Improved integrative analysis of the thiol redox proteome using filter-aided sample preparation
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Improved integrative analysis of the thiol redox proteome using filter-aided sample preparation. / Bonzon-Kulichenko, Elena; Camafeita, Emilio; Antonio Lopez, Juan; Gomez-Serrano, Maria; Jorge, Inmaculada; Calvo, Enrique; Nunez, Estefania; Trevisan-Herraz, Marco; Bagwan, Navratan; Antonio Barcena, Jose; Peral, Belen; Vazquez, Jesus.
In: Journal of Proteomics, Vol. 214, 103624, 2020.Research output: Contribution to journal › Journal article › Research › peer-review
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TY - JOUR
T1 - Improved integrative analysis of the thiol redox proteome using filter-aided sample preparation
AU - Bonzon-Kulichenko, Elena
AU - Camafeita, Emilio
AU - Antonio Lopez, Juan
AU - Gomez-Serrano, Maria
AU - Jorge, Inmaculada
AU - Calvo, Enrique
AU - Nunez, Estefania
AU - Trevisan-Herraz, Marco
AU - Bagwan, Navratan
AU - Antonio Barcena, Jose
AU - Peral, Belen
AU - Vazquez, Jesus
PY - 2020
Y1 - 2020
N2 - 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.
AB - 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.
KW - Thiol redox proteome
KW - Filter-aided sample preparation
KW - FASILOX
KW - Cys oxidation
KW - Adipose tissue
KW - Sexual dimorphism
U2 - 10.1016/j.jprot.2019.103624
DO - 10.1016/j.jprot.2019.103624
M3 - Journal article
C2 - 31874222
VL - 214
JO - Journal of Proteomics
JF - Journal of Proteomics
SN - 1874-3919
M1 - 103624
ER -
ID: 237418814