Evidence map›Paper›PMID 37544001›Full record

ArticleBulletin of mathematical biology2023

The Potential Roles of Transacylation in Intracellular Lipolysis and Related Qssa Approximations.

Ján Eliaš, Klemens Fellner, Peter Hofer, Monika Oberer, Renate Schreiber, Rudolf Zechner

Open access · hybridAbstract read
In one paragraph

Article in Bulletin of mathematical biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.6field-weighted citation impact, top 32% 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

1 citing paper in PubMed, 3 citations in OpenAlex.

  1. 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

6 authors at 1 institution in 1 country.

Ján EliašBoehringer Ingelheim RCV GmbH & Co KG, Dr. Boehringer-Gasse 5-11, 1121, Vienna, Austria.
Klemens FellnerInstitute of Mathematics and Scientific Computing, University of Graz, Heinrichstraße 36, 8010, Graz, Austria. klemens.fellner@uni-graz.at.ORCID 0000-0001-9906-8977
Peter HoferInstitute of Molecular Biosciences, University of Graz, Humboldtstraße 50, 8010, Graz, Austria.
Monika ObererInstitute of Molecular Biosciences, University of Graz, Humboldtstraße 50, 8010, Graz, Austria.
Renate SchreiberInstitute of Molecular Biosciences, University of Graz, Humboldtstraße 50, 8010, Graz, Austria.
Rudolf ZechnerInstitute of Molecular Biosciences, University of Graz, Humboldtstraße 50, 8010, Graz, Austria.
University of Graz · AT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Fatty acids (FAs) are crucial energy metabolites, signalling molecules, and membrane building blocks for a wide range of organisms. Adipose triglyceride lipase (ATGL) is the first and presumingly most crucial regulator of FA release from triacylglycerols (TGs) stored within cytosolic lipid droplets. However, besides the function of releasing FAs by hydrolysing TGs into diacylglycerols (DGs), ATGL also promotes the transacylation reaction of two DG molecules into one TG and one monoacylglycerol molecule. To date, it is unknown whether DG transacylation is a coincidental byproduct of ATGL-mediated lipolysis or whether it is physiologically relevant. Experimental evidence is scarce since both, hydrolysis and transacylation, rely on the same active site of ATGL and always occur in parallel in an ensemble of molecules. This paper illustrates the potential roles of transacylation. It shows that, depending on the kinetic parameters but also on the state of the hydrolytic machinery, transacylation can increase or decrease downstream products up to 80% respectively 30%. We provide an extensive asymptotic analysis including quasi-steady-state approximations (QSSA) with higher order correction terms and provide numerical simulation. We also argue that when assessing the validity of QSSAs one should include parameter sensitivity derivatives. Our results suggest that the transacylation function of ATGL is of biological relevance by providing feedback options and altogether stability to the lipolytic machinery in adipocytes.

Indexed as

LipaseLipolysisAdipocytesFatty AcidsMathematical ConceptsModels, BiologicalTriglyceridesFatty AcidsLipaseTriglyceridesEnzyme reactionLipolysisMichaelis–MentenQuasi steady state approximationSimulationTransacylation

Identifiers

PMID37544001
PMCPMC10404580
OpenAlexW4385616044

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.