Análise molecular da secreção não convencional da endo-oligopeptidase EC3.4.24.15 (EP24.15) / Molecular analysis of the unconventional endo-oligopeptidase EC3.4.24.15 (EP24.15) secretion.

AUTOR(ES)
DATA DE PUBLICAÇÃO

2009

RESUMO

Thimet oligopeptidase (EC3.4.24.15; EP24.15) was originally described as a neuropeptide-metabolising enzyme that lacks a typical signal-peptide sequence for entry into the secretory pathway and is secreted by cells via an unconventional and unknown mechanism. Here, we identify a novel calcium-dependent interaction between EP24.15 and calmodulin I (CaM) that is important for the stimulated, but not constitutive, secretion of EP24.15. Overexpression of CaM in HEK293 cells increase the stimulated secretion of EP24.15, which can be inhibited by the CaM inhibitor. The specific inhibition of PKA with reduced the A23187-stimulated secretion of EP24.15. Our data suggest that the interaction between EP24.15 and calmodulin is regulated within cells and is important for the stimulated secretion of EP24.15 from HEK293 cells. Surprising, the rats brain slices experiments showed that, physiological, EP24.15 has a constitutive secretion, although the A23187 and forskolin treatment are able to increase a little this enzyme secretion in these preparations.

ASSUNTO(S)

biological transport transport through the membrane transporte através da membrana cellular biology transporte biológico biology biologia celular biologia

ACESSO AO ARTIGO

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