Evidence map›Paper›PMID 22170048›Full record

ArticleThe Journal of biological chemistry2012

Glutathione degradation is a key determinant of glutathione homeostasis.

Peggy Baudouin-Cornu, Gilles Lagniel, Chitranshu Kumar, Meng-Er Huang, Jean Labarre

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
2.4field-weighted citation impact, top 13% 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

37 citing papers in PubMed, 72 citations in OpenAlex.

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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

5 authors at 4 institutions in 1 country.

Peggy Baudouin-CornuCommissariat à I'Energie Atomique (CEA), Institut de Biologie et Technologies de Saclay (iBiTecS), Service de Biologie Integrative et Genetique Moleculaire (SBIGeM), 91191 Gif-sur-Yvette, France.
Gilles Lagniel
Chitranshu Kumar
Meng-Er Huang
Jean Labarre
Institut de Biologie et Technologies · FRCommissariat à l'Énergie Atomique et aux Énergies Alternatives · FRInstitut Curie · FRUniversité Paris-Sud · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Glutathione (GSH) has several important functions in eukaryotic cells, and its intracellular concentration is tightly controlled. Combining mathematical models and (35)S labeling, we analyzed Saccharomyces cerevisiae sulfur metabolism. This led us to the observation that GSH recycling is markedly faster than previously estimated. We set up additional in vivo assays and concluded that under standard conditions, GSH half-life is around 90 min. Sulfur starvation and growth with GSH as the sole sulfur source strongly increase GSH degradation, whereas cadmium (Cd(2+)) treatment inhibits GSH degradation. Whatever the condition tested, GSH is degraded by the cytosolic Dug complex (composed of the three subunits Dug1, Dug2, and Dug3) but not by the γ-glutamyl-transpeptidase, raising the question of the role of this enzyme. In vivo, both DUG2/3 mRNA levels and Dug activity are quickly induced by sulfur deprivation in a Met4-dependent manner. This suggests that Dug activity is mainly regulated at the transcriptional level. Finally, analysis of dug2Δ and dug3Δ mutant cells shows that GSH degradation activity strongly impacts on GSH intracellular concentration and that GSH intracellular concentration does not affect GSH synthesis rate. Altogether, our data led us to reconsider important aspects of GSH metabolism, challenging notions on GSH synthesis and GSH degradation that were considered as established.

Indexed as

Basic-Leucine Zipper Transcription FactorsCadmiumCarbon-Nitrogen LigasesDipeptidasesGene DeletionGlutathioneHalf-LifeHomeostasisMultienzyme ComplexesPeptide HydrolasesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSulfurBasic-Leucine Zipper Transcription FactorsCadmiumCarbon-Nitrogen LigasesDipeptidasesDUG1 protein, S cerevisiaeDUG2 protein, S cerevisiaeDUG3 protein, S cerevisiaeGlutathioneMET4 protein, S cerevisiaeMultienzyme ComplexesPeptide HydrolasesSaccharomyces cerevisiae ProteinsSulfur

Identifiers

PMID22170048
PMCPMC3281641
OpenAlexW2074946486

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.