Evidence map›Paper›PMID 20533355›Full record

ArticleThe Journal of comparative neurology2010

Nuclear-cytoplasmic localization of acetyl coenzyme a synthetase-1 in the rat brain.

Prasanth S Ariyannur, John R Moffett, Chikkathur N Madhavarao, Peethambaran Arun, Nisha Vishnu, David M Jacobowitz, William C Hallows, John M Denu, Aryan M A Namboodiri

Open access · greenAbstract read
In one paragraph

Article in The Journal of comparative neurology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.

0numbers the graph read from it
0cells of the map it votes in
48citing papers in PubMed
2.2field-weighted citation impact, top 13% 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

48 citing papers in PubMed, 63 citations in OpenAlex.

  1. Article
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  16. Brain ethanol metabolism and mitochondria.Current topics in biochemical research · 2022
    Article
  17. Review
  18. Article
  19. Review
  20. 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 2 institutions in 1 country.

Prasanth S AriyannurDepartment of Anatomy, Molecular and Cell Biology Program and Neuroscience Program, Uniformed Services University of the Health Sciences, Bethesda, Maryland 20814, USA.
John R Moffett
Chikkathur N Madhavarao
Peethambaran Arun
Nisha Vishnu
David M Jacobowitz
William C Hallows
John M Denu
Aryan M A Namboodiri
Uniformed Services University of the Health Sciences · USUniversity of Wisconsin–Madison · US

Funding

Reversible protein acetylation and sirtuin functionR01GM065386 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI DENU, JOHN M · 2003 to 2022
$7.3M
CANAVAN DISEASE PATHOGENESIS AND TREATMENTR01NS039387 · NINDS · HENRY M. JACKSON FDN FOR THE ADV MIL/MED · PI NAMBOODIRI, ARYAN MANGALAM · 2000 to 2002
$534k
COEXISTENCE OF PEPTIDES AND NEUROTRANSMITTERS--CALRETININ IN NEUROGLIOMAZ01MH000388 · NIMH · NATIONAL INSTITUTE OF MENTAL HEALTH · PI JACOBOWITZ, D M · 1985 to 1997
–
NIGMS NIH HHS R01 GM065386NIMH NIH HHS ZO-1-MH-00388-31NINDS NIH HHS R01 NS039387NINDS NIH HHS R01 NS39387
6 · The paper itself

Abstract

Acetyl coenzyme A synthetase-1 (AceCS1) catalyzes the synthesis of acetyl coenzyme A from acetate and coenzyme A and is thought to play diverse roles ranging from fatty acid synthesis to gene regulation. By using an affinity-purified antibody generated against an 18-mer peptide sequence of AceCS1 and a polyclonal antibody directed against recombinant AceCS1 protein, we examined the expression of AceCS1 in the rat brain. AceCS1 immunoreactivity in the adult rat brain was present predominantly in cell nuclei, with only light to moderate cytoplasmic staining in some neurons, axons, and oligodendrocytes. Some nonneuronal cell nuclei were very strongly immunoreactive, including those of some oligodendrocytes, whereas neuronal nuclei ranged from unstained to moderately stained. Both antibodies stained some neuronal cell bodies and axons, especially in the hindbrain. AceCS1 immunoreactivity was stronger and more widespread in the brains of 18-day-old rats than in adults, with increased expression in oligodendrocytes and neurons, including cortical pyramidal cells. Expression of AceCS1 was substantially up-regulated in neurons throughout the brain after controlled cortical impact injury. The strong AceCS1 expression observed in the nuclei of CNS cells during brain development and after injury is consistent with a role in nuclear histone acetylation and therefore the regulation of chromatin structure and gene expression. The cytoplasmic staining observed in some oligodendrocytes, especially during postnatal brain development, suggests an additional role in CNS lipid synthesis and myelination. Neuronal and axonal localization implicates AceCS1 in cytoplasmic acetylation reactions in some neurons.

Indexed as

AnimalsBlotting, WesternBrainBrain InjuriesCell NucleusCerebral CortexChromatography, AffinityCoenzyme A LigasesCytoplasmElectrophoresis, Polyacrylamide GelFemaleGlial Fibrillary Acidic ProteinImmunoenzyme TechniquesImmunohistochemistryImmunoprecipitationMaleAcsl1 protein, ratCoenzyme A LigasesGlial Fibrillary Acidic Protein

Identifiers

PMID20533355
PMCPMC3047483
OpenAlexW2074065976

What OpenQuestion holds

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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.