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

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dc.citation.volumev. 6
dc.contributor.authorJedlicka, Leticia Dias Lima [UNIFESP]
dc.contributor.authorGuterres, Sheila Barreto [UNIFESP]
dc.contributor.authorBalbino, Aleksandro Martins [UNIFESP]
dc.contributor.authorBruno Neto, Giuseppe [UNIFESP]
dc.contributor.authorLandgraf, Richardt Gama [UNIFESP]
dc.contributor.authorFernandes, Liliam [UNIFESP]
dc.contributor.authorCarrilho, Emanuel
dc.contributor.authorBechara, Etelvino José Henriques [UNIFESP]
dc.contributor.authorAssunção, Nilson Antonio [UNIFESP]
dc.coverageLondon
dc.date.accessioned2020-07-20T16:30:59Z
dc.date.available2020-07-20T16:30:59Z
dc.date.issued2018
dc.description.abstractBackground. 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.en
dc.description.affiliationUniv Fed Sao Paulo, Inst Environm Chem & Pharmaceut Sci, Diadema, SP, Brazil
dc.description.affiliationUniv Fed Sul & Sudeste Para, Inst Studies Hlth & Biol, Collect Hlth, Maraba, PA, Brazil
dc.description.affiliationFundacao Univ Fed Rondonia, Dept Chem, Porto Velho, RO, Brazil
dc.description.affiliationUniv Sao Paulo, Sao Carlos Inst Chem, Sao Carlos, SP, Brazil
dc.description.affiliationUniv Sao Paulo, Inst Chem, Dept Fundamental Chem, Sao Paulo, SP, Brazil
dc.description.affiliationUnifespUniv Fed Sao Paulo, Inst Environm Chem & Pharmaceut Sci, Diadema, SP, Brazil
dc.description.sourceWeb of Science
dc.description.sponsorshipSao Paulo Research Foundation (FAPESP)
dc.description.sponsorshipBrazilian Innovation Agency (FINEP)
dc.description.sponsorshipIDFAPESP: 2012/02514-9
dc.description.sponsorshipIDFAPESP: 2013/07763-0
dc.description.sponsorshipIDFAPESP: 2010/01404-0
dc.format.extent-
dc.identifierhttp://dx.doi.org/10.7717/peerj.4688
dc.identifier.citationPeerj. London, v. 6, p. -, 2018.
dc.identifier.doi10.7717/peerj.4688
dc.identifier.fileWOS000430890200002.pdf
dc.identifier.issn2167-8359
dc.identifier.urihttps://repositorio.unifesp.br/handle/11600/55628
dc.identifier.wosWOS:000430890200002
dc.language.isoeng
dc.publisherPeerj Inc
dc.relation.ispartofPeerj
dc.rightsinfo:eu-repo/semantics/openAccess
dc.subjectRadical acetylationen
dc.subjectDiacetylen
dc.subjectFood additiveen
dc.subjectLung diseasesen
dc.subjectProteomicsen
dc.titleIncreased chemical acetylation of peptides and proteins in rats after daily ingestion of diacetyl analyzed by Nano-LC-MS/MSen
dc.typeinfo:eu-repo/semantics/article
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