{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Belavgeni A"],"funding":["Deutsche Forschungsgemeinschaft"],"pagination":["e2300320120"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC10214148"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["120(21)"],"pubmed_abstract":["Iridoviridae, such as the lymphocystis disease virus-1 (LCDV-1) and other viruses, encode viral insulin-like peptides (VILPs) which are capable of triggering insulin receptors (IRs) and insulin-like growth factor receptors. The homology of VILPs includes highly conserved disulfide bridges. However, the binding affinities to IRs were reported to be 200- to 500-fold less effective compared to the endogenous ligands. We therefore speculated that these peptides also have noninsulin functions. Here, we report that the LCDV-1 VILP can function as a potent and highly specific inhibitor of ferroptosis. Induction of cell death by the ferroptosis inducers erastin, RSL3, FIN56, and FINO2 and nonferroptotic necrosis produced by the thioredoxin-reductase inhibitor ferroptocide were potently prevented b"],"journal":["Proceedings of the National Academy of Sciences of the United States of America"],"pubmed_title":["vPIF-1 is an insulin-like antiferroptotic viral peptide."],"pmcid":["PMC10214148"],"funding_grant_id":["460938556","503200509","314061271"],"pubmed_authors":["Tonnus W","Gavali S","Bornstein SR","Sha W","Flade K","Maremonti F","Beer K","Gembardt F","Hugo C","Giacca M","Linkermann A","Stadtmuller M","Becker JN","Hale BG","Stumpf J","Schally AV","Mallais M","Tmava M","Perakakis N","Pratt DA","Belavgeni A","Brucker A"],"additional_accession":[]},"is_claimable":false,"name":"vPIF-1 is an insulin-like antiferroptotic viral peptide.","description":"Iridoviridae, such as the lymphocystis disease virus-1 (LCDV-1) and other viruses, encode viral insulin-like peptides (VILPs) which are capable of triggering insulin receptors (IRs) and insulin-like growth factor receptors. The homology of VILPs includes highly conserved disulfide bridges. However, the binding affinities to IRs were reported to be 200- to 500-fold less effective compared to the endogenous ligands. We therefore speculated that these peptides also have noninsulin functions. Here, we report that the LCDV-1 VILP can function as a potent and highly specific inhibitor of ferroptosis. Induction of cell death by the ferroptosis inducers erastin, RSL3, FIN56, and FINO2 and nonferroptotic necrosis produced by the thioredoxin-reductase inhibitor ferroptocide were potently prevented b","dates":{"release":"2023-01-01T00:00:00Z","publication":"2023 May","modification":"2025-04-05T08:50:48.975Z","creation":"2025-04-05T08:50:48.975Z"},"accession":"S-EPMC10214148","cross_references":{"pubmed":["37186845"],"doi":["10.1073/pnas.2300320120"]}}