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Site-specific Identification of Glutathionylation

ABSTRACT: Cardiomyocytes proteins were investigated for their glutathionylation in response to hydrogen peroxide generated from glucose oxidase and using a clickable glutathione derivative. After exposure, or not, to hydrogen peroxide the glutathionylated proteins were enriched and LC-MS/MS analyses was performed.

INSTRUMENT(S): Orbitrap Fusion

ORGANISM(S): Mus Musculus (mouse)

TISSUE(S): Cell Culture

SUBMITTER: garrett vanhecke

LAB HEAD: Young-Hoon Ahn

PROVIDER: PXD012171 | Pride | 2019-03-06

REPOSITORIES: Pride

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			Action	DRS
	2060-Ahn (peptides_1_1_0.mzid).mzid_2060-Ahn_(peptides_1_1_0.mzid).pride.mgf.gz	Mzid
	2060-Ahn (peptides_1_1_0.mzid).pride.mztab.gz	Mztab
	2060-Ahn.raw	Raw
	2060-Ahnpeptides_1_1_0.mzid.mzid.gz	Mzid
	2060-Ahnpeptides_1_1_0.mzid.mzid_2060-Ahn_peptides_1_1_0.mzid.MGF	Mzid

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Publications

Proteomic Identification of Protein Glutathionylation in Cardiomyocytes.

VanHecke Garrett C GC Abeywardana Maheeshi Yapa MY Ahn Young-Hoon YH

Journal of proteome research 20190311 4

Reactive oxygen species (ROS) are important signaling molecules, but their overproduction is associated with many cardiovascular diseases, including cardiomyopathy. ROS induce various oxidative modifications, among which glutathionylation is one of the significant protein oxidations that occur under oxidative stress. Despite previous efforts, direct and site-specific identification of glutathionylated proteins in cardiomyocytes has been limited. In this report, we used a clickable glutathione ap ...[more]

PMID: 30831029

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