German researchers map disease-relevant protein modifications
Martinsried – Researchers from the Max Planck Insitute for Biochemistry have presented a novel technique that enables them to map the entire pattern of N-glycosylation (linking a sugar to the amino acid asparagine) and the localisation in different cell types (Cell 141(5), 897-907). In a first step, the proteome researchers headed by Matthias Mann enriched the glycopeptides by binding them to lectin moieties immobilised on a filter surface. They then mapped 6,367 N-glycosylation sites in 2,352 proteins by mass spectometry, 5753 of them formerly unknown. Combining this new approach with an analysis of subcellular glycosites revealed that the sites were always orientated towards the extracellular space of the lumen of intracellular compartments.The researchers identified several new glycosylation sites associated with diseases such as Alzheimer’s or Creutzfeld-Jacob disease. Up until now, the transformation of proteins by has been widely unexplored and scientists hope that the results of this study will contribute to the identification of new disease targets and biomarkers.