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

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MetadadosDescriçãoIdioma
Autor(es): dc.creatorBreguez, Gustavo Silveira-
Autor(es): dc.creatorNeves, Leandro Xavier-
Autor(es): dc.creatorRúbio, Karina Taciana Santos-
Autor(es): dc.creatorFreitas, Lorran Miranda Andrade de-
Autor(es): dc.creatorFaria, Gabriela de Oliveira-
Autor(es): dc.creatorIsoldi, Mauro César-
Autor(es): dc.creatorBorges, William de Castro-
Autor(es): dc.creatorAndrade, Milton Hércules Guerra de-
Data de aceite: dc.date.accessioned2025-08-21T15:11:48Z-
Data de disponibilização: dc.date.available2025-08-21T15:11:48Z-
Data de envio: dc.date.issued2017-12-20-
Data de envio: dc.date.issued2017-12-20-
Data de envio: dc.date.issued2016-
Fonte completa do material: dc.identifierhttp://www.repositorio.ufop.br/handle/123456789/9226-
Fonte completa do material: dc.identifierhttps://doi.org/10.1016/j.bbapap.2016.09.017-
Fonte: dc.identifier.urihttp://educapes.capes.gov.br/handle/capes/1005295-
Descrição: dc.descriptionThe 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.-
Formato: dc.formatapplication/pdf-
Idioma: dc.languageen-
Direitos: dc.rightsaberto-
Direitos: dc.rightsO periódico Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics concede permissão para depósito deste artigo no Repositório Institucional da UFOP. Número da licença: 4210811289890.-
Palavras-chave: dc.subjectProline rich-peptides-
Palavras-chave: dc.subjectLabel-free shotgun-
Título: dc.titleExposure of cultured fibroblasts to the peptide PR-11 for the identification of induced proteome alterations and discovery of novel potential ligands.-
Aparece nas coleções:Repositório Institucional - UFOP

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