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Title: Fatiguing contractions increase protein S-glutathionylation occupancy in mouse skeletal muscle

Abstract

Protein S-glutathionylation is an important reversible post-translational modification implicated in redox signaling. Oxidative modifications to protein thiols can alter the activity of metabolic enzymes, transcription factors, kinases, phosphatases, and the function of contractile proteins. However, the extent to which muscle contraction induces oxidative modifications in redox sensitive thiols is not known. The purpose of this study was to determine the targets of S-glutathionylation redox signaling following fatiguing contractions. Anesthetized adult male CB6F1 (BALB/cBy × C57BL/6) mice were subjected to acute fatiguing contractions for 15 min using in vivo stimulations. The right (stimulated) and left (unstimulated) gastrocnemius muscleswere collected 60 min after the last stimulation and processed for redox proteomics assay of S-glutathionylation.

Authors:
 [1];  [2];  [2];  [2];  [1];  [1];  [2];  [1]
  1. Univ. of Washington, Seattle, WA (United States)
  2. Pacific Northwest National Lab. (PNNL), Richland, WA (United States)
Publication Date:
Research Org.:
Pacific Northwest National Lab. (PNNL), Richland, WA (United States)
Sponsoring Org.:
USDOE
OSTI Identifier:
1439099
Grant/Contract Number:
AC05-76RL01830
Resource Type:
Journal Article: Accepted Manuscript
Journal Name:
Redox Biology
Additional Journal Information:
Journal Volume: 17; Journal Issue: C; Journal ID: ISSN 2213-2317
Publisher:
Elsevier
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; Muscle contraction; Post-translational modification; S-glutathionylation; Redox signaling; Skeletal muscle; Thiol redox proteomics

Citation Formats

Kramer, Philip A., Duan, Jicheng, Gaffrey, Matthew J., Shukla, Anil K., Wang, Lu, Bammler, Theo K., Qian, Wei -Jun, and Marcinek, David J. Fatiguing contractions increase protein S-glutathionylation occupancy in mouse skeletal muscle. United States: N. p., 2018. Web. doi:10.1016/j.redox.2018.05.011.
Kramer, Philip A., Duan, Jicheng, Gaffrey, Matthew J., Shukla, Anil K., Wang, Lu, Bammler, Theo K., Qian, Wei -Jun, & Marcinek, David J. Fatiguing contractions increase protein S-glutathionylation occupancy in mouse skeletal muscle. United States. doi:10.1016/j.redox.2018.05.011.
Kramer, Philip A., Duan, Jicheng, Gaffrey, Matthew J., Shukla, Anil K., Wang, Lu, Bammler, Theo K., Qian, Wei -Jun, and Marcinek, David J. Wed . "Fatiguing contractions increase protein S-glutathionylation occupancy in mouse skeletal muscle". United States. doi:10.1016/j.redox.2018.05.011. https://www.osti.gov/servlets/purl/1439099.
@article{osti_1439099,
title = {Fatiguing contractions increase protein S-glutathionylation occupancy in mouse skeletal muscle},
author = {Kramer, Philip A. and Duan, Jicheng and Gaffrey, Matthew J. and Shukla, Anil K. and Wang, Lu and Bammler, Theo K. and Qian, Wei -Jun and Marcinek, David J.},
abstractNote = {Protein S-glutathionylation is an important reversible post-translational modification implicated in redox signaling. Oxidative modifications to protein thiols can alter the activity of metabolic enzymes, transcription factors, kinases, phosphatases, and the function of contractile proteins. However, the extent to which muscle contraction induces oxidative modifications in redox sensitive thiols is not known. The purpose of this study was to determine the targets of S-glutathionylation redox signaling following fatiguing contractions. Anesthetized adult male CB6F1 (BALB/cBy × C57BL/6) mice were subjected to acute fatiguing contractions for 15 min using in vivo stimulations. The right (stimulated) and left (unstimulated) gastrocnemius muscleswere collected 60 min after the last stimulation and processed for redox proteomics assay of S-glutathionylation.},
doi = {10.1016/j.redox.2018.05.011},
journal = {Redox Biology},
number = C,
volume = 17,
place = {United States},
year = {Wed May 23 00:00:00 EDT 2018},
month = {Wed May 23 00:00:00 EDT 2018}
}

Journal Article:
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