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Dibasic cleavage site is required for sorting to the regulated secretory pathway for both pro- and neuropeptide Y.
- Source :
-
Journal of Neurochemistry . 6/15/2002, Vol. 81 Issue 6, p1166-1175. 10p. - Publication Year :
- 2002
-
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. [ABSTRACT FROM AUTHOR]
- Subjects :
- *NEUROPEPTIDE Y
*PROTEIN kinases
Subjects
Details
- Language :
- English
- ISSN :
- 00223042
- Volume :
- 81
- Issue :
- 6
- Database :
- Academic Search Index
- Journal :
- Journal of Neurochemistry
- Publication Type :
- Academic Journal
- Accession number :
- 6790199
- Full Text :
- https://doi.org/10.1046/j.1471-4159.2002.00919.x