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Post-translational modifications of FDA-approved plasma biomarkers in glioblastoma samples
Author(s) -
Н. А. Петушкова,
Victor G. Zgoda,
Mikhail A. Pyatnitskiy,
О. В. Ларина,
N. B. Teryaeva,
А А Потапов,
Andrey Lisitsa
Publication year - 2017
Publication title -
plos one
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.99
H-Index - 332
ISSN - 1932-6203
DOI - 10.1371/journal.pone.0177427
Subject(s) - acetylation , ubiquitin , tandem mass spectrometry , phosphorylation , glioblastoma , chemistry , computational biology , biology , bioinformatics , cancer research , mass spectrometry , biochemistry , chromatography , gene
Liquid chromatography-tandem mass spectrometry was used to analyze plasma proteins of volunteers (control) and patients with glioblastoma multiform (GBM). A database search was pre-set with a variable post-translational modification (PTM): phosphorylation, acetylation or ubiquitination. There were no significant differences between the control and the GBM groups regarding the number of protein identifications, sequence coverage or number of PTMs. However, in GBM plasma, we unambiguously observed a decreased fraction in post-translationally modified peptides identified with high quality. The disease-specific PTM patterns were extracted and mapped to the set of FDA-approved plasma protein markers. Decreases of 46% and 24% in the number of acetylated and ubiquitinated peptides, respectively, were observed in the GBM samples. Significance of capturing disease-associated patterns of protein modifications was envisaged.

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