{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Madsen TD"],"funding":["Danmarks Grundforskningsfond","NNF Center for Basic Metabolic Research","Lundbeckfonden","Novo Nordisk Fonden","Lundbeck Foundation"],"pagination":["4033"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC7441158"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["11(1)"],"pubmed_abstract":["Peptide hormones and neuropeptides encompass a large class of bioactive peptides that regulate physiological processes like anxiety, blood glucose, appetite, inflammation and blood pressure. Here, we execute a focused discovery strategy to provide an extensive map of O-glycans on peptide hormones. We find that almost one third of the 279 classified peptide hormones carry O-glycans. Many of the identified O-glycosites are conserved and are predicted to serve roles in proprotein processing, receptor interaction, biodistribution and biostability. We demonstrate that O-glycans positioned within the receptor binding motifs of members of the neuropeptide Y and glucagon families modulate receptor activation properties and substantially extend peptide half-lives. Our study highlights the importanc"],"journal":["Nature communications"],"pubmed_title":["An atlas of O-linked glycosylation on peptide hormones reveals diverse biological roles."],"pmcid":["PMC7441158"],"funding_grant_id":["R249-2017-1095","NNF17OC0026030","NNF12OC1016060","Holst Group","DNRF107"],"pubmed_authors":["Schjoldager KT","Joshi HJ","Holst JJ","Hansen LH","Martin C","Goetze JP","Hintze J","Ye Z","Madsen TD","Andersen DB","Rosenkilde MM","Jebari S","Vakhrushev SY","Goth CK","Ju T","Kuhre RE"],"additional_accession":[]},"is_claimable":false,"name":"An atlas of O-linked glycosylation on peptide hormones reveals diverse biological roles.","description":"Peptide hormones and neuropeptides encompass a large class of bioactive peptides that regulate physiological processes like anxiety, blood glucose, appetite, inflammation and blood pressure. Here, we execute a focused discovery strategy to provide an extensive map of O-glycans on peptide hormones. We find that almost one third of the 279 classified peptide hormones carry O-glycans. Many of the identified O-glycosites are conserved and are predicted to serve roles in proprotein processing, receptor interaction, biodistribution and biostability. We demonstrate that O-glycans positioned within the receptor binding motifs of members of the neuropeptide Y and glucagon families modulate receptor activation properties and substantially extend peptide half-lives. Our study highlights the importanc","dates":{"release":"2020-01-01T00:00:00Z","publication":"2020 Aug","modification":"2026-04-16T23:16:03.427Z","creation":"2020-09-05T07:10:35Z"},"accession":"S-EPMC7441158","cross_references":{"pubmed":["32820167"],"doi":["10.1038/s41467-020-17473-1"]}}