Evidence map›Paper›PMID 24497914›Full record

ArticlePloS one2014

Endothelin-converting enzyme-1 (ECE-1) is post-transcriptionally regulated by alternative polyadenylation.

Alison R Whyteside, Anthony J Turner, Daniel W Lambert

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
1.0field-weighted citation impact, top 24% 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

6 citing papers in PubMed, 14 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Neuropeptide substance P and the immune response.Cellular and molecular life sciences : CMLS · 2016
    Review
  6. Endothelin.Pharmacological reviews · 2016
    Review
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

3 authors at 2 institutions in 1 country.

Alison R WhytesideInstitute of Molecular and Cellular Biology, University of Leeds, Leeds, United Kindom.
Anthony J TurnerInstitute of Molecular and Cellular Biology, University of Leeds, Leeds, United Kindom.
Daniel W LambertIntegrated Biosciences, School of Clinical Dentistry, University of Sheffield, Sheffield, United Kingdom ; CR-UK/YCR Sheffield Cancer Centre, University of Sheffield, Sheffield, United Kingdom.
University of Leeds · GBUniversity of Sheffield · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Endothelin-converting enzyme-1 (ECE-1) is the enzyme predominantly responsible for producing active endothelin-1 (ET-1), a mitogenic peptide implicated in the aetiology of a number of diseases, including cancer. Elevated levels of ECE-1 have been observed in a range of malignancies, with high expression conferring poor prognosis and aiding the acquisition of androgen independence in prostate cancer. The mechanisms regulating the expression of ECE-1 in cancer cells are poorly understood, hampering the development of novel therapies targeting the endothelin axis. Here we provide evidence that the expression of ECE-1 is markedly inhibited by its 3'UTR, and that alternative polyadenylation (APA) results in the production of ECE-1 transcripts with truncated 3'UTRs which promote elevated protein expression. Abolition of the ECE-1 APA sites reduced protein expression from a reporter vector in prostate cancer cells, suggesting these sites are functional. This is the first study to identify ECE-1 as a target for APA, a regulatory mechanism aberrantly activated in cancer cells, and provides novel information about the mechanisms leading to ECE-1 overexpression in malignant cells.

Indexed as

Alternative SplicingRNA Processing, Post-Transcriptional3' Untranslated RegionsAnimalsAspartic Acid EndopeptidasesBase SequenceCell LineCell Line, TumorCHO CellsCricetinaeCricetulusEndothelin-Converting EnzymesHumansImmunoblottingLuciferasesMale3' Untranslated RegionsAspartic Acid EndopeptidasesECE1 protein, humanEndothelin-Converting EnzymesLuciferasesMetalloendopeptidasesPoly ARNA Splice Sites

Identifiers

PMID24497914
PMCPMC3908869
OpenAlexW2095290832

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.