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Title: Prolyl oligopeptidase stimulates the aggregation of alpha-synuclein
Authors: Brandt, Inger
GĂ©rard, Melanie
Sergeant, Kjell
Devreese, Bart
Baekelandt, Veerle
Augustyns, Koen
Scharpé, Simon
Engelborghs, Yves
Lambeir, Anne-Marie # ×
Issue Date: Sep-2008
Publisher: Elsevier
Series Title: Peptides vol:29 issue:9 pages:1472-1478
Abstract: Despite its thorough enzymological and biochemical characterization the exact function of prolyl oligopeptidase (PO, E.C. 3.4.21.26) remains unclear. The positive effect of PO inhibitors on learning and memory in animal models for amnesia, enzyme activity measurements in patient samples and (neuro)peptide degradation studies link the enzyme with neurodegenerative disorders. The brain protein alpha-synuclein currently attracts much attention because of its proposed role in the pathology of Parkinson's disease. A fundamental question concerns how the essentially disordered protein is transformed into the highly organized fibrils that are found in Lewy bodies, the hallmarks of Parkinson's disease. Using gel electrophoresis and MALDI TOF/TOF mass spectrometry we investigated the possibility of alpha-synuclein as a PO substrate. We found that in vitro incubation of the protein with PO did not result in truncation of full-length alpha-synuclein. Surprisingly, however, we found an acceleration of the aggregation process of alpha-synuclein using turbidity measurements that was reversed by specific inhibitors of PO enzymatic activity. If PO displays this activity also in vivo, PO inhibitors might have an effect on neurodegenerative disorders through a decrease in the aggregation of alpha-synuclein.
URI: 
ISSN: 0196-9781
Publication status: published
KU Leuven publication type: IT
Appears in Collections:Research Group for Neurobiology and Gene Therapy
Interdisciplinary Research Facility Life Sciences, Campus Kulak Kortrijk
Biochemistry, Molecular and Structural Biology Section
× corresponding author
# (joint) last author

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