • TNFAIP6 protein, human
  • Sodium Dodecyl Sulfate
  • Serine
  • Carbon