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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2016
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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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Proline rich-peptides, Label-free shotgun
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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.