Evidence map›Paper›PMID 27036938›Full record

ArticleThe Journal of biological chemistry2016

Monoacylglycerol Lipases Act as Evolutionarily Conserved Regulators of Non-oxidative Ethanol Metabolism.

Christoph Heier, Ulrike Taschler, Maja Radulovic, Philip Aschauer, Thomas O Eichmann, Susanne Grond, Heimo Wolinski, Monika Oberer, Rudolf Zechner, Sepp D Kohlwein and 1 more

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2016. 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
1.8field-weighted citation impact, top 15% 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, 15 citations in OpenAlex.

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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

11 authors at 1 institution in 1 country.

Christoph HeierFrom the Institute of Molecular Biosciences, University of Graz and christoph.heier@uni-graz.at.
Ulrike TaschlerFrom the Institute of Molecular Biosciences, University of Graz and.
Maja RadulovicFrom the Institute of Molecular Biosciences, University of Graz and.
Philip AschauerFrom the Institute of Molecular Biosciences, University of Graz and.
Thomas O EichmannFrom the Institute of Molecular Biosciences, University of Graz and.
Susanne GrondFrom the Institute of Molecular Biosciences, University of Graz and.
Heimo WolinskiFrom the Institute of Molecular Biosciences, University of Graz and BioTechMed-Graz, 8010 Graz, Austria.
Monika ObererFrom the Institute of Molecular Biosciences, University of Graz and.
Rudolf ZechnerFrom the Institute of Molecular Biosciences, University of Graz and.
Sepp D KohlweinFrom the Institute of Molecular Biosciences, University of Graz and BioTechMed-Graz, 8010 Graz, Austria.
Robert ZimmermannFrom the Institute of Molecular Biosciences, University of Graz and robert.zimmermann@uni-graz.at.
University of Graz · AT

Funding

Austrian Science Fund FWF P 21296Austrian Science Fund FWF P 24294
6 · The paper itself

Abstract

Fatty acid ethyl esters (FAEEs) are non-oxidative metabolites of ethanol that accumulate in human tissues upon ethanol intake. Although FAEEs are considered as toxic metabolites causing cellular dysfunction and tissue damage, the enzymology of FAEE metabolism remains poorly understood. In this study, we used a biochemical screen in Saccharomyces cerevisiae to identify and characterize putative hydrolases involved in FAEE catabolism. We found that Yju3p, the functional orthologue of mammalian monoacylglycerol lipase (MGL), contributes >90% of cellular FAEE hydrolase activity, and its loss leads to the accumulation of FAEE. Heterologous expression of mammalian MGL in yju3Δ mutants restored cellular FAEE hydrolase activity and FAEE catabolism. Moreover, overexpression or pharmacological inhibition of MGL in mouse AML-12 hepatocytes decreased or increased FAEE levels, respectively. FAEEs were transiently incorporated into lipid droplets (LDs) and both Yju3p and MGL co-localized with these organelles. We conclude that the storage of FAEE in inert LDs and their mobilization by LD-resident FAEE hydrolases facilitate a controlled metabolism of these potentially toxic lipid metabolites.

Indexed as

Biological EvolutionAnimalsCells, CulturedChromatography, Thin LayerEthanolFatty AcidsGas Chromatography-Mass SpectrometryHepatocytesHumansInactivation, MetabolicMiceMonoacylglycerol LipasesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsEthanolFatty AcidsMonoacylglycerol LipasesSaccharomyces cerevisiae ProteinsYju3 protein, S cerevisiaeethanol metabolismfatty acid metabolismlipid dropletlipid metabolismmonoacylglycerol lipaseSaccharomyces cerevisiaeserine esterase

Identifiers

PMID27036938
PMCPMC4882453
OpenAlexW2330639377

What Socratic 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 Socratic graph.