Evidence map›Paper›PMID 27016726›Full record

ArticleJournal of lipid research2016

Glycine N-acyltransferase-like 3 is responsible for long-chain N-acylglycine formation in N18TG2 cells.

Kristen A Jeffries, Daniel R Dempsey, Emma K Farrell, Ryan L Anderson, Gabrielle J Garbade, Tatyana S Gurina, Imran Gruhonjic, Carly A Gunderson, David J Merkler

Open access · hybridAbstract read
In one paragraph

Article in Journal of lipid research, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
3.4field-weighted citation impact, top 9% 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

20 citing papers in PubMed, 27 citations in OpenAlex.

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  10. The Biosynthesis and Metabolism of theFrontiers in molecular biosciences · 2021
    Review
  11. Article
  12. Biomolecules · 2019
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  13. Article
  14. Article
  15. Review
  16. Article
  17. Bm-iAANAT and its potential role in fatty acid amide biosynthesis in Bombyx mori.Prostaglandins, leukotrienes, and essential fatty acids · 2018
    Article
  18. Article
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  20. Journal of biology and nature · 2017
    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

9 authors at 1 institution in 1 country.

Kristen A JeffriesDepartment of Chemistry, University of South Florida, Tampa, FL 33620.
Daniel R DempseyDepartment of Chemistry, University of South Florida, Tampa, FL 33620.
Emma K FarrellDepartment of Chemistry, University of South Florida, Tampa, FL 33620.
Ryan L AndersonDepartment of Chemistry, University of South Florida, Tampa, FL 33620.
Gabrielle J GarbadeDepartment of Chemistry, University of South Florida, Tampa, FL 33620.
Tatyana S GurinaDepartment of Chemistry, University of South Florida, Tampa, FL 33620.
Imran GruhonjicDepartment of Chemistry, University of South Florida, Tampa, FL 33620.
Carly A GundersonDepartment of Chemistry, University of South Florida, Tampa, FL 33620.
David J MerklerDepartment of Chemistry, University of South Florida, Tampa, FL 33620 merkler@usf.edu.ORCID 0000-0001-6659-0005
University of South Florida · US

Funding

Subtraction LipidomicsR15GM107864 · NIGMS · UNIVERSITY OF SOUTH FLORIDA · PI MERKLER, DAVID J · 2015 to 2017
$386k
Glycine N-AcyltransferasesR03DA034323 · NIDA · UNIVERSITY OF SOUTH FLORIDA · PI MERKLER, DAVID J · 2012 to 2013
$136k
NIDA NIH HHS R03 DA034323NIGMS NIH HHS R15 GM107864
6 · The paper itself

Abstract

Long-chain fatty acid amides are signaling lipids found in mammals and other organisms; however, details of the metabolic pathways for the N-acylglycines and primary fatty acid amides (PFAMs) have remained elusive. Heavy-labeled precursor and subtraction lipidomic experiments in mouse neuroblastoma N18TG2 cells, a model cell line for the study of fatty acid amide metabolism, establish the biosynthetic pathways for the N-acylglycines and the PFAMs. We provide evidence that the N-acylglycines are formed by a long-chain specific glycine-conjugating enzyme, glycine N-acyltransferase-like 3 (GLYATL3). siRNA knockdown of GLYATL3 in the N18TG2 cells resulted in a decrease in the levels of the N-acylglycines and the PFAMs. This is the first report of an enzyme responsible for long-chain N-acylglycine production in cellula. The production of the PFAMs in N18TG2 cells was reported to occur by the oxidative cleavage of the N-acylglycines, as catalyzed by peptidylglycine α-amidating monooxygenase (PAM). siRNA knockdown of PAM resulted in an accumulation of [(13)C18]N-oleoylglycine and decreased levels of [(13)C18]oleamide when the N18TG2 cells were grown in the presence of [(13)C18]oleic acid. The addition of [1-(13)C]palmitate to the N18TG2 cell growth media led to the production of a family of [1-(13)C]palmitoylated fatty acid amides, consistent with the biosynthetic pathways detailed herein.

Indexed as

AcyltransferasesAmidesAnimalsCell Line, TumorFatty AcidsGene Knockdown TechniquesLipogenesisMiceAcyltransferasesAmidesFatty AcidsGlyatl3 protein, mousearachidonic acidbrain lipidseicosanoidslipidsmass spectrometryN-acylamideneuroblastoma cellsoleamidepalmitoylationsiRNA knockdown

Identifiers

PMID27016726
PMCPMC4847626
OpenAlexW2306388496

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.