1. Methionine sulfoxides on Pr[P.sup.Sc]: a prion-specific covalent signature
- Author
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Canello, Tamar, Engelstein, Roni, Moshel, Ofra, Xanthopoulos, Konstantinos, Juanes, Maria E., Langeveld, Jan, Sklaviadis, Theodoros, Gasset, Maria, and Gabizon, Ruth
- Subjects
Mass spectrometry -- Usage ,Methionine -- Chemical properties ,Oxidation-reduction reaction -- Analysis ,Prion diseases -- Research ,Biological sciences ,Chemistry - Abstract
The unique recognition properties of [alpha]PrP mAb IPC2, protein chemistry and state of the art mass spectrometry are used for showing that while a large fraction of the methionine residues in brain Pr[P.sup.Sc] are present as methionine sulfoxides this modification could not be found on brain Pr[P.sup.C] as well as on its recombinant models. The results have shown that accumulation of Pr[P.sup.Sc] and thereafter the pathogenesis of prion disease has resulted from the poor degradation of oxidized aberrantly folded PrP.
- Published
- 2008