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

Journal Article · · Redox Biology
 [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)

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.

Research Organization:
Pacific Northwest National Laboratory (PNNL), Richland, WA (United States)
Sponsoring Organization:
USDOE
Grant/Contract Number:
AC05-76RL01830
OSTI ID:
1439099
Report Number(s):
PNNL-SA-135523; PII: S2213231718303550
Journal Information:
Redox Biology, Vol. 17, Issue C; ISSN 2213-2317
Publisher:
ElsevierCopyright Statement
Country of Publication:
United States
Language:
English
Citation Metrics:
Cited by: 53 works
Citation information provided by
Web of Science

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Figures / Tables (7)