Improved integrative analysis of the thiol redox proteome using filter-aided sample preparation

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Documents

  • Elena Bonzon-Kulichenko
  • Emilio Camafeita
  • Juan Antonio Lopez
  • Maria Gomez-Serrano
  • Inmaculada Jorge
  • Enrique Calvo
  • Estefania Nunez
  • Marco Trevisan-Herraz
  • Bagwan, Navratan
  • Jose Antonio Barcena
  • Belen Peral
  • Jesus Vazquez
Changes in the oxidation state of protein Cys residues are involved in cell signalling and play a key role in a variety of pathophysiological states. We had previously developed GELSILOX, an in-gel method that enables the large-scale, parallel analysis of dynamic alterations to the redox state of Cys sites and protein abundance changes. Here we present FASILOX, a further development of the GELSILOX approach featuring: i) significantly increased peptide recovery, ii) enhanced sensitivity for the detection of Cys oxidative alterations, and iii) streamlined workflow that results in shortened assay duration. In mitochondria isolated from the adipose tissue of obese, diabetic patients, FASILOX revealed a sexually dimorphic trait of Cys oxidation involving mainly mitochondrial oxidative phosphorylation complexes. These results provide the first evidence for a decreased efficiency in the antioxidant response of men as compared to women.
Original languageEnglish
Article number103624
JournalJournal of Proteomics
Volume214
ISSN1874-3919
DOIs
Publication statusPublished - 2020

    Research areas

  • Thiol redox proteome, Filter-aided sample preparation, FASILOX, Cys oxidation, Adipose tissue, Sexual dimorphism

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