Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/2029
Type: Artigo de periódico
Title: Inhibition of thimet oligopeptidase by siRNA alters specific intracellular peptides and potentiates isoproterenol signal transduction
Author: Russo, Lilian C.
Castro, Leandro M.
Gozzo, Fabio C.
Ferro, Emer S.
Abstract: Mammalian cells have a large number of intracellular peptides that are generated by extralysosomal proteases. In this study, the enzymatic activity of thimet oligopeptidase (EP24.15) was inhibited in human embryonic kidney (HEK) 293 cells using a specific siRNA sequence. The semi-quantitative intracellular peptidome analyses of siRNA-transfected HEK293 cells shows that the levels of specific intracellular peptides are either increased or decreased upon EP24.15 inhibition. Decreased expression of EP24.15 was sufficient to potentiate luciferase gene reporter activation by isoproterenol (1-10 mu M). The protein kinase A inhibitor KT5720 (1 mu M) reduced the positive effect of the EP24.15 siRNA on isoproterenol signaling. Thus, EP24.15 inhibition by siRNA modulates the levels of specific intracellular peptides and isoproterenol signal transduction. (C) 2012 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
Subject: Oligopeptidase
G-protein coupled receptor
siRNA
Intracellular peptide
Ubiquitinproteasome system
Editor: Elsevier
Citation: Febs Letters. Elsevier, v.586, n.19, p.3287-3292, 2012
Rights: fechado
Identifier DOI: 10.1016/j.febslet.2012.07.002
Date Issue: 2012
Appears in Collections:IQ - Artigos e Outros Documentos

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