The final walk with preptin

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 knowle...

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Bibliographic Details
Published in:	PloS one Vol. 19; no. 9; p. e0309726
Main Authors:	Mrázková, Lucie, Lubos, Marta, Voldřich, Jan, Kužmová, Erika, Zrubecká, Denisa, Gwozdiaková, Petra, Buděšínský, Miloš, Asai, Seiya, Marek, Aleš, Pícha, Jan, Tencerová, Michaela, Ferenčáková, Michaela, Barrera, Glenda Alquicer, Kaminský, Jakub, Jiráček, Jiří, Žáková, Lenka
Format:	Journal Article
Language:	English
Published:	United States Public Library of Science 12-09-2024
Subjects:	Amino acids Analogs Analysis Animals Biochemistry Biological activity Biological effects Biology and Life Sciences Bone turnover Chromatography Diabetes Health aspects Humans Instrument industry Insulin Insulin - metabolism Insulin secretion Insulin-like growth factor II Insulin-Like Growth Factor II - metabolism Medicine and Health Sciences Mice Organic chemistry Penicillin Peptide Fragments - metabolism Peptides Physiological effects Physiology Polypeptides Protein Precursors - metabolism Rats Research and Analysis Methods Solvents Czech Republic United States Japan
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Summary:	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.
Bibliography:	ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 Competing Interests: The authors have declared that no competing interests exist.
ISSN:	1932-6203 1932-6203
DOI:	10.1371/journal.pone.0309726