Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/348957
Type: Artigo
Title: Natural intracellular peptides can modulate the interactions of mouse brain proteins and thimet oligopeptidase with 14‐3‐3ε and calmodulin
Author: Russo, Lilian C.
Asega, Amanda F.
Negraes, Priscilla D.
Cruz, Lilian
Gozzo, Fabio C.
Ulrich, Henning
Camargo, Antonio C. M.
Rioli, Vanessa
Abstract: Protein interactions are crucial for most cellular process. Thus, rationally designed peptides that act as competitive assembly inhibitors of protein interactions by mimicking specific, determined structural elements have been extensively used in clinical and basic research. Recently, mammalian cells have been shown to contain a large number of intracellular peptides of unknown function. Here, we investigate the role of several of these natural intracellular peptides as putative modulators of protein interactions that are related to Ca2+‐calmodulin (CaM) and 14‐3‐3ε, which are proteins that are related to the spatial organization of signal transduction within cells. At concentrations of 1–50 μM, most of the peptides that are investigated in this study modulate the interactions of CaM and 14‐3‐3ε with proteins from the mouse brain cytoplasm or recombinant thimet oligopeptidase (EP24.15) in vitro, as measured by surface plasmon resonance. One of these peptides (VFDVELL; VFD‐7) increases the cytosolic Ca2+ concentration in a dose‐dependent manner but only if introduced into HEK293 cells, which suggests a wide biological function of this peptide. Therefore, it is exciting to suggest that natural intracellular peptides are novel modulators of protein interactions and have biological functions within cells
Subject: Cálcio
Country: Alemanha
Editor: John Wiley & Sons
Rights: Fechado
Identifier DOI: 10.1002/pmic.201200032
Address: https://onlinelibrary.wiley.com/doi/full/10.1002/pmic.201200032
Date Issue: 2012
Appears in Collections:IQ - Artigos e Outros Documentos

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