14-3-3 Epsilon modulates the stimulated secretion of endopeptidase 24.15 (2005)
- Authors:
- Autor USP: FERRO, EMER SUAVINHO - ICB
- Unidade: ICB
- Assunto: HISTOLOGIA
- Language: Português
- Abstract: Objetivo: Endopeptidase 24.15 (EC 3.4.24.15; ep24.15), a secreted protein involved in peptide metabolism, is unusual in that it does not contain a signal peptide sequence. In this work, we describe the physical interaction between ep24.15 and 14-3-3 epsilon, one isoform of the ubiquitous phosphoserine/threonine-scaffold proteins family that organizes cell signaling and is involved in exocytosis. Métodos e Resultados: The interaction between ep24.15 and 14-3-3 was analyzed both in vitro and in cell culture. In vitro, the physical interaction between ep24.15 and 14-3-3 increased following phosphorylation of ep24.15 at Ser 644 by protein kinase-A (PKA). The co-localization of ep24.15 and 14-3-3 was also increased by exposure of HEK293 cells to forskolin (10 SM). Overexpression of 14-3-3 epsilon in HEK293 cells almost doubled the secretion of ep24.15 stimulated by A23187 (7.5 SM) from 10% (1.4 ± 0.24 AFU/min/10 6 cells) to 19% (2.54 ± 0.24 AFU/min/10 6 cells) (p < 0.001) of the total intracellular enzyme activity. Treatment with forskolin had a synergistic effect on the A23187- stimulated secretion of ep24.15 that was totally blocked by the PKA inhibitor KT5720. The ep24.15 point mutation S644A reduced the co-localization of ep24.15 and 14-3-3 in stably transfected HEK293 cells. Conclusões: We have demonstrated that the interaction between ep24.15 and 14-3-3 has a critical role in regulating the stimulated secretion of ep24.15. We have also shown that theunconventional pathway of ep24.15 secretion shares more similarities than differences with that of signal peptidecontaining proteins. However, it remains to be determined how this enzyme crosses the plasma membrane without been located within secretory vesicles
- Imprenta:
- Publisher: Federação de Sociedades de Biologia Experimental
- Publisher place: Águas de Lindóia, São Paulo
- Date published: 2005
- Source:
- Título do periódico: Resumos
- Conference titles: Reunião Anual da Federação de Sociedades de Biologia Experimental, FeSBE
-
ABNT
CARREÑO, F. R. et al. 14-3-3 Epsilon modulates the stimulated secretion of endopeptidase 24.15. 2005, Anais.. Águas de Lindóia, São Paulo: Federação de Sociedades de Biologia Experimental, 2005. . Acesso em: 30 set. 2024. -
APA
Carreño, F. R., Goñi, C. N., Castro, L. M., & Ferro, E. S. (2005). 14-3-3 Epsilon modulates the stimulated secretion of endopeptidase 24.15. In Resumos. Águas de Lindóia, São Paulo: Federação de Sociedades de Biologia Experimental. -
NLM
Carreño FR, Goñi CN, Castro LM, Ferro ES. 14-3-3 Epsilon modulates the stimulated secretion of endopeptidase 24.15. Resumos. 2005 ;[citado 2024 set. 30 ] -
Vancouver
Carreño FR, Goñi CN, Castro LM, Ferro ES. 14-3-3 Epsilon modulates the stimulated secretion of endopeptidase 24.15. Resumos. 2005 ;[citado 2024 set. 30 ] - Secretion of metalloendopeptidase 24.15 (EC 3.4.24.15)
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