Proteome-wide identification and quantification of S-glutathionylation targets in mouse liver

David J. McGarry (Lead / Corresponding author), Wenzhang Chen, Probir Chakravarty, Douglas L. Lamont, C. Roland Wolf, Colin J. Henderson

    Research output: Contribution to journalArticle

    17 Citations (Scopus)

    Abstract

    Protein S-glutathionylation is a reversible post-translational modification regulating sulfhydryl homeostasis. However, little is known about the proteins and pathways regulated by S-glutathionylation in whole organisms and current approaches lack the sensitivity to examine this modification under basal conditions. We now report the quantification and identification of S-glutathionylated proteins from animal tissue, using a highly sensitive methodology combining high-accuracy proteomics with tandem mass tagging to provide precise, extensive coverage of S-glutathionylated targets in mouse liver. Critically, we show significant enrichment of S-glutathionylated mitochondrial and Krebs cycle proteins, identifying that S-glutathionylation is heavily involved in energy metabolism processes in vivo. Furthermore, using mice nulled for glutathione S-transferase Pi (GSTP) we address the potential for S-glutathionylation to be mediated enzymatically. The data demonstrate the impact of S-glutathionylation in cellular homeostasis, particularly in relation to energy regulation and is of significant interest for those wishing to examine S-glutathionylation in an animal model.

    Original languageEnglish
    Pages (from-to)25-32
    Number of pages8
    JournalBiochemical Journal
    Volume469
    Issue number1
    Early online date20 Apr 2015
    DOIs
    Publication statusPublished - Jun 2015

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    Protein S
    Proteome
    Liver
    Animals
    Glutathione S-Transferase pi
    Homeostasis
    Proteins
    Citric Acid Cycle
    Post Translational Protein Processing
    Tissue
    Proteomics
    Energy Metabolism
    Animal Models

    Cite this

    McGarry, David J. ; Chen, Wenzhang ; Chakravarty, Probir ; Lamont, Douglas L. ; Wolf, C. Roland ; Henderson, Colin J. / Proteome-wide identification and quantification of S-glutathionylation targets in mouse liver. In: Biochemical Journal. 2015 ; Vol. 469, No. 1. pp. 25-32.
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    abstract = "Protein S-glutathionylation is a reversible post-translational modification regulating sulfhydryl homeostasis. However, little is known about the proteins and pathways regulated by S-glutathionylation in whole organisms and current approaches lack the sensitivity to examine this modification under basal conditions. We now report the quantification and identification of S-glutathionylated proteins from animal tissue, using a highly sensitive methodology combining high-accuracy proteomics with tandem mass tagging to provide precise, extensive coverage of S-glutathionylated targets in mouse liver. Critically, we show significant enrichment of S-glutathionylated mitochondrial and Krebs cycle proteins, identifying that S-glutathionylation is heavily involved in energy metabolism processes in vivo. Furthermore, using mice nulled for glutathione S-transferase Pi (GSTP) we address the potential for S-glutathionylation to be mediated enzymatically. The data demonstrate the impact of S-glutathionylation in cellular homeostasis, particularly in relation to energy regulation and is of significant interest for those wishing to examine S-glutathionylation in an animal model.",
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    Proteome-wide identification and quantification of S-glutathionylation targets in mouse liver. / McGarry, David J. (Lead / Corresponding author); Chen, Wenzhang; Chakravarty, Probir; Lamont, Douglas L.; Wolf, C. Roland; Henderson, Colin J.

    In: Biochemical Journal, Vol. 469, No. 1, 06.2015, p. 25-32.

    Research output: Contribution to journalArticle

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    AB - Protein S-glutathionylation is a reversible post-translational modification regulating sulfhydryl homeostasis. However, little is known about the proteins and pathways regulated by S-glutathionylation in whole organisms and current approaches lack the sensitivity to examine this modification under basal conditions. We now report the quantification and identification of S-glutathionylated proteins from animal tissue, using a highly sensitive methodology combining high-accuracy proteomics with tandem mass tagging to provide precise, extensive coverage of S-glutathionylated targets in mouse liver. Critically, we show significant enrichment of S-glutathionylated mitochondrial and Krebs cycle proteins, identifying that S-glutathionylation is heavily involved in energy metabolism processes in vivo. Furthermore, using mice nulled for glutathione S-transferase Pi (GSTP) we address the potential for S-glutathionylation to be mediated enzymatically. The data demonstrate the impact of S-glutathionylation in cellular homeostasis, particularly in relation to energy regulation and is of significant interest for those wishing to examine S-glutathionylation in an animal model.

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