Exposure of cultured fibroblasts to the peptide PR-11 for the identification of induced proteome alterations and discovery of novel potential ligands.
dc.contributor.author | Breguez, Gustavo Silveira | |
dc.contributor.author | Neves, Leandro Xavier | |
dc.contributor.author | Rúbio, Karina Taciana Santos | |
dc.contributor.author | Freitas, Lorran Miranda Andrade de | |
dc.contributor.author | Faria, Gabriela de Oliveira | |
dc.contributor.author | Isoldi, Mauro César | |
dc.contributor.author | Borges, William de Castro | |
dc.contributor.author | Andrade, Milton Hércules Guerra de | |
dc.date.accessioned | 2017-12-20T15:09:35Z | |
dc.date.available | 2017-12-20T15:09:35Z | |
dc.date.issued | 2016 | |
dc.description.abstract | 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. | pt_BR |
dc.identifier.citation | 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. | pt_BR |
dc.identifier.doi | https://doi.org/10.1016/j.bbapap.2016.09.017 | |
dc.identifier.issn | 1570-9639 | |
dc.identifier.uri | http://www.repositorio.ufop.br/handle/123456789/9226 | |
dc.language.iso | en_US | pt_BR |
dc.rights | aberto | pt_BR |
dc.rights.license | 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. | pt_BR |
dc.subject | Proline rich-peptides | pt_BR |
dc.subject | Label-free shotgun | pt_BR |
dc.title | Exposure of cultured fibroblasts to the peptide PR-11 for the identification of induced proteome alterations and discovery of novel potential ligands. | pt_BR |
dc.type | Artigo publicado em periodico | pt_BR |
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