{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Subbotina E"],"funding":["HHS | National Institutes of Health","BLRD VA","NIDDK NIH HHS","NHLBI NIH HHS","Fraternal Order of Eagles","U.S. Department of Veterans Affairs"],"pagination":["16042-7"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC4702977"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["112(52)"],"pubmed_abstract":["Exercise remains the most effective way to promote physical and metabolic wellbeing, but molecular mechanisms underlying exercise tolerance and its plasticity are only partially understood. In this study we identify musclin-a peptide with high homology to natriuretic peptides (NP)-as an exercise-responsive myokine that acts to enhance exercise capacity in mice. We use human primary myoblast culture and in vivo murine models to establish that the activity-related production of musclin is driven by Ca(2+)-dependent activation of Akt1 and the release of musclin-encoding gene (Ostn) transcription from forkhead box O1 transcription factor inhibition. Disruption of Ostn and elimination of musclin secretion in mice results in reduced exercise tolerance that can be rescued by treatment with recomb"],"journal":["Proceedings of the National Academy of Sciences of the United States of America"],"pubmed_title":["Musclin is an activity-stimulated myokine that enhances physical endurance."],"pmcid":["PMC4702977"],"funding_grant_id":["Pilot Grant","I01 BX000718","K08 HL093368","R01 HL113089","HL113089","DK092412","R01 DK092412","HL093368","1I0BX000718"],"pubmed_authors":["Perez-Terzic CM","Zhu Z","Walsh SA","Sierra A","Reyes S","Subbotina E","Koganti SR","Hodgson-Zingman DM","Acevedo MR","Zingman LV","Gao Z","Stepniak E"],"additional_accession":[]},"is_claimable":false,"name":"Musclin is an activity-stimulated myokine that enhances physical endurance.","description":"Exercise remains the most effective way to promote physical and metabolic wellbeing, but molecular mechanisms underlying exercise tolerance and its plasticity are only partially understood. In this study we identify musclin-a peptide with high homology to natriuretic peptides (NP)-as an exercise-responsive myokine that acts to enhance exercise capacity in mice. We use human primary myoblast culture and in vivo murine models to establish that the activity-related production of musclin is driven by Ca(2+)-dependent activation of Akt1 and the release of musclin-encoding gene (Ostn) transcription from forkhead box O1 transcription factor inhibition. Disruption of Ostn and elimination of musclin secretion in mice results in reduced exercise tolerance that can be rescued by treatment with recomb","dates":{"release":"2015-01-01T00:00:00Z","publication":"2015 Dec","modification":"2025-04-19T16:59:08.258Z","creation":"2019-06-06T15:16:10Z"},"accession":"S-EPMC4702977","cross_references":{"pubmed":["26668395"],"doi":["10.1073/pnas.1514250112"]}}