Evidence map›Paper›PMID 21436262›Full record

ArticleMolecular endocrinology (Baltimore, Md.)2011

Processing of proaugurin is required to suppress proliferation of tumor cell lines.

Akihiko Ozawa, Adam N Lick, Iris Lindberg

Open access · bronzeAbstract read
In one paragraph

Article in Molecular endocrinology (Baltimore, Md.), 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
1.7field-weighted citation impact, top 15% 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

28 citing papers in PubMed, 35 citations in OpenAlex.

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  13. The Orphan C2orf40 Gene is a Neuroimmune Factor in Alzheimer's Disease.JSM Alzheimer's disease and related dementia · 2016
    Article
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  17. Esophageal cancer-related gene-4 (ECRG4) interactions with the innate immunity receptor complex.Inflammation research : official journal of the European Histamine Research Society ... [et al.] · 2015
    Article
  18. Article
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  20. Overexpression of ECRG4 enhances chemosensitivity to 5-fluorouracil in the human gastric cancer SGC-7901 cell line.Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine · 2013
    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

3 authors at 1 institution in 1 country.

Akihiko OzawaDepartment of Anatomy and Neurobiology, University of Maryland-Baltimore, 20 Penn Street, Baltimore, Maryland 21201, USA.
Adam N Lick
Iris Lindberg
University of Maryland, Baltimore · US

Funding

Identification of Novel Peptide HormonesR21DK084481 · NIDDK · UNIVERSITY OF MARYLAND BALTIMORE · PI LINDBERG, IRIS · 2009 to 2010
$413k
NIDDK NIH HHS R21 DK084481
6 · The paper itself

Abstract

Augurin is a secretory molecule produced in pituitary, thyroid, and esophagus and implicated in a wide array of physiological processes, from ACTH release to tumor suppression. However, the specific proaugurin-derived peptides present in various cell types are not yet known. In order to shed light on the posttranslational modifications required for biological activity, we here describe the posttranslational processing of proaugurin in AtT-20 and Lovo cells and identify proaugurin-derived products generated by convertases. In vitro cleavage of proaugurin with proprotein convertases produced multiple peptides, including a major product with a mass of 9.7 kDa by mass spectrometry. Metabolic labeling of C-terminally tagged proaugurin in AtT-20 and AtT-20/PC2 cells resulted in a major 15-kDa tagged form on SDS-PAGE, which likely corresponds to the 9.7-kDa in vitro fragment, with the added tag, its linker, and posttranslational modification(s). The secretion of neither proaugurin nor this cleavage product was stimulated by forskolin, indicating its lack of storage in regulated secretory granules and lack of cleavage by PC2. Incubation of cells with the furin inhibitor nona-d-arginine resulted in impaired cleavage of proaugurin, whereas metalloprotease inhibitors did not affect proaugurin proteolysis. These data support the idea that proaugurin is cleaved by furin and secreted via the constitutive secretory pathway. Interestingly, proaugurin was sulfated during trafficking; sulfation was completely inhibited by brefeldin A. Proliferation assays with three different tumor cell lines demonstrated that only furin-cleaved proaugurin could suppress cell proliferation, suggesting that proteolytic cleavage is a posttranslational requirement for proaugurin to suppress cell proliferation.

Indexed as

Cell ProliferationDown-RegulationAmino Acid SequenceAnimalsCell Line, TumorFurinHumansMiceMolecular Sequence DataMolecular WeightNeoplasm ProteinsProprotein ConvertasesProtein PrecursorsProtein Processing, Post-TranslationalSecretory PathwaySpectrometry, Mass, Matrix-Assisted Laser Desorption-Ionizationesophageal cancer related gene 4 protein, mouseFurinFURIN protein, humanNeoplasm ProteinsProprotein ConvertasesProtein Precursors

Identifiers

PMID21436262
PMCPMC3082321
OpenAlexW2060908481

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.