Title
Interaction of prolyl oligopeptidase with <tex>$\alpha$</tex>-synuclein
Author
Faculty/Department
Faculty of Pharmaceutical, Biomedical and Veterinary Sciences. Pharmacy
Publication type
article
Publication
Subject
Pharmacology. Therapy
Source (journal)
CNS and neurological disorders drug targets
Volume/pages
10(2011) :3 , p. 349-354
ISSN
1871-5273
ISI
000290613100010
Carrier
E
Target language
English (eng)
Affiliation
University of Antwerp
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.
Full text (open access)
https://repository.uantwerpen.be/docman/irua/9aff25/1648.pdf
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