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Vol. 33, No. 1, 2011
Issue release date: April 2011
Section title: Original Paper
Dev Neurosci 2011;33:38–47
(DOI:10.1159/000322082)

Sequential Expression, Activity and Nuclear Localization of Prolyl Oligopeptidase Protein in the Developing Rat Brain

Hannula M.J. · Männistö P.T. · Myöhänen T.T.
Division of Pharmacology and Toxicology, University of Helsinki, Helsinki, Finland

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Article / Publication Details

First-Page Preview
Abstract of Original Paper

Received: 6/24/2010
Accepted: 10/14/2010
Published online: 12/14/2010

Number of Print Pages: 10
Number of Figures: 5
Number of Tables: 0

ISSN: 0378-5866 (Print)
eISSN: 1421-9859 (Online)

For additional information: http://www.karger.com/DNE

Abstract

Prolyl oligopeptidase (POP) is a serine protease that hydrolyzes peptides shorter than 30-mer. Some evidence has recently been obtained that POP can generate protein-protein interactions and therefore participate in various physiological and pathological events. Several studies have reported that POP may be involved in neurogenesis since its activity increases during development and can be found in the nucleus of proliferating tissues. In cell cultures, POP has been shown to be localized in the nucleus, but only early in the development, since during maturation it is moved to the cytosol. We have now studied for the first time the expression of POP protein, its enzymatic activity and nuclear localization in vivo in the developing rat brain. We observed that enzymatic activity of POP is highest on embryonic day 18 while the protein amounts reach their peak at birth. Furthermore, POP is located in the nucleus only early in the development but is transferred to the cytosol already before parturition. Our in vivo results confirm the previous cell culture results supporting the role of POP in neurogenesis. A discordance of antenatal protein amounts and enzymatic activities is suggesting a tight regulation of POP activity and possibly even a nonhydrolytic role at that stage.


Article / Publication Details

First-Page Preview
Abstract of Original Paper

Received: 6/24/2010
Accepted: 10/14/2010
Published online: 12/14/2010

Number of Print Pages: 10
Number of Figures: 5
Number of Tables: 0

ISSN: 0378-5866 (Print)
eISSN: 1421-9859 (Online)

For additional information: http://www.karger.com/DNE


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