Dibasic cleavage site is required for sorting to the regulated secretory pathway for both pro- and neuropeptide Y |
| |
Authors: | Brakch Noureddine Allemandou Flore Cavadas Claudia Grouzmann Eric Brunner Hans R |
| |
Institution: | Division of Hypertension and Vascular Medicine, University Hospital, Lausanne, Switzerland. noureddine.brakch@chuv.hospvd.ch |
| |
Abstract: | To investigate the signals governing routing of biologically active peptides to the 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 and or ProNPY C-terminal sequence. Targeting to the regulated secretory pathway was studied using protein kinase A (8-BrcAMP), protein kinase C (phorbol myristate acetate) specific activators and protein synthesis inhibitor cycloheximide, and by pulse chase. The analysis of expressed peptides in cells and culture media indicated that: neuropeptide Y (NPY) and ProNPY were differently secreted, whilst NPY was exclusively secreted via regulatory pathway; ProNPY was secreted via regulated and constitutive-like secretory pathways. ProNPY secretion behaviour was not Proteolytic cleavage efficiency-dependent. The dibasic cleavage was essential for ProNPY and NPY cAMP-dependent regulated secretion and may have function as a retention signal. |
| |
Keywords: | constitutive secretion dibasic cleavage site NPY proteolytic processing regulated secretion |
本文献已被 PubMed 等数据库收录! |