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Accepted (AM)Open Access (License Unspecified), Open
Journal article
Proteomic Identification of Protein Glutathionylation in Cardiomyocytes
Journal of proteome research, v 18(4), pp 1806-1818
05 Apr 2019
PMID: 30831029
Featured in Collection : UN Sustainable Development Goals @ Drexel
Abstract
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 approach in a HL-1 mouse cardiomyocyte cell line under exposure to hydrogen peroxide, finding 1763 glutathionylated peptides with specific Cys modification sites, which include many muscle-specific proteins. Bioinformatic and cluster analyses found 125 glutathionylated proteins, whose mutations or dysfunctions are associated with cardiomyopathy, many of which include sarcomeric structural and contractile proteins, chaperone, and other signaling or regulatory proteins. We further provide functional implication of glutathionylation for several identified proteins, including CSRP3/MLP and complex I, II, and III, by analyzing glutathionylated sites in their structures. Our report establishes a chemoselective method for direct identification of glutathionylated proteins and provides potential target proteins whose glutathionylation may contribute to muscle diseases.
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Details
- Title
- Proteomic Identification of Protein Glutathionylation in Cardiomyocytes
- Creators
- Garrett C VanHecke - Wayne State UniversityMaheeshi Yapa Abeywardana - Wayne State UniversityYoung-Hoon Ahn - Wayne State University
- Publication Details
- Journal of proteome research, v 18(4), pp 1806-1818
- Publisher
- American Chemical Society; Washington, DC
- Grant note
- R01 HL131740 / NHLBI NIH HHS P30 ES020957 / NIEHS NIH HHS S10 OD010700 / NIH HHS
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- College of Arts and Sciences; Chemistry; Drexel University
- Web of Science ID
- WOS:000464068900030
- Scopus ID
- 2-s2.0-85063124128
- Other Identifier
- 991020100064504721
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- Web of Science research areas
- Biochemical Research Methods