Exposure of cultured fibroblasts to the peptide PR-11 for the identification of induced proteome alterations and discovery of novel potential ligands.
Autor(a) principal: | |
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Data de Publicação: | 2016 |
Outros Autores: | , , , , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Institucional da UFOP |
Texto Completo: | http://www.repositorio.ufop.br/handle/123456789/9226 https://doi.org/10.1016/j.bbapap.2016.09.017 |
Resumo: | The PR-11 peptide corresponds to the N-terminal and active region of the endogenously synthesized PR-39 molecule, of porcine origin. It is known to possess various biological effects including antimicrobial properties, angiogenic and anti-inflammatory activities. Apart from its reported activity as a proteasome inhibitor, a more comprehensive understanding of its function, at the molecular level, is still lacking. In this study, we used a label-free shotgun strategy to evaluate the proteomic alterations caused by exposure of cultured fibroblasts to the peptide PR-11. This approach revealed that more than half of the identified moleculeswere related to signalling, transcription and translation. Proteins directly associated to regulation of angiogenesis and interaction with the hypoxia-inducible factor 1-α (HIF-1α) were significantly altered. In addition, at least three differentially expressed molecules of the NF-κB pathway were detected, suggesting an anti-inflammatory property of PR-11. At last, we demonstrated novel potential ligands of PR-11, through its immobilization for affinity chromatography. Among the elutedmolecules, gC1qR, a known complement receptor, appearedmarkedly enriched. This provided preliminary evidence of a PR-11 ligand possibly involved in the internalization of this peptide. Altogether, our findings contributed to a better understanding of the cellular pathways affected by PR-39 derived molecules. |
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Breguez, Gustavo SilveiraNeves, Leandro XavierRúbio, Karina Taciana SantosFreitas, Lorran Miranda Andrade deFaria, Gabriela de OliveiraIsoldi, Mauro CésarBorges, William de CastroAndrade, Milton Hércules Guerra de2017-12-20T15:09:35Z2017-12-20T15:09:35Z2016BREGUEZ, G. S. et al. Exposure of cultured fibroblasts to the peptide PR-11 for the identification of induced proteome alterations and discovery of novel potential ligands. Biochimica et Biophysica Acta. Proteins and Proteomics, v. 1864, p. 1775-1786, 2016.Disponível em: <http://www.sciencedirect.com/science/article/pii/S157096391630200X?via%3Dihub>. Acesso em: 15 set. 2017.1570-9639http://www.repositorio.ufop.br/handle/123456789/9226https://doi.org/10.1016/j.bbapap.2016.09.017The PR-11 peptide corresponds to the N-terminal and active region of the endogenously synthesized PR-39 molecule, of porcine origin. It is known to possess various biological effects including antimicrobial properties, angiogenic and anti-inflammatory activities. Apart from its reported activity as a proteasome inhibitor, a more comprehensive understanding of its function, at the molecular level, is still lacking. In this study, we used a label-free shotgun strategy to evaluate the proteomic alterations caused by exposure of cultured fibroblasts to the peptide PR-11. This approach revealed that more than half of the identified moleculeswere related to signalling, transcription and translation. Proteins directly associated to regulation of angiogenesis and interaction with the hypoxia-inducible factor 1-α (HIF-1α) were significantly altered. In addition, at least three differentially expressed molecules of the NF-κB pathway were detected, suggesting an anti-inflammatory property of PR-11. At last, we demonstrated novel potential ligands of PR-11, through its immobilization for affinity chromatography. Among the elutedmolecules, gC1qR, a known complement receptor, appearedmarkedly enriched. This provided preliminary evidence of a PR-11 ligand possibly involved in the internalization of this peptide. Altogether, our findings contributed to a better understanding of the cellular pathways affected by PR-39 derived molecules.O periódico Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics concede permissão para depósito deste artigo no Repositório Institucional da UFOP. Número da licença: 4210811289890.info:eu-repo/semantics/openAccessProline rich-peptidesLabel-free shotgunExposure of cultured fibroblasts to the peptide PR-11 for the identification of induced proteome alterations and discovery of novel potential ligands.info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleengreponame:Repositório Institucional da UFOPinstname:Universidade Federal de Ouro Preto (UFOP)instacron:UFOPLICENSElicense.txtlicense.txttext/plain; charset=utf-8924http://www.repositorio.ufop.br/bitstream/123456789/9226/2/license.txt62604f8d955274beb56c80ce1ee5dcaeMD52ORIGINALARTIGO_ExposureCulturedFibroblast.pdfARTIGO_ExposureCulturedFibroblast.pdfapplication/pdf932399http://www.repositorio.ufop.br/bitstream/123456789/9226/1/ARTIGO_ExposureCulturedFibroblast.pdf601e497e272dc9204a49e66a555117f9MD51123456789/92262020-02-20 09:57:47.588oai:localhost: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ório InstitucionalPUBhttp://www.repositorio.ufop.br/oai/requestrepositorio@ufop.edu.bropendoar:32332020-02-20T14:57:47Repositório Institucional da UFOP - Universidade Federal de Ouro Preto (UFOP)false |
dc.title.pt_BR.fl_str_mv |
Exposure of cultured fibroblasts to the peptide PR-11 for the identification of induced proteome alterations and discovery of novel potential ligands. |
title |
Exposure of cultured fibroblasts to the peptide PR-11 for the identification of induced proteome alterations and discovery of novel potential ligands. |
spellingShingle |
Exposure of cultured fibroblasts to the peptide PR-11 for the identification of induced proteome alterations and discovery of novel potential ligands. Breguez, Gustavo Silveira Proline rich-peptides Label-free shotgun |
title_short |
Exposure of cultured fibroblasts to the peptide PR-11 for the identification of induced proteome alterations and discovery of novel potential ligands. |
title_full |
Exposure of cultured fibroblasts to the peptide PR-11 for the identification of induced proteome alterations and discovery of novel potential ligands. |
title_fullStr |
Exposure of cultured fibroblasts to the peptide PR-11 for the identification of induced proteome alterations and discovery of novel potential ligands. |
title_full_unstemmed |
Exposure of cultured fibroblasts to the peptide PR-11 for the identification of induced proteome alterations and discovery of novel potential ligands. |
title_sort |
Exposure of cultured fibroblasts to the peptide PR-11 for the identification of induced proteome alterations and discovery of novel potential ligands. |
author |
Breguez, Gustavo Silveira |
author_facet |
Breguez, Gustavo Silveira Neves, Leandro Xavier Rúbio, Karina Taciana Santos Freitas, Lorran Miranda Andrade de Faria, Gabriela de Oliveira Isoldi, Mauro César Borges, William de Castro Andrade, Milton Hércules Guerra de |
author_role |
author |
author2 |
Neves, Leandro Xavier Rúbio, Karina Taciana Santos Freitas, Lorran Miranda Andrade de Faria, Gabriela de Oliveira Isoldi, Mauro César Borges, William de Castro Andrade, Milton Hércules Guerra de |
author2_role |
author author author author author author author |
dc.contributor.author.fl_str_mv |
Breguez, Gustavo Silveira Neves, Leandro Xavier Rúbio, Karina Taciana Santos Freitas, Lorran Miranda Andrade de Faria, Gabriela de Oliveira Isoldi, Mauro César Borges, William de Castro Andrade, Milton Hércules Guerra de |
dc.subject.por.fl_str_mv |
Proline rich-peptides Label-free shotgun |
topic |
Proline rich-peptides Label-free shotgun |
description |
The PR-11 peptide corresponds to the N-terminal and active region of the endogenously synthesized PR-39 molecule, of porcine origin. It is known to possess various biological effects including antimicrobial properties, angiogenic and anti-inflammatory activities. Apart from its reported activity as a proteasome inhibitor, a more comprehensive understanding of its function, at the molecular level, is still lacking. In this study, we used a label-free shotgun strategy to evaluate the proteomic alterations caused by exposure of cultured fibroblasts to the peptide PR-11. This approach revealed that more than half of the identified moleculeswere related to signalling, transcription and translation. Proteins directly associated to regulation of angiogenesis and interaction with the hypoxia-inducible factor 1-α (HIF-1α) were significantly altered. In addition, at least three differentially expressed molecules of the NF-κB pathway were detected, suggesting an anti-inflammatory property of PR-11. At last, we demonstrated novel potential ligands of PR-11, through its immobilization for affinity chromatography. Among the elutedmolecules, gC1qR, a known complement receptor, appearedmarkedly enriched. This provided preliminary evidence of a PR-11 ligand possibly involved in the internalization of this peptide. Altogether, our findings contributed to a better understanding of the cellular pathways affected by PR-39 derived molecules. |
publishDate |
2016 |
dc.date.issued.fl_str_mv |
2016 |
dc.date.accessioned.fl_str_mv |
2017-12-20T15:09:35Z |
dc.date.available.fl_str_mv |
2017-12-20T15:09:35Z |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
format |
article |
status_str |
publishedVersion |
dc.identifier.citation.fl_str_mv |
BREGUEZ, G. S. et al. Exposure of cultured fibroblasts to the peptide PR-11 for the identification of induced proteome alterations and discovery of novel potential ligands. Biochimica et Biophysica Acta. Proteins and Proteomics, v. 1864, p. 1775-1786, 2016.Disponível em: <http://www.sciencedirect.com/science/article/pii/S157096391630200X?via%3Dihub>. Acesso em: 15 set. 2017. |
dc.identifier.uri.fl_str_mv |
http://www.repositorio.ufop.br/handle/123456789/9226 |
dc.identifier.issn.none.fl_str_mv |
1570-9639 |
dc.identifier.doi.none.fl_str_mv |
https://doi.org/10.1016/j.bbapap.2016.09.017 |
identifier_str_mv |
BREGUEZ, G. S. et al. Exposure of cultured fibroblasts to the peptide PR-11 for the identification of induced proteome alterations and discovery of novel potential ligands. Biochimica et Biophysica Acta. Proteins and Proteomics, v. 1864, p. 1775-1786, 2016.Disponível em: <http://www.sciencedirect.com/science/article/pii/S157096391630200X?via%3Dihub>. Acesso em: 15 set. 2017. 1570-9639 |
url |
http://www.repositorio.ufop.br/handle/123456789/9226 https://doi.org/10.1016/j.bbapap.2016.09.017 |
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eng |
language |
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openAccess |
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