Evidence map›Paper›PMID 26206726›Full record

ArticleAmino acids2015

Intrinsic carnosine metabolism in the human kidney.

Verena Peters, Celine Q F Klessens, Hans J Baelde, Benjamin Singler, Kimberley A M Veraar, Ana Zutinic, Jakub Drozak, Johannes Zschocke, Claus P Schmitt, Emile de Heer

Open access · hybridAbstract read
In one paragraph

Article in Amino acids, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed, 1 pooled it
3.4field-weighted citation impact, top 8% 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

31 citing papers in PubMed, 1 synthesis or guideline pooled it, 68 citations in OpenAlex.

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  15. The Role of GSH in Intracellular Iron Trafficking.International journal of molecular sciences · 2021
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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

10 authors at 3 institutions in 3 countries.

Verena PetersUniversity Children's Hospital, University of Heidelberg, Im Neuenheimer Feld 672, 69120, Heidelberg, Germany.
Celine Q F KlessensDepartment of Pathology, Leiden University Medical Center, Albinusdreef 2, 2333 ZA, Leiden, The Netherlands. c.q.f.klessens@lumc.nl.
Hans J BaeldeDepartment of Pathology, Leiden University Medical Center, Albinusdreef 2, 2333 ZA, Leiden, The Netherlands.
Benjamin SinglerUniversity Children's Hospital, University of Heidelberg, Im Neuenheimer Feld 672, 69120, Heidelberg, Germany.
Kimberley A M VeraarDepartment of Pathology, Leiden University Medical Center, Albinusdreef 2, 2333 ZA, Leiden, The Netherlands.
Ana ZutinicDepartment of Pathology, Leiden University Medical Center, Albinusdreef 2, 2333 ZA, Leiden, The Netherlands.
Jakub DrozakDepartment of Metabolic Regulation, Faculty of Biology, University of Warsaw, Krakowskie Przedmieście 26/28, 00-927, Warsaw, Poland.
Johannes ZschockeDepartment of Human Genetics, Medical University of Innsbruck, Innrain 52, Christoph-Probst-Platz, 6020, Innsbruck, Austria.
Claus P SchmittUniversity Children's Hospital, University of Heidelberg, Im Neuenheimer Feld 672, 69120, Heidelberg, Germany.
Emile de HeerDepartment of Pathology, Leiden University Medical Center, Albinusdreef 2, 2333 ZA, Leiden, The Netherlands.
Leiden University Medical Center · NLInnsbruck Medical University · ATUniversity of Warsaw · PL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Histidine-containing dipeptides like carnosine and anserine have protective functions in both health and disease. Animal studies suggest that carnosine can be metabolized within the kidney. The goal of this study was to obtain evidence of carnosine metabolism in the human kidney and to provide insight with regards to diabetic nephropathy. Expression, distribution, and localization of carnosinase-1 (CNDP1), carnosine synthase (CARNS), and taurine transporters (TauT) were measured in human kidneys. CNDP1 and CARNS activities were measured in vitro. CNDP1 and CARNS were located primarily in distal and proximal tubules, respectively. Specifically, CNDP1 levels were high in tubular cells and podocytes (20.3 ± 3.4 and 15 ± 3.2 ng/mg, respectively) and considerably lower in endothelial cells (0.5 ± 0.1 ng/mg). CNDP1 expression was correlated with the degradation of carnosine and anserine (r = 0.88 and 0.81, respectively). Anserine and carnosine were also detectable by HPLC in the renal cortex. Finally, TauT mRNA and protein were found in all renal epithelial cells. In diabetic patients, CNDP1 seemed to be reallocated to proximal tubules. We report compelling evidence that the kidney has an intrinsic capacity to metabolize carnosine. Both CNDP1 and CARNS are expressed in glomeruli and tubular cells. Carnosine-synthesizing and carnosine-hydrolyzing enzymes are localized in distinct compartments in the nephron and increased CNDP1 levels suggest a higher CNDP1 activity in diabetic kidneys.

Indexed as

Gene Expression RegulationAnserineCarnosineChromatography, High Pressure LiquidDiabetic NeuropathiesDipeptidasesEndothelial CellsEpithelial CellsGene Expression ProfilingHumansHydrolysisImmunohistochemistryKidneyKidney TubulesMembrane GlycoproteinsMembrane Transport ProteinsAnserineCarnosinecarnosine synthetaseCNDP1 protein, humanDipeptidasesMembrane GlycoproteinsMembrane Transport ProteinsPeptide SynthasesRNA, MessengerTaurine TransportersAnserineCarnosinase (CNDP1)CarnosineDiabetic nephropathyMetabolism

Identifiers

PMID26206726
PMCPMC4633449
OpenAlexW1041726898

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.