Publication
Title
Interaction of prolyl oligopeptidase with -synuclein
Author
Abstract
Prolyl oligopeptidase (PO) interacts with α-synuclein in vitro. It is a weak interaction that induces a nucleation prone conformation of α-synuclein. PO accelerates aggregation and fibril formation of α-synuclein in a process that can be reversed by specific inhibitors and is also influenced by an impairing mutation in the PO active site. There is evidence that PO and α-synuclein also interact intracellularly, especially in conditions where the expression of α-synuclein is high. Specific PO inhibitors reduce the number of cells with α-synuclein inclusions in a cellular model of Parkinson's disease. If these interactions also exist in the human brain, PO may be a target for the treatment of Parkinson's disease and other synucleinopathies. Whether PO also contributes to the normal physiological functions of α-synuclein remains an open question, but there are some intriguing parallels between the proposed functions of both proteins that deserve further investigation.
Language
English
Source (journal)
CNS and neurological disorders drug targets
Publication
2011
ISSN
1871-5273
Volume/pages
10:3(2011), p. 349-354
ISI
000290613100010
Full text (open access)
UAntwerpen
Faculty/Department
Research group
[E?say:metaLocaldata.cgzprojectinf]
Oligopeptidase inhibitors in brain function and dysfunction: towards new therapeutic strategies for neuroprotection (NEUROPRO).
Investigation of prolyl oligopeptidase as a therapeutic target for neuropathological diseases: inhibitors, substrates and ligands.
Publication type
Subject
Affiliation
Publications with a UAntwerp address
External links
Web of Science
Record
Identification
Creation 22.06.2011
Last edited 06.08.2017
To cite this reference