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

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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.
Original languageEnglish
JournalJournal of Biological Chemistry
Volume283
Issue49
Pages (from-to)33919-26
Number of pages8
ISSN0021-9258
DOIs
Publication statusPublished - 5 Dec 2008

    Research areas

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

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