1. TSG-6 transfers proteins between glycosaminoglycans via a Ser28-mediated covalent catalytic mechanism.
- Author
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Sanggaard KW, Sonne-Schmidt CS, Krogager TP, Kristensen T, Wisniewski HG, Thøgersen IB, and Enghild JJ
- Subjects
- Carbon chemistry, Catalysis, Cell Adhesion Molecules chemistry, Cell Line, Cross-Linking Reagents chemistry, Cross-Linking Reagents pharmacology, Humans, Mass Spectrometry methods, Molecular Conformation, Peptides chemistry, Protein Binding, Recombinant Proteins chemistry, Sodium Dodecyl Sulfate chemistry, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization, Cell Adhesion Molecules physiology, Glycosaminoglycans chemistry, Serine chemistry
- Abstract
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.
- Published
- 2008
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