Please use this identifier to cite or link to this item: http://www.repositorio.ufop.br/handle/123456789/9226
Title: Exposure of cultured fibroblasts to the peptide PR-11 for the identification of induced proteome alterations and discovery of novel potential ligands.
Authors: 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
Keywords: Proline rich-peptides
Label-free shotgun
Issue Date: 2016
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.
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.
URI: http://www.repositorio.ufop.br/handle/123456789/9226
metadata.dc.identifier.doi: https://doi.org/10.1016/j.bbapap.2016.09.017
ISSN: 1570-9639
metadata.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.
Appears in Collections:DECBI - Artigos publicados em periódicos

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