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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

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

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Author(s):
Lima Jedlicka, Leticia Dias [1, 2] ; Guterres, Sheila Barreto [1, 3] ; Balbino, Aleksandro Martins [1] ; Neto, Giuseppe Bruno [1] ; Landgraf, Richardt Gama [1] ; Fernandes, Liliam [1] ; Carrilho, Emanuel [4] ; Henriques Bechara, Etelvino Jose [1, 5] ; Assuncao, Nilson A. [1]
Total Authors: 9
Affiliation:
[1] Univ Fed Sao Paulo, Inst Environm Chem & Pharmaceut Sci, Diadema, SP - Brazil
[2] Univ Fed Sul & Sudeste Para, Inst Studies Hlth & Biol, Collect Hlth, Maraba, PA - Brazil
[3] Fundacao Univ Fed Rondonia, Dept Chem, Porto Velho, RO - Brazil
[4] Univ Sao Paulo, Sao Carlos Inst Chem, Sao Carlos, SP - Brazil
[5] Univ Sao Paulo, Inst Chem, Dept Fundamental Chem, Sao Paulo, SP - Brazil
Total Affiliations: 5
Document type: Journal article
Source: PeerJ; v. 6, APR 25 2018.
Web of Science Citations: 2
Abstract

Background. Acetylation 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 in vitro led us to investigate whether diacetyl-treated rats suffer protein acetylation as well. Methods. Wistar 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 colurnn 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 microTOE-Q II (QTOF) equipped with captive source and an electrospray-ionization source. The data frommass spectrometry were processed using a Compass 1.7 and analyzed using Protein Scape, software that uses Mascot algorithms to perform protein searches. Results. A 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. Conclusions. These 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. (AU)

FAPESP's process: 13/07763-0 - Studies of Radical Acetylation of Proteins Using Proteomics Tools
Grantee:Leticia Dias Lima Jedlicka
Support Opportunities: Scholarships in Brazil - Doctorate
FAPESP's process: 12/02514-9 - Use of proteomics techniques to study radical acetylation of proteins triggered by products of the reaction biacetyl/peroxinitrite
Grantee:Nilson Antonio de Assunção
Support Opportunities: Regular Research Grants
FAPESP's process: 10/01404-0 - In vivo and in vitro studies of the leptin role in different models of lung inflammation: inflammatory mediators and signaling airways participation
Grantee:Richardt Gama Landgraf
Support Opportunities: Research Grants - Young Investigators Grants