期刊
FEBS LETTERS
卷 586, 期 19, 页码 3287-3292出版社
WILEY
DOI: 10.1016/j.febslet.2012.07.002
关键词
Oligopeptidase; G-protein coupled receptor; siRNA; Intracellular peptide; Ubiquitinproteasome system
资金
- Brazilian National Research Council (CNPq) [559698/2009-7]
- University of Sao Paulo [2011.1.9333.1.3, NAPNA]
- CNPq
- Fundacao de Amparo a Pesquisa do Estado de Sao Paulo (FAPESP)
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.
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