Evidence map›Paper›PMID 39264940›Full record

ArticlePloS one2024

The final walk with preptin.

Lucie Mrázková, Marta Lubos, Jan Voldřich, Erika Kužmová, Denisa Zrubecká, Petra Gwozdiaková, Miloš Buděšínský, Seiya Asai, Aleš Marek, Jan Pícha and 6 more

Abstract read
In one paragraph

Article in PloS one, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

16 authors.

Lucie MrázkováInstitute of Organic Chemistry and Biochemistry of the Czech Academy of Sciences, Prague, Czech Republic.
Marta LubosInstitute of Organic Chemistry and Biochemistry of the Czech Academy of Sciences, Prague, Czech Republic.
Jan VoldřichInstitute of Organic Chemistry and Biochemistry of the Czech Academy of Sciences, Prague, Czech Republic.
Erika KužmováInstitute of Organic Chemistry and Biochemistry of the Czech Academy of Sciences, Prague, Czech Republic.
Denisa ZrubeckáInstitute of Organic Chemistry and Biochemistry of the Czech Academy of Sciences, Prague, Czech Republic.
Petra GwozdiakováInstitute of Organic Chemistry and Biochemistry of the Czech Academy of Sciences, Prague, Czech Republic.
Miloš BuděšínskýInstitute of Organic Chemistry and Biochemistry of the Czech Academy of Sciences, Prague, Czech Republic.
Seiya AsaiInstitute of Organic Chemistry and Biochemistry of the Czech Academy of Sciences, Prague, Czech Republic.
Aleš MarekInstitute of Organic Chemistry and Biochemistry of the Czech Academy of Sciences, Prague, Czech Republic.
Jan PíchaInstitute of Organic Chemistry and Biochemistry of the Czech Academy of Sciences, Prague, Czech Republic.
Michaela TencerováInstitute of Physiology of the Czech Academy of Sciences, Prague, Czech Republic.
Michaela FerenčákováInstitute of Physiology of the Czech Academy of Sciences, Prague, Czech Republic.
Glenda Alquicer BarreraInstitute of Physiology of the Czech Academy of Sciences, Prague, Czech Republic.
Jakub KaminskýInstitute of Organic Chemistry and Biochemistry of the Czech Academy of Sciences, Prague, Czech Republic.
Jiří JiráčekInstitute of Organic Chemistry and Biochemistry of the Czech Academy of Sciences, Prague, Czech Republic.
Lenka ŽákováInstitute of Organic Chemistry and Biochemistry of the Czech Academy of Sciences, Prague, Czech Republic.ORCID 0000-0001-6439-2574

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Preptin, a 34-amino acid peptide derived from pro-IGF2, is believed to influence various physiological processes, including insulin secretion and the regulation of bone metabolism. Despite its recognized involvement, the precise physiological role of preptin remains enigmatic. To address this knowledge gap, we synthesized 16 analogs of preptin, spanning a spectrum from full-length forms to fragments, and conducted comprehensive comparative activity evaluations alongside native human, mouse and rat preptin. Our study aimed to elucidate the physiological role of preptin. Contrary to previous indications of broad biological activity, our thorough analyses across diverse cell types revealed no significant biological activity associated with preptin or its analogs. This suggests that the associations of preptin with various diseases or tissue-specific abundance fluctuations may be influenced by factors beyond preptin itself, such as higher levels of IGF2 or IGF2 proforms present in tissues. In conclusion, our findings challenge the conventional notion of preptin as an isolated biologically active molecule and underscore the complexity of its interactions within biological systems. Rather than acting independently, the observed effects of preptin may arise from experimental conditions, elevated preptin concentrations, or interactions with related molecules such as IGF2.

Indexed as

Insulin-Like Growth Factor IIAnimalsHumansInsulinMicePeptide FragmentsProtein PrecursorsRatsIGF2 protein, humanInsulinInsulin-Like Growth Factor IIPeptide FragmentspreptinProtein Precursors

Identifiers

PMID39264940
PMCPMC11392399

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Registered trials

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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.