Acute and chronic blood serum proteome changes in patients with methanol poisoning

Abstract

Twenty-four blood serum samples from patients with acute methanol poisoning (M) from the mass methanol poisoning outbreak in the Czech Republic in 2012 were compared with 46 patient samples taken four years after poisoning (S) (overlap of 10 people with group M) and with a control group (C) of 24 samples of patients with a similar proportion of chronic alcohol abuse. When comparing any two groups, tens to hundreds of proteins with a significant change in concentration were identified. Fifteen proteins showed significant changes when compared between any two groups. The group with acute methanol poisoning showed significant changes in protein concentrations for at least 64 proteins compared to the other groups. Among the most important identified proteins closely related to intoxication are mainly those involved in blood coagulation, metabolism of vitamin A (increased retinol-binding protein), immune response (e.g., increased complement factor I, complement factors C3 and C5), and lipid transport (increased apolipoprotein A I, apolipoprotein A II, adiponectin). For blood coagulation, the most affected proteins with significant changes in the methanol poisoning group were von Willebrand factor, carboxypeptidase N, alpha-2-antiplasmin (all increased), inter-alpha-trypsin inhibitor heavy chain H4, kininogen-1, plasma serine protease inhibitor, plasminogen (all decreased). However, heparin administration used for the methanol poisoning group could have interfered with some of the changes in their concentrations. Data are available via ProteomeXchange with the identifier PXD035726.

Proteotypic peptides of hairs for the identification of common European domestic and wild animal species revealed by in‐sample protein digestion and mass spectrometry analysis

“…2020 [48] or Cejnar et al. 2022 [49]. Briefly, peptides in the raw spectra were identified and quantified by MaxQuant software (ver.…”

“…Peaks were identified and the normalized label-free quantification value intensities were extracted similarly as in Smirnova et al 2020 [48] or Cejnar et al 2022 [49]. Briefly, peptides in the raw spectra were identified and quantified by MaxQuant software (ver.…”

Characterization of vestibular schwannoma tissues using liquid chromatography‐tandem mass spectrometry analysis of specific peptide fragments separated by in‐sample tryptic protein digestion followed by mathematical analysis

“…The discrimination analysis (DA) of MS data was run similarly as in our previous studies [16,23]. Proteins in the raw spectra were identified and intensities were extracted by MaxQuant label-free quantification (LFQ) software (version 1.6.17 for Windows) [24] using the Homo sapiens NCBI protein database (assembly GRCh38.p14) and the UniProt Homo sapiens proteome database (UP000005640, accessed May 25, 2022).…”

“…Protein groups identified through target-decoy database strategy (the "Reverse" column in the MaxQuant proteinGroups file), proteins identified only by the MS/MS spectra for modified peptides (the "Only identified by site" column in the MaxQuant proteinGroups file), potential contaminants (on condition that all identifiers in the "Protein.IDs" column in the MaxQuant proteinGroups file start with the "CON_" prefix), and protein groups identified by less than two unique peptides (the "Unique peptides" column) were removed and are not included in any subsequent analyses. The overall protein intensity was computed similarly as in our previous studies [16,23]: for each unique peptide detected for a given protein, the MaxQuant LFQ value was divided by peptide length, and the maximum of these values was used as the protein intensity quantification value.…”

“…For partial least squares-discrimination analysis (PLS-DA) [26] and linear discriminant analysis over principal components (PCA-LDA), the data were centered and scaled, and the zero variance points were removed between the samples. Only proteins identified in at least 50% of the samples in any of the studied groups were used (similarly as in our previous study [23]). For the complete list of proteins and their quantified intensities see Table S2.…”