Evidence map›Paper›PMID 33022862›Full record

ArticleActa physiologica (Oxford, England)2021

Protein O-GlcNAcylation levels are regulated independently of dietary intake in a tissue and time-specific manner during rat postnatal development.

Thomas Dupas, Manon Denis, Justine Dontaine, Antoine Persello, Laurent Bultot, Angélique Erraud, Didier Vertommen, Bertrand Bouchard, Arnaud Tessier, Matthieu Rivière and 12 more

Open access · hybridAbstract read
In one paragraph

Article in Acta physiologica (Oxford, England), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
0.8field-weighted citation impact, top 28% 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

11 citing papers in PubMed, 14 citations in OpenAlex.

  1. Article
  2. Article
  3. O-GlcNAcylation in ischemic diseases.Frontiers in pharmacology · 2024
    Review
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  5. Review
  6. Article
  7. Article
  8. Article
  9. Review
  10. AnInternational journal of molecular sciences · 2021
    Article
  11. Article
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

22 authors at 8 institutions in 4 countries.

Thomas DupasUniversité de Nantes, CHU Nantes, CNRS, INSERM, l'institut du thorax, Nantes, France.
Manon DenisUniversité de Nantes, CHU Nantes, CNRS, INSERM, l'institut du thorax, Nantes, France.
Justine DontaineUniversité catholique de Louvain, Institut de Recherche Expérimentale et Clinique, Pole of Cardiovascular Research, Brussels, Belgium.
Antoine PerselloUniversité de Nantes, CHU Nantes, CNRS, INSERM, l'institut du thorax, Nantes, France.
Laurent BultotUniversité catholique de Louvain, Institut de Recherche Expérimentale et Clinique, Pole of Cardiovascular Research, Brussels, Belgium.
Angélique ErraudUniversité de Nantes, CHU Nantes, CNRS, INSERM, l'institut du thorax, Nantes, France.
Didier VertommenUniversité catholique de Louvain, de Duve Institute, Mass Spectrometry Platform, Brussels, Belgium.
Bertrand BouchardMontreal Heart Institute Research Center and Department of Nutrition, Université de Montréal, Montreal, Québec, Canada.
Arnaud TessierFaculté des Sciences et des Techniques, Université de Nantes, CNRS, Chimie et Interdisciplinarité: Synthèse, Analyse, Modélisation (CEISAM), UMR CNRS 6230, Nantes, France.
Matthieu RivièreFaculté des Sciences et des Techniques, Université de Nantes, CNRS, Chimie et Interdisciplinarité: Synthèse, Analyse, Modélisation (CEISAM), UMR CNRS 6230, Nantes, France.
Jacques LebretonFaculté des Sciences et des Techniques, Université de Nantes, CNRS, Chimie et Interdisciplinarité: Synthèse, Analyse, Modélisation (CEISAM), UMR CNRS 6230, Nantes, France.
Edith Bigot-CorbelDepartement of Biochemistry, CHU de Nantes, Nantes, France.
Jérôme MontnachUniversité de Nantes, CHU Nantes, CNRS, INSERM, l'institut du thorax, Nantes, France.
Michel De WaardUniversité de Nantes, CHU Nantes, CNRS, INSERM, l'institut du thorax, Nantes, France.
Chantal GauthierUniversité de Nantes, CHU Nantes, CNRS, INSERM, l'institut du thorax, Nantes, France.
Yan BurelleInterdisciplinary School of Health Sciences, Faculty of Health Sciences and Department of Cellular and Molecular Medicine, Faculty of Medicine, University of Ottawa, Ottawa, ON, Canada.
Aaron K OlsonDivision of Cardiology, Department of Pediatrics, University of Washington, Seattle, WA, 98105, USA.
Bertrand RozecUniversité de Nantes, CHU Nantes, CNRS, INSERM, l'institut du thorax, Nantes, France.
Christine Des RosiersMontreal Heart Institute Research Center and Department of Nutrition, Université de Montréal, Montreal, Québec, Canada.
Luc BertrandUniversité catholique de Louvain, Institut de Recherche Expérimentale et Clinique, Pole of Cardiovascular Research, Brussels, Belgium.
Tarik IssadUniversité de Paris, INSERM U1016, CNRS UMR 8104, Paris, France.
Benjamin LauzierUniversité de Nantes, CHU Nantes, CNRS, INSERM, l'institut du thorax, Nantes, France.ORCID 0000-0002-1370-6155
Centre National de la Recherche Scientifique · FRMontreal Heart Institute · CAUCLouvain · BECentre Hospitalier Universitaire de Nantes · FRde Duve Institute · BEUniversity of Ottawa · CAUniversity of Washington · USWalloon Excellence in Lifesciences and Biotechnology · BE

Funding

Metabolic regulation of O-GlcNAc and cardiac function during hypertrophyR01HL122546 · NHLBI · SEATTLE CHILDREN'S HOSPITAL · PI OLSON, AARON K · 2015 to 2019
$2.7M
National Heart, Lung, and Blood Institute: NIHR01HL122546NHLBI NIH HHS R01 HL122546
6 · The paper itself

Abstract

aimMetabolic sources switch from carbohydrates in utero, to fatty acids after birth and then a mix once adults. O-GlcNAcylation (O-GlcNAc) is a post-translational modification considered as a nutrient sensor. The purpose of this work was to assess changes in protein O-GlcNAc levels, regulatory enzymes and metabolites during the first periods of life and decipher the impact of O-GlcNAcylation on cardiac proteins.

methodsHeart, brain and liver were harvested from rats before and after birth (D-1 and D0), in suckling animals (D12), after weaning with a standard (D28) or a low-carbohydrate diet (D28F), and adults (D84). O-GlcNAc levels and regulatory enzymes were evaluated by western blots. Mass spectrometry (MS) approaches were performed to quantify levels of metabolites regulating O-GlcNAc and identify putative cardiac O-GlcNAcylated proteins.

resultsProtein O-GlcNAc levels decrease drastically and progressively from D-1 to D84 (13-fold, P < .05) in the heart, whereas the changes were opposite in liver and brain. O-GlcNAc levels were unaffected by weaning diet in any tissues. Changes in expression of enzymes and levels of metabolites regulating O-GlcNAc were tissue-dependent. MS analyses identified changes in putative cardiac O-GlcNAcylated proteins, namely those involved in the stress response and energy metabolism, such as ACAT1, which is only O-GlcNAcylated at D0.

conclusionOur results demonstrate that protein O-GlcNAc levels are not linked to dietary intake and regulated in a time and tissue-specific manner during postnatal development. We have identified by untargeted MS putative proteins with a particular O-GlcNAc signature across the development process suggesting specific role of these proteins.

Indexed as

AcetylglucosamineProtein Processing, Post-TranslationalAnimalsEatingMass SpectrometryRatsAcetylglucosaminedevelopmenthexosamine biosynthesis pathwaymass spectrometrymetabolismO-GlcNAcylationO-GlcNAcylomic

Identifiers

PMID33022862
PMCPMC7988603
OpenAlexW3092426092

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.