Dibasic cleavage site is required for sorting to the regulated secretory pathway for both pro- and neuropeptide Y.
作者： Noureddine Brakch , Flore Allemandou , Claudia Cavadas , Eric Grouzmann , Hans R. Brunner
DOI: 10.1046/J.1471-4159.2002.00919.X
关键词:
摘要: To investigate the signals governing routing of biologically active peptides to regulated secretory pathway, we have expressed mutated and non-mutated proneuropeptide Y (ProNPY) in pituitary-derived AtT20 cells. The mutations were carried out on dibasic cleavage site or ProNPY C-terminal sequence. Targeting pathway was studied using protein kinase A (8-BrcAMP), C (phorbol myristate acetate) specific activators synthesis inhibitor cycloheximide, by pulse chase. analysis cells culture media indicated that: neuropeptide (NPY) differently secreted, whilst NPY exclusively secreted via regulatory pathway; constitutive-like pathways. secretion behaviour not Proteolytic efficiency-dependent. essential for cAMP-dependent may function as a retention signal.
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