Evidence map›Paper›PMID 29713565›Full record

ArticlePeerJ2018

Increased chemical acetylation of peptides and proteins in rats after daily ingestion of diacetyl analyzed by Nano-LC-MS/MS.

Leticia Dias Lima Jedlicka, Sheila Barreto Guterres, Aleksandro Martins Balbino, Giuseppe Bruno Neto, Richardt Gama Landgraf, Liliam Fernandes, Emanuel Carrilho, Etelvino José Henriques Bechara, Nilson A Assuncao

Open access · goldAbstract read
In one paragraph

Article in PeerJ, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.2field-weighted citation impact, top 47% 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

2 citing papers in PubMed, 8 citations in OpenAlex.

  1. Posttranslational Modifications ofPharmacological reviews · 2024
    Review
  2. 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.

Leticia Dias Lima JedlickaInstitute of Environmental, Chemical and Pharmaceutical Sciences, Universidade Federal de São Paulo, Diadema, SP, Brazil.
Sheila Barreto GuterresInstitute of Environmental, Chemical and Pharmaceutical Sciences, Universidade Federal de São Paulo, Diadema, SP, Brazil.
Aleksandro Martins BalbinoInstitute of Environmental, Chemical and Pharmaceutical Sciences, Universidade Federal de São Paulo, Diadema, SP, Brazil.
Giuseppe Bruno NetoInstitute of Environmental, Chemical and Pharmaceutical Sciences, Universidade Federal de São Paulo, Diadema, SP, Brazil.
Richardt Gama LandgrafInstitute of Environmental, Chemical and Pharmaceutical Sciences, Universidade Federal de São Paulo, Diadema, SP, Brazil.
Liliam FernandesInstitute of Environmental, Chemical and Pharmaceutical Sciences, Universidade Federal de São Paulo, Diadema, SP, Brazil.
Emanuel CarrilhoSão Carlos Institute of Chemistry, Universidade de São Paulo, São Carlos, SP, Brazil.
Etelvino José Henriques BecharaInstitute of Environmental, Chemical and Pharmaceutical Sciences, Universidade Federal de São Paulo, Diadema, SP, Brazil.
Nilson A AssuncaoInstitute of Environmental, Chemical and Pharmaceutical Sciences, Universidade Federal de São Paulo, Diadema, SP, Brazil.
Universidade Federal de São Paulo · BRUniversidade de São Paulo · BR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundAcetylation alters several protein properties including molecular weight, stability, enzymatic activity, protein-protein interactions, and other biological functions. Our previous findings demonstrating that diacetyl/peroxynitrite can acetylate L-lysine, L-histidine, and albumin

methodsWistar rats were administered diacetyl daily for four weeks, after which they were sacrificed, and their lung proteins were extracted to be analysed by Nano-LC-MS/MS (Q-TOF). A C18 reversed-phase column and gradient elution with formic acid/acetonitrile solutions from 2 to 50% over 150 min were used to separate the proteins. Protein detection was performed using a microTOF-Q II (QTOF) equipped with captive source and an electrospray-ionization source. The data from mass spectrometry were processed using a Compass 1.7 and analyzed using Protein Scape, software that uses Mascot algorithms to perform protein searches.

resultsA set of 3,162 acetylated peptides derived from 351 acetylated proteins in the diacetyl-treated group was identified. Among them, 23 targeted proteins were significantly more acetylated in the diacetyl-treated group than in the PBS control. Protein acetylation of the group treated with 540 mg/kg/day of diacetyl was corroborated by Western blotting analysis.

conclusionsThese data support our hypothesis that diacetyl exposure in animals may lead to the generation of acetyl radicals, compounds that attach to proteins, affecting their functions and triggering adverse health problems.

Indexed as

DiacetylFood additiveLung diseasesProteomics.Radical acetylation

Identifiers

PMID29713565
PMCPMC5923218
OpenAlexW2802952093

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.