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Journal article
Isotopically Labeled Clickable Glutathione to Quantify Protein S-Glutathionylation
Chembiochem : a European journal of chemical biology, v 21(6), pp 853-859
16 Mar 2020
PMID: 31560820
Featured in Collection : UN Sustainable Development Goals @ Drexel
Abstract
Protein S-glutathionylation is one of the important cysteine oxidation events that regulate various redox-mediated biological processes. Despite several existing methods, there are few proteomic approaches to identify and quantify specific cysteine residues susceptible to S-glutathionylation. We previously developed a clickable glutathione approach that labels intracellular glutathione with azido-Ala by using a mutant form of glutathione synthetase. In this study, we developed a quantification strategy with clickable glutathione by using isotopically labeled heavy and light derivatives of azido-Ala, which provides the relative quantification of glutathionylated peptides in mass spectrometry-based proteomic analysis. We applied isotopically labeled clickable glutathione to HL-1 cardiomyocytes, quantifying relative levels of 1398 glutathionylated peptides upon addition of hydrogen peroxide. Importantly, we highlight elevated levels of glutathionylation on sarcomere-associated muscle proteins while validating glutathionylation of two structural proteins, alpha-actinin and desmin. Our report provides a chemical proteomic strategy to quantify specific glutathionylated cysteines.
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Details
- Title
- Isotopically Labeled Clickable Glutathione to Quantify Protein S-Glutathionylation
- Creators
- Garrett C. VanHecke - Wayne State UniversityMaheeshi Yapa Abeywardana - Wayne State UniversityBo Huang - Wayne State UniversityYoung-Hoon Ahn - Wayne State University
- Publication Details
- Chembiochem : a European journal of chemical biology, v 21(6), pp 853-859
- Publisher
- Wiley
- Number of pages
- 7
- Grant note
- P30 CA 02253 / NIH Cancer Center Support Grant; United States Department of Health & Human Services; National Institutes of Health (NIH) - USA Wayne State University Research Award P30 ES 020957 / NIH Center Grant; United States Department of Health & Human Services; National Institutes of Health (NIH) - USA S10 OD 010700 / NIH Shared Instrumentation Grant; United States Department of Health & Human Services; National Institutes of Health (NIH) - USA R01 HL131740 / US National Institutes of Health (NIH); United States Department of Health & Human Services; National Institutes of Health (NIH) - USA
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- College of Arts and Sciences; Chemistry; Drexel University
- Web of Science ID
- WOS:000493018200001
- Scopus ID
- 2-s2.0-85074616978
- Other Identifier
- 991020100058304721
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InCites Highlights
Data related to this publication, from InCites Benchmarking & Analytics tool:
- Web of Science research areas
- Biochemistry & Molecular Biology
- Chemistry, Medicinal