Exposure of cultured fibroblasts to the peptide PR-11 for the identification of induced proteome alterations and discovery of novel potential ligands.

dc.contributor.authorBreguez, Gustavo Silveira
dc.contributor.authorNeves, Leandro Xavier
dc.contributor.authorRúbio, Karina Taciana Santos
dc.contributor.authorFreitas, Lorran Miranda Andrade de
dc.contributor.authorFaria, Gabriela de Oliveira
dc.contributor.authorIsoldi, Mauro César
dc.contributor.authorBorges, William de Castro
dc.contributor.authorAndrade, Milton Hércules Guerra de
dc.date.accessioned2017-12-20T15:09:35Z
dc.date.available2017-12-20T15:09:35Z
dc.date.issued2016
dc.description.abstractThe 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.citationBREGUEZ, 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.doihttps://doi.org/10.1016/j.bbapap.2016.09.017
dc.identifier.issn1570-9639
dc.identifier.urihttp://www.repositorio.ufop.br/handle/123456789/9226
dc.language.isoen_USpt_BR
dc.rightsabertopt_BR
dc.rights.licenseO 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.subjectProline rich-peptidespt_BR
dc.subjectLabel-free shotgunpt_BR
dc.titleExposure of cultured fibroblasts to the peptide PR-11 for the identification of induced proteome alterations and discovery of novel potential ligands.pt_BR
dc.typeArtigo publicado em periodicopt_BR
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