Distribution of Immunoreactive Prolyl Oligopeptidase in Human and Rat Brain

Myöhänen, Timo T.; Venäläinen, Jarkko I.; Tupala, Erkki; Garcı́a-Horsman, J. Arturo; Miettinen, Reijo; Männistö, Pekka T.

doi:10.1007/s11064-007-9316-y

Cited by 54 publications

(55 citation statements)

References 39 publications

(72 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…In situ hybridization analysis showed labeling in the hippocampus (Fig. 1A) as previously reported (Bellemère et al 2004;Myöhänen et al 2007). Within the hippocampus, RNA labeling was observed in principal neurons of CA1, CA2, CA3 regions and dentate gyrus (Fig.…”

Section: Prep Localization In the Hippocampussupporting

confidence: 86%

Prolyl Endopeptidase-Deficient Mice Have Reduced Synaptic Spine Density in the CA1 Region of the Hippocampus, Impaired LTP, and Spatial Learning and Memory

D’Agostino

Kim²,

Liu³

et al. 2012

Cerebral Cortex

View full text Add to dashboard Cite

Prolyl endopeptidase (PREP) is a phylogenetically conserved serine protease and, in humans and rodents, is highly expressed in the brain. Several neuropeptides associated with learning and memory and neurodegenerative disorders have been proposed to be the substrates for PREP, suggesting a possible role for PREP in these processes. However, its physiological function remains elusive. Combining genetic, anatomical, electrophysiological, and behavioral approaches, we show that PREP genetrap mice have decreased synaptic spine density in the CA1 region of the hippocampus, reduced hippocampal long-term potentiation, impaired hippocampalmediated learning and memory, and reduced growth-associated protein-43 levels when compared with wild-type controls. These observations reveal a role for PREP in mediating hippocampal plasticity and spatial memory formation, with implications for its pharmacological manipulation in diseases related to cognitive impairment.

show abstract

Section: Prep Localization In the Hippocampussupporting

confidence: 86%

Prolyl Endopeptidase-Deficient Mice Have Reduced Synaptic Spine Density in the CA1 Region of the Hippocampus, Impaired LTP, and Spatial Learning and Memory

D’Agostino

Kim²,

Liu³

et al. 2012

Cerebral Cortex

View full text Add to dashboard Cite

show abstract

“…4c–5c) and moderate amounts in the thalamus (fig. 4b, 5b), similarly to the adult rat brain [36,38]. …”

Section: Resultsmentioning

confidence: 99%

“…The amounts of POP protein and the specificity of POP antibody in rat embryos was confirmed by Western blot analysis using anti-chicken POP antibody (dilution 1:5,000) as described in Myöhänen et al [34,36]. Standard SDS-PAGE, transfer and blocking techniques were used and rabbit anti-chicken IgY with horseradish peroxidase conjugate (dilution 1:20,000; product No.…”

Section: Methodsmentioning

confidence: 99%

See 1 more Smart Citation

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

Hannula¹,

Männistö²,

Myöhänen³

2010

Dev Neurosci

Self Cite

View full text Add to dashboard Cite

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.

show abstract

“…PREP-specific IgY was then purified by affinity chromatography using a HiTrap NHS column coupled with purified PREP as reported (Venäläinen et al 2002). Antibody specificity in human tissues has been characterized earlier by Myöhänen et al (2007).…”

Section: Preparation Of Polyclonal Prep Antibodymentioning

confidence: 99%

Distribution of Prolyl Oligopeptidase in Human Peripheral Tissues and in Ovarian and Colorectal Tumors

Myöhänen

Pyykkö

Männistö

et al. 2012

J Histochem Cytochem.

Self Cite

View full text Add to dashboard Cite

SummaryProlyl oligopeptidase (PREP) is a serine protease that hydrolyzes peptides shorter than 30-mer, and it has been connected with multiple physiological and pathological conditions. PREP has been mostly studied in the brain, but significant PREP activities have been measured in peripheral tissues. Moreover, increased PREP activities have been found in tumors. In this study, the authors studied the immunohistochemical distribution of PREP protein in human peripheral tissues and in ovarian and colorectal tumors. PREP was found to be widely distributed in human peripheral tissues and specifically in certain cells. The most intense PREP expression was seen in the testis, ovaries, liver, and some parts of the skin. At the cellular level, high PREP levels were seen as a rule in secreting epithelial cells and cells involved in reproduction. Increased PREP expression was seen in most of the tumors studied. PREP expression was higher in malignant than benign tumors, and in ovarian epithelial cancers, there was a trend for increased PREP staining with increased malignancy grade. Results suggest that PREP may be associated with secretory processes as well as in reproduction. A more abundant expression of PREP in malignant than benign tumors suggests that PREP may be associated with expansion and metastasis of tumors. (J Histochem Cytochem 60:706-715, 2012)

show abstract

Distribution of Immunoreactive Prolyl Oligopeptidase in Human and Rat Brain

Cited by 54 publications

References 39 publications

Prolyl Endopeptidase-Deficient Mice Have Reduced Synaptic Spine Density in the CA1 Region of the Hippocampus, Impaired LTP, and Spatial Learning and Memory

Prolyl Endopeptidase-Deficient Mice Have Reduced Synaptic Spine Density in the CA1 Region of the Hippocampus, Impaired LTP, and Spatial Learning and Memory

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

Distribution of Prolyl Oligopeptidase in Human Peripheral Tissues and in Ovarian and Colorectal Tumors

Contact Info

Product

Resources

About