Evidence map›Paper›PMID 40332189›Full record

ArticleInternational journal of molecular sciences2025

Enzymes Drive Glutathione Shunt to Explain Oxidative State Using an In-Parallel Multi-Omic Method.

Valerie C Wasinger, Sonia Bustamante, Nashwa Najib, Ashish Diwan, Tharusha Jayasena, Nahian S Chowdhury, Julia Beretov, Siobhan Schabrun

Abstract read
In one paragraph

Article in International journal of molecular sciences, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
–field-weighted citation impact
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

3 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
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

8 authors.

Valerie C WasingerBioanalytical Mass Spectrometry Facility, Mark Wainwright Analytical Centre, University of New South Wales, Sydney, NSW 2052, Australia.ORCID 0000-0001-5338-0869
Sonia BustamanteBioanalytical Mass Spectrometry Facility, Mark Wainwright Analytical Centre, University of New South Wales, Sydney, NSW 2052, Australia.
Nashwa NajibDepartment of Orthopaedic Surgery, St. George and Sutherland Clinical Campuses, School of Clinical Medicine, University of New South Wales, Sydney, NSW 2052, Australia.
Ashish DiwanDepartment of Orthopaedic Surgery, St. George and Sutherland Clinical Campuses, School of Clinical Medicine, University of New South Wales, Sydney, NSW 2052, Australia.ORCID 0000-0003-1037-8421
Tharusha JayasenaCentre for Healthy Brain Ageing (CHeBA), Discipline of Psychiatry & Mental Health, School of Clinical Medicine, Faculty of Health & Medicine, University of New South Wales, Sydney, NSW 2052, Australia.
Nahian S ChowdhuryCenter for Pain IMPACT, Neuroscience Research Australia, Sydney, NSW 2031, Australia.ORCID 0009-0003-1132-2072
Julia BeretovSt. George and Sutherland Clinical Campuses, School of Clinical Medicine, University of New South Wales, Sydney, NSW 2052, Australia.ORCID 0000-0001-5582-0020
Siobhan SchabrunGray Centre for Mobility & Activity, Parkwood Institute, St. Joseph's Healthcare, London, ON N6C 0A7, Canada.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The glutathione shunt is one of the most important contributors to the cellular redox state, with implications across cancer, chronic diseases, diseases of ageing, and autoimmune diseases, including inflammatory bowel disease (IBD). Traditionally, the redox state is gauged by the ratio of the surrogate metabolites GSH and GSSG. However, this presents methodological challenges and offers a constrained illustration of metabolites without a systems-level understanding of redox dynamics, failing to elucidate variations across an entire biochemical network. Targeted proteomics can fill this void. Here, we describe an in-parallel metabolomic and proteomic targeted method to encompass measurements directly related to the shunt. Samples are simultaneously prepared to extract the substrate building blocks, cysteine, cystine, methionine, glutamic acid, and kynurenine; and the proteins, SLC7A11 (xCT), Glutamate Cysteine Ligase (GSH1), Glutathione Synthetase (GSH2), Glutathione Peroxidase (GPx), and Glutathione Reductase (GSHR) for targeted mass spectrometry. We demonstrate the method by targeted analysis of proteins in plasma, serum, nasal swab, and saliva and apply the multi-omic method to assess changes in the glutathione shunt in the serum of patients diagnosed with IBD. This allows for a broader narrative to establish context at which the glutathione shunt is operating.

Indexed as

GlutathioneMetabolomicsProteomicsAmino Acid Transport System y+Glutamate-Cysteine LigaseGlutathione PeroxidaseGlutathione ReductaseGlutathione SynthaseHumansInflammatory Bowel DiseasesMultiomicsOxidation-ReductionOxidative StressAmino Acid Transport System y+Glutamate-Cysteine LigaseGlutathioneGlutathione PeroxidaseGlutathione ReductaseGlutathione SynthaseSLC7A11 protein, humanbiomarkerglutathione shuntGPxGSHGSSGIBDliquid biopsySLCA7A1

Identifiers

PMID40332189
PMCPMC12026767

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Registered trials

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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.