Evidence map›Paper›PMID 30420639›Full record

ArticleNature communications2018

Human adipose glycerol flux is regulated by a pH gate in AQP10.

Kamil Gotfryd, Andreia Filipa Mósca, Julie Winkel Missel, Sigurd Friis Truelsen, Kaituo Wang, Mariana Spulber, Simon Krabbe, Claus Hélix-Nielsen, Umberto Laforenza, Graça Soveral and 2 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 67 papers.

0numbers the graph read from it
0cells of the map it votes in
67citing papers in PubMed
4.6field-weighted citation impact, top 4% 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

67 citing papers in PubMed, 127 citations in OpenAlex.

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  18. Molecular basis for human aquaporin inhibition.Proceedings of the National Academy of Sciences of the United States of America · 2024
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7 more citing papers are in PubMed but not listed here.

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

12 authors at 4 institutions in 4 countries.

Kamil GotfrydUniversity of Copenhagen, Department of Biomedical Sciences, Nørre Allé 14, DK-2200, Copenhagen N, Denmark.ORCID http://orcid.org/0000-0002-0299-0779
Andreia Filipa MóscaUniversidade de Lisboa, Research Institute for Medicines (iMed.ULisboa), Faculty of Pharmacy, Av. Prof. Gama Pinto, 1649-003, Lisbon, Portugal.
Julie Winkel MisselUniversity of Copenhagen, Department of Biomedical Sciences, Nørre Allé 14, DK-2200, Copenhagen N, Denmark.
Sigurd Friis TruelsenTechnical University of Denmark, Department of Environmental Engineering, Bygningstorvet Building 115, DK-2800 Kgs, Lyngby, Denmark.ORCID http://orcid.org/0000-0003-2410-5184
Kaituo WangUniversity of Copenhagen, Department of Biomedical Sciences, Nørre Allé 14, DK-2200, Copenhagen N, Denmark.ORCID http://orcid.org/0000-0002-5922-7109
Mariana SpulberAquaporin A/S, Nymøllevej 78, DK-2800, Lyngby, Denmark.
Simon KrabbeUniversity of Copenhagen, Department of Biology, Universitetsparken 13, DK-2100, Copenhagen OE, Denmark.ORCID http://orcid.org/0000-0001-7204-6989
Claus Hélix-NielsenTechnical University of Denmark, Department of Environmental Engineering, Bygningstorvet Building 115, DK-2800 Kgs, Lyngby, Denmark.
Umberto LaforenzaUniversity of Pavia, Department of Molecular Medicine, Human Physiology Unit, Via Forlanini 6, I-27100, Pavia, Italy.ORCID http://orcid.org/0000-0003-2951-5983
Graça SoveralUniversidade de Lisboa, Research Institute for Medicines (iMed.ULisboa), Faculty of Pharmacy, Av. Prof. Gama Pinto, 1649-003, Lisbon, Portugal.ORCID http://orcid.org/0000-0001-8487-110X
Per Amstrup PedersenUniversity of Copenhagen, Department of Biology, Universitetsparken 13, DK-2100, Copenhagen OE, Denmark. papedersen@bio.ku.dk.ORCID http://orcid.org/0000-0001-8648-9748
Pontus GourdonUniversity of Copenhagen, Department of Biomedical Sciences, Nørre Allé 14, DK-2200, Copenhagen N, Denmark. pontus@sund.ku.dk.ORCID http://orcid.org/0000-0002-8631-3539
University of Copenhagen · DKTechnical University of Denmark · DKUniversity of Lisbon · PTUniversity of Pavia · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Obesity is a major threat to global health and metabolically associated with glycerol homeostasis. Here we demonstrate that in human adipocytes, the decreased pH observed during lipolysis (fat burning) correlates with increased glycerol release and stimulation of aquaglyceroporin AQP10. The crystal structure of human AQP10 determined at 2.3 Å resolution unveils the molecular basis for pH modulation-an exceptionally wide selectivity (ar/R) filter and a unique cytoplasmic gate. Structural and functional (in vitro and in vivo) analyses disclose a glycerol-specific pH-dependence and pinpoint pore-lining His80 as the pH-sensor. Molecular dynamics simulations indicate how gate opening is achieved. These findings unravel a unique type of aquaporin regulation important for controlling body fat mass. Thus, targeting the cytoplasmic gate to induce constitutive glycerol secretion may offer an attractive option for treating obesity and related complications.

Indexed as

AdipocytesAdipose TissueAgedAquaporinsFemaleGlycerolHumansHydrogen-Ion ConcentrationIon Channel GatingMaleMiddle AgedMolecular Dynamics SimulationPrincipal Component AnalysisAQP10 protein, humanAquaporinsGlycerol

Identifiers

PMID30420639
PMCPMC6232157
OpenAlexW2899545382

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.