Evidence map›Paper›PMID 32948897›Full record

ArticleEuropean journal of applied physiology2020

The role of alanine glyoxylate transaminase-2 (agxt2) in β-alanine and carnosine metabolism of healthy mice and humans.

Jan Stautemas, Natalia Jarzebska, Zhou Xiang Shan, Laura Blancquaert, Inge Everaert, Sarah de Jager, Siegrid De Baere, Arne Hautekiet, Anneke Volkaert, Filip B D Lefevere and 8 more

Abstract read
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In one paragraph

Article in European journal of applied physiology, 2020. 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
0.2field-weighted citation impact, top 44% 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

3 citing papers in PubMed, 5 citations in OpenAlex.

  1. Article
  2. Physiological Roles of Carnosine in Myocardial Function and Health.Advances in nutrition (Bethesda, Md.) · 2022
    Review
  3. 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

18 authors at 8 institutions in 4 countries.

Jan StautemasDepartment of Movement and Sports Sciences, Ghent University, Watersportlaan 2, 9000, Gent, Belgium. jan.stautemas@ugent.be.ORCID http://orcid.org/0000-0001-7473-9340
Natalia JarzebskaUniversity Centre for Vascular Medicine and Department of Internal Medicine, Technische Universität Dresden, Dresden, Germany.
Zhou Xiang ShanAnhui Institute of Sport Science and Technology, Anhui University of Science and Technology Anhui, Anhui, China.
Laura BlancquaertDepartment of Movement and Sports Sciences, Ghent University, Watersportlaan 2, 9000, Gent, Belgium.ORCID http://orcid.org/0000-0001-6996-1393
Inge EveraertDepartment of Movement and Sports Sciences, Ghent University, Watersportlaan 2, 9000, Gent, Belgium.ORCID http://orcid.org/0000-0002-1800-4355
Sarah de JagerDepartment of Movement and Sports Sciences, Ghent University, Watersportlaan 2, 9000, Gent, Belgium.
Siegrid De BaereDepartment of Pharmacology, Toxicology and Biochemistry, Ghent University, Ghent, Belgium.ORCID http://orcid.org/0000-0002-1382-5699
Arne HautekietDepartment of Physical Medicine and Rehabilitation, Ghent University Hospital, Ghent, Belgium.
Anneke VolkaertDepartment of Movement and Sports Sciences, Ghent University, Watersportlaan 2, 9000, Gent, Belgium.
Filip B D LefevereDepartment of Movement and Sports Sciences, Ghent University, Watersportlaan 2, 9000, Gent, Belgium.
Jens Martens-LobenhofferInstitute of Clinical Pharmacology, Otto-Von-Guericke University, Magdeburg, Germany.ORCID http://orcid.org/0000-0002-3829-7992
Stefanie M Bode-BögerInstitute of Clinical Pharmacology, Otto-Von-Guericke University, Magdeburg, Germany.ORCID http://orcid.org/0000-0002-5132-6591
Chang Keun KimExercise and Metabolism Research Center, Zhejiang Normal University, Jinhua, China.
James LeiperMRC London Institute of Medical Sciences, Hammersmith Hospital Campus, London, UK.ORCID http://orcid.org/0000-0003-4656-519X
Norbert WeissUniversity Centre for Vascular Medicine and Department of Internal Medicine, Technische Universität Dresden, Dresden, Germany.ORCID http://orcid.org/0000-0001-9013-0017
Siska CroubelsDepartment of Pharmacology, Toxicology and Biochemistry, Ghent University, Ghent, Belgium.ORCID http://orcid.org/0000-0001-6357-3517
Roman N RodionovUniversity Centre for Vascular Medicine and Department of Internal Medicine, Technische Universität Dresden, Dresden, Germany.ORCID http://orcid.org/0000-0003-0935-0763
Wim DeraveDepartment of Movement and Sports Sciences, Ghent University, Watersportlaan 2, 9000, Gent, Belgium.ORCID http://orcid.org/0000-0002-2225-5587
Ghent University · BEOtto-von-Guericke-Universität Magdeburg · DETechnische Universität Dresden · DEAnhui University of Science and Technology · CNGhent University Hospital · BEHammersmith Hospital · GBUniversity Hospital Carl Gustav Carus · DEZhejiang Normal University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

purposeChronic β-alanine supplementation leads to increased levels of muscle histidine-containing dipeptides. However, the majority of ingested β-alanine is, most likely, degraded by two transaminases: GABA-T and AGXT2. In contrast to GABA-T, the in vivo role of AGXT2 with respect to β-alanine metabolism is unknown. The purpose of the present work is to investigate if AGXT2 is functionally involved in β-alanine homeostasis.

methodsMuscle histidine-containing dipeptides levels were determined in AGXT2 overexpressing or knock-out mice and in human subjects with different rs37369 genotypes which is known to affect AGXT2 activity. Further, plasma β-alanine kinetic was measured and urine was obtained from subjects with different rs37369 genotypes following ingestion of 1400 mg β-alanine.

resultOverexpression of AGXT2 decreased circulating and muscle histidine-containing dipeptides (> 70% decrease; p < 0.05), while AGXT2 KO did not result in altered histidine-containing dipeptides levels. In both models, β-alanine remained unaffected in the circulation and in muscle (p > 0.05). In humans, the results support the evidence that decreased AGXT2 activity is not associated with altered histidine-containing dipeptides levels (p > 0.05). Additionally, following an acute dose of β-alanine, no differences in pharmacokinetic response were measured between subjects with different rs37369 genotypes (p > 0.05). Interestingly, urinary β-alanine excretion was 103% higher in subjects associated with lower AGXT2 activity, compared to subjects associated with normal AGXT2 activity (p < 0.05).

conclusionThe data suggest that in vivo, β-alanine is a substrate of AGXT2; however, its importance in the metabolism of β-alanine and histidine-containing dipeptides seems small.

Indexed as

AdultAnimalsbeta-AlanineCarnosineDipeptidesGenotypeHistidineHumansMaleMiceMice, Inbred C57BLMice, KnockoutMusclesTransaminasesYoung AdultAlanine-glyoxylate transaminasebeta-AlanineCarnosineDipeptidesHistidineTransaminasesAnserineBeta-alanineCarnosiners37369

Identifiers

PMID32948897
OpenAlexW3087182178

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.