Evidence map›Paper›PMID 24454770›Full record

ArticlePloS one2014

Furin is the major proprotein convertase required for KISS1-to-Kisspeptin processing.

Sitaram Harihar, Keke M Pounds, Tomoo Iwakuma, Nabil G Seidah, Danny R Welch

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 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.1field-weighted citation impact, top 23% 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

14 citing papers in PubMed, 23 citations in OpenAlex.

  1. KISS1 and Kisspeptins Detection in Cell Lines.Methods in molecular biology (Clifton, N.J.) · 2024
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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

5 authors at 3 institutions in 2 countries.

Sitaram HariharDepartment of Cancer Biology, The University of Kansas Medical Center, Kansas City, Kansas, United States of America.
Keke M PoundsDepartment of Cancer Biology, The University of Kansas Medical Center, Kansas City, Kansas, United States of America ; Department of Molecular Physiology, The University of Kansas Medical Center, Kansas City, Kansas, United States of America.
Tomoo IwakumaDepartment of Cancer Biology, The University of Kansas Medical Center, Kansas City, Kansas, United States of America ; The University of Kansas Cancer Center, The University of Kansas Medical Center, Kansas City, Kansas, United States of America ; Department of Molecular Physiology, The University of Kansas Medical Center, Kansas City, Kansas, United States of America.
Nabil G SeidahClinical Research Institute of Montreal, affiliated to Université de Montréal, Montréal, Québec, Canada.
Danny R WelchDepartment of Cancer Biology, The University of Kansas Medical Center, Kansas City, Kansas, United States of America ; The University of Kansas Cancer Center, The University of Kansas Medical Center, Kansas City, Kansas, United States of America ; Department of Molecular Physiology, The University of Kansas Medical Center, Kansas City, Kansas, United States of America ; Department of Pathology and Laboratory Medicine, The University of Kansas Medical Center, Kansas City, Kansas, United States of America.
The University of Kansas Cancer Center · USUniversity of Kansas Medical Center · USUniversité de Montréal · CA

Funding

Transgenic & Gene-Targeting Shared ResourceP30CA168524 · NCI · UNIVERSITY OF KANSAS MEDICAL CENTER · PI NICOLE L NOLLEN · 2012 to 2026
$40.1M
KISS1: Defining Mechanisms for Antimetastatic TherapyR01CA134981 · NCI · UNIVERSITY OF KANSAS MEDICAL CENTER · PI WELCH, DANNY R. · 2009 to 2014
$1.5M
NCI NIH HHS P30 CA168524NCI NIH HHS P30-CA168524NCI NIH HHS R01 CA134981NCI NIH HHS R01-CA134981
6 · The paper itself

Abstract

KISS1 is a broadly functional secreted proprotein that is then processed into small peptides, termed kisspeptins (KP). Since sequence analysis showed cleavage at KR or RR dibasic sites of the nascent protein, it was hypothesized that enzyme(s) belonging to the proprotein convertase family of proteases process KISS1 to generate KP. To this end, cell lines over-expressing KISS1 were treated with the proprotein convertase inhibitors, Dec-RVKR-CMK and α1-PDX, and KISS1 processing was completely inhibited. To identify the specific enzyme(s) responsible for KISS1 processing, mRNA expression was systematically analyzed for six proprotein convertases found in secretory pathways. Consistent expression of the three proteases - furin, PCSK5 and PCSK7 - were potentially implicated in KISS1 processing. However, shRNA-mediated knockdown of furin - but not PCSK5 or PCSK7 - blocked KISS1 processing. Thus, furin appears to be the essential enzyme for the generation of kisspeptins.

Indexed as

Protein Processing, Post-TranslationalCell Line, TumorFurinHumansKisspeptinsMutationNeoplasm MetastasisFurinKISS1 protein, humanKisspeptins

Identifiers

PMID24454770
PMCPMC3890299
OpenAlexW1993619070

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.