Journal
JOURNAL OF PROTEOMICS
Volume 214, Issue -, Pages -Publisher
ELSEVIER
DOI: 10.1016/j.jprot.2019.103624
Keywords
Thiol redox proteome; Filter-aided sample preparation; FASILOX; Cys oxidation; Adipose tissue; Sexual dimorphism
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Funding
- Spanish Ministry of Science, Innovation and Universities [BI02015-67580-P, PGC2018-097019-B-I00, RTI2018-093864-B-100]
- Ministry of Economy, Industry and Competitiveness through the Carlos III Institute of Health-Fondo de Investigation Sanitaria grant PRB3 (ISCIII-SGEFI/ERDF, ProteoRed) [BFU2016-80006-P, IPT17/0019]
- Fundacio MaratoTV3 [122/C/2015]
- la Caixa Banking Foundation [HR17-00247]
- Instituto de Salud Carlos III (ISCIII)
- Ministerio de Ciencia, Innovation y Universidades (MCNU)
- Pro CNIC Foundation
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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.
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