Evidence map›Paper›PMID 25763823›Full record

ArticlePloS one2015

A mouse model of L-2-hydroxyglutaric aciduria, a disorder of metabolite repair.

Rim Rzem, Younes Achouri, Etienne Marbaix, Olivier Schakman, Elsa Wiame, Sandrine Marie, Philippe Gailly, Marie-Françoise Vincent, Maria Veiga-da-Cunha, Emile Van Schaftingen

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
4.7field-weighted citation impact, top 5% 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

40 citing papers in PubMed, 57 citations in OpenAlex.

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  5. Metabolic Plasticity in Embryogenesis Throughout the Lens of NADMethods in molecular biology (Clifton, N.J.) · 2026
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  8. LysineFrontiers in molecular neuroscience · 2025
    Review
  9. Article
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  11. Review
  12. Review
  13. Article
  14. Emerging cellular themes in leukodystrophies.Frontiers in cell and developmental biology · 2022
    Review
  15. Article
  16. Genes · 2021
    Article
  17. Article
  18. Article
  19. Article
  20. 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

10 authors at 3 institutions in 1 country.

Rim RzemWelbio and Laboratory of Physiological Chemistry, de Duve Institute, Université catholique de Louvain, Brussels, Belgium.
Younes AchouriWelbio and Laboratory of Physiological Chemistry, de Duve Institute, Université catholique de Louvain, Brussels, Belgium.
Etienne MarbaixCell Unit, de Duve Institute, Université catholique de Louvain, Brussels, Belgium.
Olivier SchakmanLaboratory of Cell Physiology, Institute of Neuroscience, Université catholique de Louvain, Brussels, Belgium.
Elsa WiameWelbio and Laboratory of Physiological Chemistry, de Duve Institute, Université catholique de Louvain, Brussels, Belgium.
Sandrine MarieLaboratory of Metabolic Diseases, Cliniques Universitaires Saint-Luc, Université catholique de Louvain, Brussels, Belgium.
Philippe GaillyLaboratory of Cell Physiology, Institute of Neuroscience, Université catholique de Louvain, Brussels, Belgium.
Marie-Françoise VincentLaboratory of Metabolic Diseases, Cliniques Universitaires Saint-Luc, Université catholique de Louvain, Brussels, Belgium.
Maria Veiga-da-CunhaWelbio and Laboratory of Physiological Chemistry, de Duve Institute, Université catholique de Louvain, Brussels, Belgium.
Emile Van SchaftingenWelbio and Laboratory of Physiological Chemistry, de Duve Institute, Université catholique de Louvain, Brussels, Belgium.
de Duve Institute · BECliniques Universitaires Saint-Luc · BEUCLouvain · BE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The purpose of the present work was to progress in our understanding of the pathophysiology of L-2-hydroxyglutaric aciduria, due to a defect in L-2-hydroxyglutarate dehydrogenase, by creating and studying a mouse model of this disease. L-2-hydroxyglutarate dehydrogenase-deficient mice (l2hgdh-/-) accumulated L-2-hydroxyglutarate in tissues, most particularly in brain and testis, where the concentration reached ≈ 3.5 μmol/g. Male mice showed a 30% higher excretion of L-2-hydroxyglutarate compared to female mice, supporting that this dicarboxylic acid is partially made in males by lactate dehydrogenase C, a poorly specific form of this enzyme exclusively expressed in testes. Involvement of mitochondrial malate dehydrogenase in the formation of L-2-hydroxyglutarate was supported by the commensurate decrease in the formation of this dicarboxylic acid when down-regulating this enzyme in mouse l2hgdh-/- embryonic fibroblasts. The concentration of lysine and arginine was markedly increased in the brain of l2hgdh-/- adult mice. Saccharopine was depleted and glutamine was decreased by ≈ 40%. Lysine-α-ketoglutarate reductase, which converts lysine to saccharopine, was inhibited by L-2-hydroxyglutarate with a Ki of ≈ 0.8 mM. As low but significant activities of the bifunctional enzyme lysine-α-ketoglutarate reductase/saccharopine dehydrogenase were found in brain, these findings suggest that the classical lysine degradation pathway also operates in brain and is inhibited by the high concentrations of L-2-hydroxyglutarate found in l2hgdh-/- mice. Pathological analysis of the brain showed significant spongiosis. The vacuolar lesions mostly affected oligodendrocytes and myelin sheats, as in other dicarboxylic acidurias, suggesting that the pathophysiology of this model of leukodystrophy may involve irreversible pumping of a dicarboxylate in oligodendrocytes. Neurobehavioral testing indicated that the mice mostly suffered from a deficit in learning capacity. In conclusion, the findings support the concept that L-2-hydroxyglutaric aciduria is a disorder of metabolite repair. The accumulation of L-2-hydroxyglutarate exerts toxic effects through various means including enzyme inhibition and glial cell swelling.

Indexed as

Disease Models, AnimalAlcohol OxidoreductasesAnimalsArginineBrainBrain Diseases, Metabolic, InbornCells, CulturedFemaleGlutaratesKetone OxidoreductasesLysineMaleMiceMice, KnockoutTestis2-oxoglutarate synthaseAlcohol Oxidoreductasesalpha-hydroxyglutarateArginineGlutaratesKetone OxidoreductasesL2HGDH protein, mouseLysine

Identifiers

PMID25763823
PMCPMC4357467
OpenAlexW1967447913

What OpenQuestion holds

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LicenceCC BY
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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.