Dibasic cleavage site is required for sorting to the regulated secretory pathway for both pro- and neuropeptide Y

Details

Serval ID
serval:BIB_B782CACE0D1D
Type
Article: article from journal or magazin.
Collection
Publications
Institution
Title
Dibasic cleavage site is required for sorting to the regulated secretory pathway for both pro- and neuropeptide Y
Journal
Journal of Neurochemistry
Author(s)
Brakch  N., Allemandou  F., Cavadas  C., Grouzmann  E., Brunner  H. R.
ISSN
0022-3042 (Print)
Publication state
Published
Issued date
06/2002
Volume
81
Number
6
Pages
1166-75
Notes
Journal Article
Research Support, Non-U.S. Gov't --- Old month value: Jun
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
Amino Acid Substitution Animals Cell Line Neuropeptide Y/*chemistry/genetics/*metabolism Peptide Hydrolases/metabolism Protein Precursors/*chemistry/genetics/*metabolism Protein Sorting Signals/genetics/*physiology Rats
Pubmed
Web of science
Open Access
Yes
Create date
28/01/2008 10:35
Last modification date
20/08/2019 15:25
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