Increased chemical acetylation of peptides and proteins in rats after daily ingestion of diacetyl analyzed by Nano-LC-MS/MS
Autor(a) principal: | |
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Data de Publicação: | 2018 |
Outros Autores: | , , , , , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Institucional da UNIFESP |
Texto Completo: | https://repositorio.unifesp.br/handle/11600/55628 http://dx.doi.org/10.7717/peerj.4688 |
Resumo: | 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. |
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Jedlicka, Leticia Dias Lima [UNIFESP]Guterres, Sheila Barreto [UNIFESP]Balbino, Aleksandro Martins [UNIFESP]Bruno Neto, Giuseppe [UNIFESP]Landgraf, Richardt Gama [UNIFESP]Fernandes, Liliam [UNIFESP]Carrilho, EmanuelBechara, Etelvino José Henriques [UNIFESP]Assunção, Nilson Antonio [UNIFESP]2020-07-20T16:30:59Z2020-07-20T16:30:59Z2018Peerj. London, v. 6, p. -, 2018.2167-8359https://repositorio.unifesp.br/handle/11600/55628http://dx.doi.org/10.7717/peerj.4688WOS000430890200002.pdf10.7717/peerj.4688WOS:000430890200002Background. 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.Sao Paulo Research Foundation (FAPESP)Brazilian Innovation Agency (FINEP)Univ Fed Sao Paulo, Inst Environm Chem & Pharmaceut Sci, Diadema, SP, BrazilUniv Fed Sul & Sudeste Para, Inst Studies Hlth & Biol, Collect Hlth, Maraba, PA, BrazilFundacao Univ Fed Rondonia, Dept Chem, Porto Velho, RO, BrazilUniv Sao Paulo, Sao Carlos Inst Chem, Sao Carlos, SP, BrazilUniv Sao Paulo, Inst Chem, Dept Fundamental Chem, Sao Paulo, SP, BrazilUniv Fed Sao Paulo, Inst Environm Chem & Pharmaceut Sci, Diadema, SP, BrazilFAPESP: 2012/02514-9FAPESP: 2013/07763-0FAPESP: 2010/01404-0Web of Science-engPeerj IncPeerjRadical acetylationDiacetylFood additiveLung diseasesProteomicsIncreased chemical acetylation of peptides and proteins in rats after daily ingestion of diacetyl analyzed by Nano-LC-MS/MSinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleLondonv. 6info:eu-repo/semantics/openAccessreponame:Repositório Institucional da UNIFESPinstname:Universidade Federal de São Paulo (UNIFESP)instacron:UNIFESPORIGINALWOS000430890200002.pdfapplication/pdf6858024${dspace.ui.url}/bitstream/11600/55628/1/WOS000430890200002.pdfac6e6cfa28281d2fd33d22b733afb64aMD51open accessTEXTWOS000430890200002.pdf.txtWOS000430890200002.pdf.txtExtracted texttext/plain53781${dspace.ui.url}/bitstream/11600/55628/8/WOS000430890200002.pdf.txt84d79ed5283f7718181e4adf13b22524MD58open accessTHUMBNAILWOS000430890200002.pdf.jpgWOS000430890200002.pdf.jpgIM Thumbnailimage/jpeg7263${dspace.ui.url}/bitstream/11600/55628/10/WOS000430890200002.pdf.jpg2daa525c99f064ed897156a4633fb858MD510open access11600/556282023-06-05 19:28:09.31open accessoai:repositorio.unifesp.br:11600/55628Repositório InstitucionalPUBhttp://www.repositorio.unifesp.br/oai/requestopendoar:34652023-06-05T22:28:09Repositório Institucional da UNIFESP - Universidade Federal de São Paulo (UNIFESP)false |
dc.title.en.fl_str_mv |
Increased chemical acetylation of peptides and proteins in rats after daily ingestion of diacetyl analyzed by Nano-LC-MS/MS |
title |
Increased chemical acetylation of peptides and proteins in rats after daily ingestion of diacetyl analyzed by Nano-LC-MS/MS |
spellingShingle |
Increased chemical acetylation of peptides and proteins in rats after daily ingestion of diacetyl analyzed by Nano-LC-MS/MS Jedlicka, Leticia Dias Lima [UNIFESP] Radical acetylation Diacetyl Food additive Lung diseases Proteomics |
title_short |
Increased chemical acetylation of peptides and proteins in rats after daily ingestion of diacetyl analyzed by Nano-LC-MS/MS |
title_full |
Increased chemical acetylation of peptides and proteins in rats after daily ingestion of diacetyl analyzed by Nano-LC-MS/MS |
title_fullStr |
Increased chemical acetylation of peptides and proteins in rats after daily ingestion of diacetyl analyzed by Nano-LC-MS/MS |
title_full_unstemmed |
Increased chemical acetylation of peptides and proteins in rats after daily ingestion of diacetyl analyzed by Nano-LC-MS/MS |
title_sort |
Increased chemical acetylation of peptides and proteins in rats after daily ingestion of diacetyl analyzed by Nano-LC-MS/MS |
author |
Jedlicka, Leticia Dias Lima [UNIFESP] |
author_facet |
Jedlicka, Leticia Dias Lima [UNIFESP] Guterres, Sheila Barreto [UNIFESP] Balbino, Aleksandro Martins [UNIFESP] Bruno Neto, Giuseppe [UNIFESP] Landgraf, Richardt Gama [UNIFESP] Fernandes, Liliam [UNIFESP] Carrilho, Emanuel Bechara, Etelvino José Henriques [UNIFESP] Assunção, Nilson Antonio [UNIFESP] |
author_role |
author |
author2 |
Guterres, Sheila Barreto [UNIFESP] Balbino, Aleksandro Martins [UNIFESP] Bruno Neto, Giuseppe [UNIFESP] Landgraf, Richardt Gama [UNIFESP] Fernandes, Liliam [UNIFESP] Carrilho, Emanuel Bechara, Etelvino José Henriques [UNIFESP] Assunção, Nilson Antonio [UNIFESP] |
author2_role |
author author author author author author author author |
dc.contributor.author.fl_str_mv |
Jedlicka, Leticia Dias Lima [UNIFESP] Guterres, Sheila Barreto [UNIFESP] Balbino, Aleksandro Martins [UNIFESP] Bruno Neto, Giuseppe [UNIFESP] Landgraf, Richardt Gama [UNIFESP] Fernandes, Liliam [UNIFESP] Carrilho, Emanuel Bechara, Etelvino José Henriques [UNIFESP] Assunção, Nilson Antonio [UNIFESP] |
dc.subject.eng.fl_str_mv |
Radical acetylation Diacetyl Food additive Lung diseases Proteomics |
topic |
Radical acetylation Diacetyl Food additive Lung diseases Proteomics |
description |
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. |
publishDate |
2018 |
dc.date.issued.fl_str_mv |
2018 |
dc.date.accessioned.fl_str_mv |
2020-07-20T16:30:59Z |
dc.date.available.fl_str_mv |
2020-07-20T16:30:59Z |
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dc.identifier.citation.fl_str_mv |
Peerj. London, v. 6, p. -, 2018. |
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https://repositorio.unifesp.br/handle/11600/55628 http://dx.doi.org/10.7717/peerj.4688 |
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2167-8359 |
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10.7717/peerj.4688 |
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