An atlas of O-linked glycosylation on peptide hormones reveals diverse biological roles

Research output: Contribution to journalJournal articlepeer-review

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An atlas of O-linked glycosylation on peptide hormones reveals diverse biological roles. / Madsen, Thomas D.; Hansen, Lasse H.; Hintze, John; Ye, Zilu; Jebari, Shifa; Andersen, Daniel B.; Joshi, Hiren J.; Ju, Tongzhong; Goetze, Jens P.; Martin, Cesar; Rosenkilde, Mette M.; Holst, Jens J.; Kuhre, Rune E.; Goth, Christoffer K.; Vakhrushev, Sergey Y.; Schjoldager, Katrine T.

In: Nature Communications, Vol. 11, No. 1, 4033, 2020.

Research output: Contribution to journalJournal articlepeer-review

Harvard

Madsen, TD, Hansen, LH, Hintze, J, Ye, Z, Jebari, S, Andersen, DB, Joshi, HJ, Ju, T, Goetze, JP, Martin, C, Rosenkilde, MM, Holst, JJ, Kuhre, RE, Goth, CK, Vakhrushev, SY & Schjoldager, KT 2020, 'An atlas of O-linked glycosylation on peptide hormones reveals diverse biological roles', Nature Communications, vol. 11, no. 1, 4033. https://doi.org/10.1038/s41467-020-17473-1

APA

Madsen, T. D., Hansen, L. H., Hintze, J., Ye, Z., Jebari, S., Andersen, D. B., Joshi, H. J., Ju, T., Goetze, J. P., Martin, C., Rosenkilde, M. M., Holst, J. J., Kuhre, R. E., Goth, C. K., Vakhrushev, S. Y., & Schjoldager, K. T. (2020). An atlas of O-linked glycosylation on peptide hormones reveals diverse biological roles. Nature Communications, 11(1), [4033]. https://doi.org/10.1038/s41467-020-17473-1

Vancouver

Madsen TD, Hansen LH, Hintze J, Ye Z, Jebari S, Andersen DB et al. An atlas of O-linked glycosylation on peptide hormones reveals diverse biological roles. Nature Communications. 2020;11(1). 4033. https://doi.org/10.1038/s41467-020-17473-1

Author

Madsen, Thomas D. ; Hansen, Lasse H. ; Hintze, John ; Ye, Zilu ; Jebari, Shifa ; Andersen, Daniel B. ; Joshi, Hiren J. ; Ju, Tongzhong ; Goetze, Jens P. ; Martin, Cesar ; Rosenkilde, Mette M. ; Holst, Jens J. ; Kuhre, Rune E. ; Goth, Christoffer K. ; Vakhrushev, Sergey Y. ; Schjoldager, Katrine T. / An atlas of O-linked glycosylation on peptide hormones reveals diverse biological roles. In: Nature Communications. 2020 ; Vol. 11, No. 1.

Bibtex

@article{cf43b936b3d544a298d87e609c9e197b,
title = "An atlas of O-linked glycosylation on peptide hormones reveals diverse biological roles",
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.",
author = "Madsen, {Thomas D.} and Hansen, {Lasse H.} and John Hintze and Zilu Ye and Shifa Jebari and Andersen, {Daniel B.} and Joshi, {Hiren J.} and Tongzhong Ju and Goetze, {Jens P.} and Cesar Martin and Rosenkilde, {Mette M.} and Holst, {Jens J.} and Kuhre, {Rune E.} and Goth, {Christoffer K.} and Vakhrushev, {Sergey Y.} and Schjoldager, {Katrine T.}",
year = "2020",
doi = "10.1038/s41467-020-17473-1",
language = "English",
volume = "11",
journal = "Nature Communications",
issn = "2041-1723",
publisher = "nature publishing group",
number = "1",

}

RIS

TY - JOUR

T1 - An atlas of O-linked glycosylation on peptide hormones reveals diverse biological roles

AU - Madsen, Thomas D.

AU - Hansen, Lasse H.

AU - Hintze, John

AU - Ye, Zilu

AU - Jebari, Shifa

AU - Andersen, Daniel B.

AU - Joshi, Hiren J.

AU - Ju, Tongzhong

AU - Goetze, Jens P.

AU - Martin, Cesar

AU - Rosenkilde, Mette M.

AU - Holst, Jens J.

AU - Kuhre, Rune E.

AU - Goth, Christoffer K.

AU - Vakhrushev, Sergey Y.

AU - Schjoldager, Katrine T.

PY - 2020

Y1 - 2020

N2 - 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.

AB - 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.

U2 - 10.1038/s41467-020-17473-1

DO - 10.1038/s41467-020-17473-1

M3 - Journal article

C2 - 32820167

AN - SCOPUS:85089678360

VL - 11

JO - Nature Communications

JF - Nature Communications

SN - 2041-1723

IS - 1

M1 - 4033

ER -

ID: 247688751