Evidence map›Paper›PMID 37598269›Full record

ArticleCommunications biology2023

Non-glycosylated IGF2 prohormones are more mitogenic than native IGF2.

Pavlo Potalitsyn, Lucie Mrázková, Irena Selicharová, Michaela Tencerová, Michaela Ferenčáková, Martina Chrudinová, Tereza Turnovská, Andrzej Marek Brzozowski, Aleš Marek, Jakub Kaminský and 2 more

Open access · goldAbstract read
In one paragraph

Article in Communications biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
1.4field-weighted citation impact, top 17% 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

10 citing papers in PubMed, 7 citations in OpenAlex.

  1. Insulin-like growth factor receptor signaling in physiology and disease.Signal transduction and targeted therapy · 2026
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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

12 authors at 4 institutions in 2 countries.

Pavlo PotalitsynInstitute of Organic Chemistry and Biochemistry, Czech Academy of Sciences, Flemingovo nám. 2, 116 10, Prague 6, Czech Republic.ORCID http://orcid.org/0000-0002-4703-6559
Lucie MrázkováInstitute of Organic Chemistry and Biochemistry, Czech Academy of Sciences, Flemingovo nám. 2, 116 10, Prague 6, Czech Republic.
Irena SelicharováInstitute of Organic Chemistry and Biochemistry, Czech Academy of Sciences, Flemingovo nám. 2, 116 10, Prague 6, Czech Republic.
Michaela TencerováInstitute of Physiology, Czech Academy of Sciences, Vídeňská 1083, Prague 4, Czech Republic.ORCID http://orcid.org/0000-0001-8670-425X
Michaela FerenčákováInstitute of Physiology, Czech Academy of Sciences, Vídeňská 1083, Prague 4, Czech Republic.
Martina ChrudinováInstitute of Organic Chemistry and Biochemistry, Czech Academy of Sciences, Flemingovo nám. 2, 116 10, Prague 6, Czech Republic.
Tereza TurnovskáInstitute of Organic Chemistry and Biochemistry, Czech Academy of Sciences, Flemingovo nám. 2, 116 10, Prague 6, Czech Republic.
Andrzej Marek BrzozowskiYork Structural Biology Laboratory, Department of Chemistry, University of York, Heslington, York, YO10 5DD, UK.ORCID http://orcid.org/0000-0001-7426-8948
Aleš MarekInstitute of Organic Chemistry and Biochemistry, Czech Academy of Sciences, Flemingovo nám. 2, 116 10, Prague 6, Czech Republic.
Jakub KaminskýInstitute of Organic Chemistry and Biochemistry, Czech Academy of Sciences, Flemingovo nám. 2, 116 10, Prague 6, Czech Republic.
Jiří JiráčekInstitute of Organic Chemistry and Biochemistry, Czech Academy of Sciences, Flemingovo nám. 2, 116 10, Prague 6, Czech Republic. jiracek@uochb.cas.cz.ORCID http://orcid.org/0000-0003-3848-2773
Lenka ŽákováInstitute of Organic Chemistry and Biochemistry, Czech Academy of Sciences, Flemingovo nám. 2, 116 10, Prague 6, Czech Republic. zakova@uochb.cas.cz.ORCID http://orcid.org/0000-0001-6439-2574
Czech Academy of Sciences, Institute of Organic Chemistry and Biochemistry · CZCharles University · CZCzech Academy of Sciences · CZUniversity of York · GB

Funding

Biotechnology and Biological Sciences Research Council BB/W003783/1Medical Research Council MR/R009066/1
6 · The paper itself

Abstract

Insulin-like Growth Factor-2 (IGF2) is important for the regulation of human embryonic growth and development, and for adults' physiology. Incorrect processing of the IGF2 precursor, pro-IGF2(156), leads to the formation of two IGF2 proforms, big-IGF2(87) and big-IGF2(104). Unprocessed and mainly non-glycosylated IGF2 proforms are found at abnormally high levels in certain diseases, but their mode of action is still unclear. Here, we found that pro-IGF2(156) has the lowest ability to form its inactivating complexes with IGF-Binding Proteins and has higher proliferative properties in cells than IGF2 and other IGF prohormones. We also showed that big-IGF2(104) has a seven-fold higher binding affinity for the IGF2 receptor than IGF2, and that pro-IGF2(87) binds and activates specific receptors and stimulates cell growth similarly to the mature IGF2. The properties of these pro-IGF2 forms, especially of pro-IGF2(156) and big-IGF2(104), indicate them as hormones that may be associated with human diseases related to the accumulation of IGF-2 proforms in the circulation.

Indexed as

Insulin-Like Growth Factor IIIntercellular Signaling Peptides and ProteinsAdultCell CycleCell ProliferationHumansMitogensIGF2 protein, humanInsulin-Like Growth Factor IIIntercellular Signaling Peptides and ProteinsMitogens

Identifiers

PMID37598269
PMCPMC10439913
OpenAlexW4386001747

What OpenQuestion holds

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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.