Evidence map›Paper›PMID 23888047›Full record

ArticleThe Journal of biological chemistry2013

A role for glutathione transferase Omega 1 (GSTO1-1) in the glutathionylation cycle.

Deepthi Menon, Philip G Board

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 66 papers, 3 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
66citing papers in PubMed, 3 pooled it
4.9field-weighted citation impact, top 4% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

66 citing papers in PubMed, 3 syntheses or guidelines pooled it, 139 citations in OpenAlex.

  1. Pooled it
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  11. Review
  12. Glutathione-Dependent Pathways in Cancer Cells.International journal of molecular sciences · 2024
    Review
  13. Article
  14. Article
  15. Regulation of GlutathioneInternational journal of molecular sciences · 2024
    Article
  16. Article
  17. Article
  18. Article
  19. Chemistry and biology of enzymes in protein glutathionylation.Current opinion in chemical biology · 2023
    Review
  20. Review

6 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors at 1 institution in 1 country.

Deepthi MenonFrom the Department of Molecular Bioscience, John Curtin School of Medical Research, Australian National University, Canberra ACT-2600, Australia.
Philip G BoardFrom the Department of Molecular Bioscience, John Curtin School of Medical Research, Australian National University, Canberra ACT-2600, Australia. Electronic address: Philip.Board@anu.edu.au.
Australian National University · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The glutathionylation of intracellular protein thiols can protect against irreversible oxidation and can act as a redox switch regulating metabolic pathways. In this study we discovered that the Omega class glutathione transferase GSTO1-1 plays a significant role in the glutathionylation cycle. The catalytic activity of GSTO1-1 was determined in vitro by assaying the deglutathionylation of a synthetic peptide by tryptophan fluorescence quenching and in T47-D epithelial breast cancer cells by both immunoblotting and the direct determination of total glutathionylation. Mutating the active site cysteine residue (Cys-32) ablated the deglutathionylating activity of GSTO1-1. Furthermore, we demonstrate that the expression of GSTO1-1 in T47-D cells that are devoid of endogenous GSTO1-1 resulted in a 50% reduction in total glutathionylation levels. Mass spectrometry and immunoprecipitation identified β-actin as a protein that is specifically deglutathionylated by GSTO1-1 in T47-D cells. In contrast to the deglutathionylation activity, we also found that GSTO1-1 is associated with the rapid glutathionylation of cellular proteins when the cells are exposed to S-nitrosoglutathione. The common A140D genetic polymorphism in GSTO1 was found to have significant effects on the kinetics of both the deglutathionylation and glutathionylation reactions. Genetic variation in GSTO1-1 has been associated with a range of diseases, and the discovery that a frequent GSTO1-1 polymorphism affects glutathionylation cycle reactions reveals a common mechanism where it can act on multiple proteins and pathways.

Indexed as

ActinsAmino Acid SubstitutionCatalytic DomainCell Line, TumorGlutathioneGlutathione TransferaseHumansMutation, MissensePolymorphism, GeneticProtein Processing, Post-TranslationalActinsGlutathioneGlutathione TransferaseGSTO1 protein, humanEnzyme CatalysisGenetic PolymorphismGlutathione Transferase OmegaGlutathionylationRedox RegulationThiol

Identifiers

PMID23888047
PMCPMC3764784
OpenAlexW2128989053

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.