An atlas of O-linked glycosylation on peptide hormones reveals diverse biological roles
dc.contributor.author | Madsen, Thomas D. | |
dc.contributor.author | Hansen, Lasse H. | |
dc.contributor.author | Hintze, John | |
dc.contributor.author | Ye, Zilu | |
dc.contributor.author | Jebari Benslaiman, Shifa | |
dc.contributor.author | Andersen, Daniel B. | |
dc.contributor.author | Joshi, Hiren J. | |
dc.contributor.author | Ju, Tongzhong | |
dc.contributor.author | Goetze, Jens P. | |
dc.contributor.author | Martin, Cesar | |
dc.contributor.author | Rosenkilde, Mette M. | |
dc.contributor.author | Holst, Jens J. | |
dc.contributor.author | Kuhre, Rune E. | |
dc.contributor.author | Goth, Christoffer K. | |
dc.contributor.author | Vakhrushev, Sergey Y. | |
dc.contributor.author | Schjoldager, Katrine T. | |
dc.date.accessioned | 2020-12-21T11:47:43Z | |
dc.date.available | 2020-12-21T11:47:43Z | |
dc.date.issued | 2020-08-20 | |
dc.identifier.citation | Nature Communications 11 : (2020) // Article ID 4033 | es_ES |
dc.identifier.issn | 2041-1723 | |
dc.identifier.uri | http://hdl.handle.net/10810/49183 | |
dc.description.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 importance of O-glycosylation in the biology of peptide hormones, and our map of O-glycosites in this large class of biomolecules serves as a discovery platform for an important class of molecules with potential opportunities for drug designs. O-glycosylation is an abundant post-translational modification but its relevance for bioactive peptides is unclear. Here, the authors detect O-glycans on almost one third of the classified peptide hormones and show that O-glycosylation can modulate peptide half-lives and receptor activation properties. | es_ES |
dc.description.sponsorship | This work was supported by the Novo Nordisk Foundation, the Lundbeck Foundation, Danish National Research Foundation Grant DNRF107. | es_ES |
dc.language.iso | eng | es_ES |
dc.publisher | Nature | es_ES |
dc.rights | info:eu-repo/semantics/openAccess | es_ES |
dc.rights.uri | http://creativecommons.org/licenses/by/3.0/es/ | * |
dc.subject | natriuretic peptide | es_ES |
dc.subject | polypeptide | es_ES |
dc.subject | enzyme | es_ES |
dc.subject | specificity | es_ES |
dc.subject | analogs | es_ES |
dc.subject | plasma | es_ES |
dc.subject | glycoproteins | es_ES |
dc.subject | secretion | es_ES |
dc.subject | discovery | es_ES |
dc.subject | mechanism | es_ES |
dc.title | An atlas of O-linked glycosylation on peptide hormones reveals diverse biological roles | es_ES |
dc.type | info:eu-repo/semantics/article | es_ES |
dc.rights.holder | This article is licensed under a Creative CommonsAttribution 4.0 International License, which permits use, sharing,adaptation, distribution and reproduction in any medium or format, as long as you giveappropriate credit to the original author(s) and the source, provide a link to the CreativeCommons license, and indicate if changes were made. The images or other third partymaterial in this article are included in the article’s Creative Commons license, unlessindicated otherwise in a credit line to the material. If material is not included in thearticle’s Creative Commons license and your intended use is not permitted by statutoryregulation or exceeds the permitted use, you will need to obtain permission directly fromthe copyright holder. To view a copy of this license, visithttp://creativecommons.org/licenses/by/4.0/. | es_ES |
dc.rights.holder | Atribución 3.0 España | * |
dc.relation.publisherversion | https://www.nature.com/articles/s41467-020-17473-1 | es_ES |
dc.identifier.doi | 10.1038/s41467-020-17473-1 | |
dc.departamentoes | Bioquímica y biología molecular | es_ES |
dc.departamentoeu | Biokimika eta biologia molekularra | es_ES |
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