Evidence map›Paper›PMID 28209804›Full record

ArticleJournal of lipid research2017

Long-chain acyl-CoA synthetase isoforms differ in preferences for eicosanoid species and long-chain fatty acids.

Eric L Klett, Shufen Chen, Alekhya Yechoor, Fred B Lih, Rosalind A Coleman

Erratum issuedOpen access · hybridAbstract read
In one paragraph

Article in Journal of lipid research, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 59 papers.

0numbers the graph read from it
0cells of the map it votes in
59citing papers in PubMed
4.7field-weighted citation impact, top 5% 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

59 citing papers in PubMed, 103 citations in OpenAlex.

  1. Review
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  10. Recommendations for robust and reproducible research on ferroptosis.Nature reviews. Molecular cell biology · 2025
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  19. ACSL3 regulates breast cancer progressionCancer biology & medicine · 2024
    Article
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors at 2 institutions in 1 country.

Eric L KlettDepartment of Medicine, Division of Endocrinology, University of North Carolina School of Medicine, Chapel Hill, NC 27599 eklett@med.unc.edu.
Shufen ChenDepartment of Medicine, Division of Endocrinology, University of North Carolina School of Medicine, Chapel Hill, NC 27599.
Alekhya YechoorDepartment of Nutrition, University of North Carolina School of Public Health, Chapel Hill, NC 27599.
Fred B LihDivision of Intramural Research, Epigenetics and Stem Cell Biology Laboratory (ESCBL), National Institute of Environmental Health Sciences, National Institutes of Health, Research Triangle Park, NC 27709.
Rosalind A ColemanDepartment of Nutrition, University of North Carolina School of Public Health, Chapel Hill, NC 27599.
University of North Carolina at Chapel Hill · USNational Institute of Environmental Health Sciences · US

Funding

UNIV OF NORTH CAROLINA CLINICAL NUTRITION RESEARCH UNITP30DK056350 · NIDDK · UNIV OF NORTH CAROLINA CHAPEL HILL · PI SUSAN M. SMITH · 1999 to 2026
$31.6M
Acyl-CoA Synthetase: Structure, Function and RegulationR01DK059935 · NIDDK · UNIV OF NORTH CAROLINA CHAPEL HILL · PI COLEMAN, ROSALIND ANNE · 2002 to 2015
$4.7M
Lipid Metabolism and Beta-cell FunctionR01DK107481 · NIDDK · UNIV OF NORTH CAROLINA CHAPEL HILL · PI KLETT, ERIC · 2016 to 2020
$1.7M
Role of acyl-CoA synthetases in mouse pancreatic ??-cell functionK08DK090141 · NIDDK · UNIV OF NORTH CAROLINA CHAPEL HILL · PI KLETT, ERIC · 2010 to 2014
$775k
NIDDK NIH HHS K08 DK090141NIDDK NIH HHS P30 DK056350NIDDK NIH HHS R01 DK059935NIDDK NIH HHS R01 DK107481
6 · The paper itself

Abstract

Because the signaling eicosanoids, epoxyeicosatrienoic acids (EETs) and HETEs, are esterified to membrane phospholipids, we asked which long-chain acyl-CoA synthetase (ACSL) isoforms would activate these molecules and whether the apparent FA substrate preferences of each ACSL isoform might differ depending on whether it was assayed in mammalian cell membranes or as a purified bacterial recombinant protein. We found that all five ACSL isoforms were able to use EETs and HETEs as substrates and showed by LC-MS/MS that ACSLs produce EET-CoAs. We found differences in substrate preference between ACS assays performed in COS7 cell membranes and recombinant purified proteins. Similarly, preferences and Michaelis-Menten kinetics for long-chain FAs were distinctive. Substrate preferences identified for the purified ACSLs did not correspond to those observed in ACSL-deficient mouse models. Taken together, these data support the concept that each ACSL isoform exhibits a distinct substrate preference, but apparent substrate specificities depend upon multiple factors including membrane character, coactivators, inhibitors, protein interactions, and posttranslational modification.

Indexed as

AnimalsChlorocebus aethiopsCoenzyme A LigasesCOS CellsEicosanoidsIsoenzymesLong-Chain-Fatty-Acid-CoA LigaseRatsSubstrate SpecificityCoenzyme A LigasesEicosanoidsIsoenzymesLong-Chain-Fatty-Acid-CoA Ligaseacyl-coenzyme Aarachidonic acidcytochrome P450fatty acid/metabolismphospholipids

Identifiers

PMID28209804
PMCPMC5408607
OpenAlexW2588418869

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.