Proteolysis and peptidases (2004)
- Author:
- USP affiliated author: FERRO, EMER SUAVINHO - ICB
- School: ICB
- Subject: HISTOLOGIA
- Language: Inglês
- Abstract: Extralysosomal proteolysis by multicatalytic complexes such as the 26S proteasome produces large amounts of peptides in the cytosol, mitochondria and nuclei of eukaryotic cells, and there is increasing evidence that the resulting free intracellular peptides can modulate specific protein interactions. The demonstration that free peptides added to the intracellular milieu can regulate cellular functions mediated by protein interactions suggests new putative roles for these molecules in gene regulation, metabolism, cell signaling and protein targeting. Such interactions frequently involve specific consensus amino acid sequences that can be predicted based on similarities in domain composition. We have recently developed a new strategy for identifying novel natural peptides, the sequences of which correspond to fragments of intracellular proteins and contain putative post-translational modification sites. In this presentation, we show evidences that intracellular peptides released by proteasomes may be involved in regulating protein interactions. In particular, the cell biology of endopeptidase 24.15 (thimet oligopeptidase; EC 3.4.24.15) will be discussed in detail since this enzyme has been implicated in both extracellular and intracellular peptide metabolism
- Imprenta:
- Source:
- Título do periódico: Abstracts
- Conference title: Congress of the Brazilian Society for Cell Biology
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ABNT
FERRO, Emer Suavinho. Proteolysis and peptidases. 2004, Anais.. Campinas: Instituto de Ciências Biomédicas, Universidade de São Paulo, 2004. . Acesso em: 29 jun. 2022. -
APA
Ferro, E. S. (2004). Proteolysis and peptidases. In Abstracts. Campinas: Instituto de Ciências Biomédicas, Universidade de São Paulo. -
NLM
Ferro ES. Proteolysis and peptidases. Abstracts. 2004 ;[citado 2022 jun. 29 ] -
Vancouver
Ferro ES. Proteolysis and peptidases. Abstracts. 2004 ;[citado 2022 jun. 29 ] - Hypotensive action of hemopressin, an endogenous peptide substrate of metalloendopeptidase 24.15
- A structure-based site-directed mutagenesis study on the neurolysin (EC 3.4.24.16.) and thimet oligopeptidase (EC3.4.24.15) catalysis
- Novos mecanismos de secreção e associação extracelular de proteínas: implicações no metabolismo celular de peptídeos
- 14.3.3 plays important role on endopeptidase 24.15 (EC 3.4.24.25) secretion
- Produção de retrovírus recombinantes para o silenciamento da oligopeptidase EP24.15
- Identification of endogenous substrates of thimet oligopeptidase (EC 3.4.24.15) in human embryonic kidney cells
- Vôos de fênix [Depoimento a Carlos Fioravanti]: fragmento de proteína ligado ao controle da pressão arterial pode ajudar a emagrecer e a tratar dependência química
- Analysis of intracellular peptidic content in beta 2 microglobulin/TAP1 knockout mice by mass spectrometry
- Hemopressin induces antinociception in an experimental model of neuropathic pain
- New approaches for G-protein coupled receptor ligands identification
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