Proteomics

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Redox proteome analysis identifies reversible oxidized proteins in retinoic acid differentiated SH-SY5Y cells


ABSTRACT: Retinoic acid stimulated SH-SY5Y cells are a common model system to study the initial phases of neuronal differentiation. Although these processes are associated with redox-sensitive processes, no comprehensive analysis of oxidative modified cysteines, as one of the main targets for reactive oxygen species, was available. Here, we used quantitative and differential proteomics and redox proteomics, to fill this gap. Our results indicate, that alterations in the redox state very early in the differentiation process, affect the expression of marker proteins and the extension of neurites. The spatiotemporal analysis of reactive oxygen species, suggests a NOX-dependent peak in cytoplasmic O2.-/H2O2 level 2h after retinoic acid stimulation. At the same timepoint 241 out of 275 proteins with an altered cysteine redox state appeared to be reversibly oxidised in the retinoic acid treated samples. Our analyses suggest that redox alterations affect proteins involved in the retinoic acid homeostasis and cytoskeletal dynamics.

INSTRUMENT(S): LTQ Orbitrap Elite, Q Exactive

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Cell Culture, Neuroblast

SUBMITTER: Gereon Poschmann  

LAB HEAD: Gereon Poschmann

PROVIDER: PXD014381 | Pride | 2020-03-30

REPOSITORIES: Pride

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Publications

The Proteomic Landscape of Cysteine Oxidation That Underpins Retinoic Acid-Induced Neuronal Differentiation.

Brenig Katrin K   Grube Leonie L   Schwarzländer Markus M   Köhrer Karl K   Stühler Kai K   Poschmann Gereon G  

Journal of proteome research 20200403 5


The initial phases of neuronal differentiation are key to neuronal function. A particularly informative model to study these initial phases are retinoic acid-stimulated SH-SY5Y cells. Although these progressions are associated with redox-sensitive processes, it is largely undefined how the cellular proteome underpins redox dynamics and the management of reactive oxygen species. Here, we map the global cysteine-based redox landscape of SH-SY5Y cells using quantitative redox proteomics. We find ev  ...[more]

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