Evidence map›Paper›PMID 17197235›Full record

ArticleBiochimica et biophysica acta2007

Ontogeny of mRNA expression and activity of long-chain acyl-CoA synthetase (ACSL) isoforms in Mus musculus heart.

Hendrik de Jong, Andrea C Neal, Rosalind A Coleman, Tal M Lewin

Open access · greenAbstract readComparative Study
In one paragraph

Article in Biochimica et biophysica acta, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
0.8field-weighted citation impact, top 30% 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

19 citing papers in PubMed, 37 citations in OpenAlex.

  1. Trial
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  11. Acyl-CoA metabolism and partitioning.Annual review of nutrition · 2014
    Review
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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

4 authors at 1 institution in 2 countries.

Hendrik de JongDepartment of Nutrition, University of North Carolina at Chapel Hill, CB# 7461, NC 27599, USA.
Andrea C Neal
Rosalind A Coleman
Tal M Lewin
University of North Carolina at Chapel Hill · 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
Obesity and Diabetes induced cardiomyopathyK01DK059931 · NIDDK · UNIVERSITY OF NORTH CAROLINA CHAPEL HILL · PI LEWIN, TAL M · 2002 to 2004
$299k
NIDDK NIH HHS DK56350NIDDK NIH HHS DK59931NIDDK NIH HHS DK59935NIDDK NIH HHS K01 DK059931NIDDK NIH HHS P30 DK056350NIDDK NIH HHS R01 DK059935
6 · The paper itself

Abstract

Long-chain acyl-CoA synthetases (ACSL) activate fatty acids (FA) and provide substrates for virtually every metabolic pathway that catabolizes FA or synthesizes complex lipids. We have hypothesized that each of the five cloned ACSL isoforms partitions FA towards specific downstream pathways. Adult heart expresses all five cloned ACSL isoforms, but their independent functional roles have not been elucidated. Studies implicate ACSL1 in both oxidative and lipid synthetic pathways. To clarify the functional role of ACSL1 and the other ACSL isoforms (3-6), we examined ACS specific activity and Acsl mRNA expression in the developing mouse heart which increases FA oxidative pathways for energy production after birth. Compared to the embryonic heart, ACS specific activity was 14-fold higher on post-natal day 1 (P1). On P1, as compared to the fetus, only Acsl1 mRNA increased, whereas transcripts for the other Acsl isoforms remained the same, suggesting that ACSL1 is the major isoform responsible for activating long-chain FA for myocardial oxidation after birth. In contrast, the mRNA abundance of Acsl3 was highest on E16, and decreased dramatically by P7, suggesting that ACSL3 may play a critical role during the development of the fetal heart. Our data support the hypothesis that each ACSL has a specific role in the channeling of FA towards distinct metabolic fates.

Indexed as

Lipid MetabolismAnimalsAnimals, NewbornCoenzyme A LigasesFatty AcidsFetusGene Expression Regulation, EnzymologicHeartIsoenzymesLong-Chain-Fatty-Acid-CoA LigaseMiceMyocardiumOxidation-ReductionRNA, MessengerCoenzyme A LigasesFatty AcidsIsoenzymesLong-Chain-Fatty-Acid-CoA LigaseRNA, Messenger

Identifiers

PMID17197235
PMCPMC1797059
OpenAlexW2044731074

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.