Evidence map›Paper›PMID 19687473›Full record

ReviewThe journal of histochemistry and cytochemistry : official journal of the Histochemistry Society2009

Issues about the physiological functions of prolyl oligopeptidase based on its discordant spatial association with substrates and inconsistencies among mRNA, protein levels, and enzymatic activity.

Timo T Myöhänen, J Arturo García-Horsman, Jofre Tenorio-Laranga, Pekka T Männistö

Open access · greenAbstract readReview
In one paragraph

Review in The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
3.1field-weighted citation impact, top 8% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

27 citing papers in PubMed, 71 citations in OpenAlex.

  1. Identification of biallelic loss-of-functionJournal of medical genetics · 2026
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  18. Hypothalamic prolyl endopeptidase (PREP) regulates pancreatic insulin and glucagon secretion in mice.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  19. Article
  20. Distribution of prolyl oligopeptidase in human peripheral tissues and in ovarian and colorectal tumors.The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society · 2012
    Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors at 1 institution in 1 country.

Timo T MyöhänenDepartment of Pharmacology and Toxicology, University of Kuopio, PO Box 1627, FI-70211 Kuopio, Finland. Timo.Myohanen@uku.fi
J Arturo García-Horsman
Jofre Tenorio-Laranga
Pekka T Männistö
University of Eastern Finland · FI

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Prolyl oligopeptidase (POP) is a serine endopeptidase that hydrolyses proline-containing peptides shorter than 30 amino acids. POP may be associated with cognitive functions, possibly via the cleavage of neuropeptides. Recent studies have also suggested novel non-hydrolytic and non-catalytic functions for POP. Moreover, POP has also been proposed as a regulator of inositol 1,4,5-triphosphate signaling and several other functions such as cell proliferation and differentiation, as well as signal transduction in the central nervous system, and it is suspected to be involved in pathological conditions such as Parkinson's and Alzheimer's diseases and cancer. POP inhibitors have been developed to restore the depleted neuropeptide levels encountered in aging or in neurodegenerative disorders. These compounds have shown some antiamnesic effects in animal models. However, the mechanisms of these hypothesized actions are still far from clear. Moreover, the physiological role of POP has remained unknown, and a lack of basic studies, including its distribution, is obvious. The aim of this review is to gather information about POP and to propose some novel roles for this enzyme based on its distribution and its discordant spatial association with its best known substrates.

Indexed as

AnimalsBrainCatalysisCell DifferentiationCell ProliferationHumansMotor ActivityNeurotransmitter AgentsOrgan SpecificityProlyl OligopeptidasesRNA, MessengerSerine EndopeptidasesSignal TransductionSubstrate SpecificityNeurotransmitter AgentsPREPL protein, humanProlyl OligopeptidasesRNA, MessengerSerine Endopeptidases

Identifiers

PMID19687473
PMCPMC2728128
OpenAlexW2147131319

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.