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- W1988269315 abstract "Current clinical trials in Duchenne muscular dystrophy (DMD) would greatly benefit from objective measures for therapeutic efficacy. In order to avoid repeated muscle biopsies, we explored the serum as an alternative source for molecular biomarkers to assess disease severity and response to therapy, hypothesizing that the disrupted muscle integrity will be reflected in the serum proteome. In this study a combination of different bottom-up mass spectrometry (MS)-based proteomics workflows was applied to maximize the number of identifications of proteins from the serum. The serum samples were treated with a peptide ligand library (Proteominer™, Bio-Rad) to reduce the large dynamic range in protein concentration and thus relatively enrich the low and medium abundant proteins. The Proteominer-treated serum was fractionated on a gradient 1D-SDS gel. After in-gel digestion the resulting peptide mixtures were analysed on an LC- ion trap mass spectrometer. Proteominer treatment of serum samples resulted in an eightfold increase in the number of protein identifications when compared to untreated serum. Moreover, combining data from different enzymatic digestions with Lys-N and trypsin along with LC–ESI-MS/MS using collision-induced dissociation (CID) and electron transfer dissociation (ETD) fragmentation methods improved peptide identifications with respect to sequence coverage. We compared serum samples from healthy controls and DMD patients. The identified proteins which may serve as candidate biomarkers for DMD will be discussed at the meeting." @default.
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- W1988269315 date "2011-10-01" @default.
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- W1988269315 title "P1.49 Mass spectrometry based clinical proteomics for biomarker discovery in Duchenne muscular dystrophy" @default.
- W1988269315 doi "https://doi.org/10.1016/j.nmd.2011.06.809" @default.
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