Proteomics

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Clickable glutathione-based Isotope Coded Affinity Label to quantify glutathionylation

ABSTRACT: Identification of cysteines with high oxidation susceptibility is important for understanding redox-mediated biological processes associated with health and disease. We developed a chemical proteomic strategy that helps find cysteines with high susceptibility to S-glutathionylation. Our strategy is based on the isotopically labelled clickable glutathione derivatives that can quantify relative levels of glutathionylated and reduced forms (SSG vs. SH) of cysteines in mass spectrometry, which is named 'Clickable Glutathione-based Isotope-coded Affinity-Tag (G-ICAT).' The G-ICAT approach was applied to the mouse C2C12 cell line upon addition of hydrogen peroxide, finding 1,518 glutathionylated cysteines and their relative levels of SSG over SH upon adding hydron peroxide. This chemical proteomic strategy will significantly contribute to identifying functional cysteines regulated by glutathionylation in redox signaling.

INSTRUMENT(S): Orbitrap Fusion

ORGANISM(S): Mus Musculus (mouse)

TISSUE(S): Myoblast, Cell Culture

SUBMITTER: Young-Hoon Ahn  

LAB HEAD: Young-Hoon Ahn

PROVIDER: PXD034976 | Pride | 2024-03-07

REPOSITORIES: Pride

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Publications

Chemoproteomic strategy identified p120-catenin glutathionylation regulates E-cadherin degradation and cell migration.

Kukulage Dhanushika S K DSK   Yapa Abeywardana Maheeshi M   Matarage Don Nadee N J NNJ   Hu Ren-Ming RM   Shishikura Kyosuke K   Matthews Megan L ML   Ahn Young-Hoon YH  

Cell chemical biology 20230914 12

Identification of cysteines with high oxidation susceptibility is important for understanding redox-mediated biological processes. In this report, we report a chemical proteomic strategy that finds cysteines with high susceptibility to S-glutathionylation. Our proteomic strategy, named clickable glutathione-based isotope-coded affinity tag (G-ICAT), identified 1,518 glutathionylated cysteines while determining their relative levels of glutathionylated and reduced forms upon adding hydrogen perox  ...[more]

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