An investigation into the origin of the biased agonism associated with the urotensin II receptor activation

The urotensin II receptor (UTR) has long been studied mainly for its involvement in the cardiovascular homeostasis both in health and disease state. Two endogenous ligands activate UTR, i.e. urotensin II (U‐II) and urotensin II‐related peptide (URP). Extensive expression of the two ligands uncovers...

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Published inJournal of peptide science Vol. 21; no. 5; pp. 392 - 399
Main Authors Brancaccio, Diego, Merlino, Francesco, Limatola, Antonio, Yousif, Ali Munaim, Gomez-Monterrey, Isabel, Campiglia, Pietro, Novellino, Ettore, Grieco, Paolo, Carotenuto, Alfonso
Format Journal Article
LanguageEnglish
Published England Blackwell Publishing Ltd 01.05.2015
Wiley Subscription Services, Inc
Subjects
Amino Acid Sequence
Animals
biased agonism
conformation by NMR
docking studies
Humans
Magnetic Resonance Spectroscopy
Models, Molecular
Molecular Docking Simulation
Peptide Hormones - agonists
Peptide Hormones - chemical synthesis
Peptide Hormones - chemistry
Peptide Hormones - metabolism
Peptides
Protein Conformation
Receptors, G-Protein-Coupled - chemistry
Receptors, G-Protein-Coupled - metabolism
Sodium Dodecyl Sulfate - chemistry
Structure-Activity Relationship
therapeutic peptide
urotensin II-related peptide
urotensin-II
Urotensins - agonists
Urotensins - chemistry
Urotensins - metabolism
conformation by NMR
docking studies
biased agonism
urotensin II-related peptide
urotensin-II
therapeutic peptide
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Abstract The urotensin II receptor (UTR) has long been studied mainly for its involvement in the cardiovascular homeostasis both in health and disease state. Two endogenous ligands activate UTR, i.e. urotensin II (U‐II) and urotensin II‐related peptide (URP). Extensive expression of the two ligands uncovers the diversified pathophysiological effects mediated by the urotensinergic system such as cardiovascular disorders, smooth muscle cell proliferation, renal disease, diabetes, and tumour growth. As newly reported, U‐II and URP have distinct effects on transcriptional activity, cell proliferation, and myocardial contractile activities supporting the idea that U‐II and URP interact with UTR in a distinct manner (biased agonism). To shed light on the origin of the divergent activities of the two endogenous ligands, we performed a conformational study on URP by solution NMR in sodium dodecyl sulfate micelle solution and compared the obtained NMR structure of URP with that of hU‐II previously determined. Finally, we undertook docking studies between URP, hU‐II, and an UT receptor model. Copyright © 2015 European Peptide Society and John Wiley & Sons, Ltd. The urotensin II receptor (UTR) has long been studied mainly for its involvement in the cardiovascular homeostosis. The endogenous ligands of UTR, U‐II, and URP can exert common as well as different actions (biased agonism). To shed light on the origin of the divergent activities of two endogenous ligands, we performed a conformational study on URP, compared the obtained NMR structure of URP with that of hU‐II previously determined, and undertook docking studies between URP, hU‐II, and a newly developed UT receptor model.
AbstractList The urotensin II receptor (UTR) has long been studied mainly for its involvement in the cardiovascular homeostasis both in health and disease state. Two endogenous ligands activate UTR, i.e. urotensin II (U-II) and urotensin II-related peptide (URP). Extensive expression of the two ligands uncovers the diversified pathophysiological effects mediated by the urotensinergic system such as cardiovascular disorders, smooth muscle cell proliferation, renal disease, diabetes, and tumour growth. As newly reported, U-II and URP have distinct effects on transcriptional activity, cell proliferation, and myocardial contractile activities supporting the idea that U-II and URP interact with UTR in a distinct manner (biased agonism). To shed light on the origin of the divergent activities of the two endogenous ligands, we performed a conformational study on URP by solution NMR in sodium dodecyl sulfate micelle solution and compared the obtained NMR structure of URP with that of hU-II previously determined. Finally, we undertook docking studies between URP, hU-II, and an UT receptor model. Copyright copyright 2015 European Peptide Society and John Wiley & Sons, Ltd. The urotensin II receptor (UTR) has long been studied mainly for its involvement in the cardiovascular homeostosis. The endogenous ligands of UTR, U-II, and URP can exert common as well as different actions (biased agonism). To shed light on the origin of the divergent activities of two endogenous ligands, we performed a conformational study on URP, compared the obtained NMR structure of URP with that of hU-II previously determined, and undertook docking studies between URP, hU-II, and a newly developed UT receptor model.
The urotensin II receptor (UTR) has long been studied mainly for its involvement in the cardiovascular homeostasis both in health and disease state. Two endogenous ligands activate UTR, i.e. urotensin II (U-II) and urotensin II-related peptide (URP). Extensive expression of the two ligands uncovers the diversified pathophysiological effects mediated by the urotensinergic system such as cardiovascular disorders, smooth muscle cell proliferation, renal disease, diabetes, and tumour growth. As newly reported, U-II and URP have distinct effects on transcriptional activity, cell proliferation, and myocardial contractile activities supporting the idea that U-II and URP interact with UTR in a distinct manner (biased agonism). To shed light on the origin of the divergent activities of the two endogenous ligands, we performed a conformational study on URP by solution NMR in sodium dodecyl sulfate micelle solution and compared the obtained NMR structure of URP with that of hU-II previously determined. Finally, we undertook docking studies between URP, hU-II, and an UT receptor model.
The urotensin II receptor (UTR) has long been studied mainly for its involvement in the cardiovascular homeostasis both in health and disease state. Two endogenous ligands activate UTR, i.e. urotensin II (U‐II) and urotensin II‐related peptide (URP). Extensive expression of the two ligands uncovers the diversified pathophysiological effects mediated by the urotensinergic system such as cardiovascular disorders, smooth muscle cell proliferation, renal disease, diabetes, and tumour growth. As newly reported, U‐II and URP have distinct effects on transcriptional activity, cell proliferation, and myocardial contractile activities supporting the idea that U‐II and URP interact with UTR in a distinct manner (biased agonism). To shed light on the origin of the divergent activities of the two endogenous ligands, we performed a conformational study on URP by solution NMR in sodium dodecyl sulfate micelle solution and compared the obtained NMR structure of URP with that of hU‐II previously determined. Finally, we undertook docking studies between URP, hU‐II, and an UT receptor model. Copyright © 2015 European Peptide Society and John Wiley & Sons, Ltd. The urotensin II receptor (UTR) has long been studied mainly for its involvement in the cardiovascular homeostosis. The endogenous ligands of UTR, U‐II, and URP can exert common as well as different actions (biased agonism). To shed light on the origin of the divergent activities of two endogenous ligands, we performed a conformational study on URP, compared the obtained NMR structure of URP with that of hU‐II previously determined, and undertook docking studies between URP, hU‐II, and a newly developed UT receptor model.
The urotensin II receptor (UTR) has long been studied mainly for its involvement in the cardiovascular homeostasis both in health and disease state. Two endogenous ligands activate UTR, i.e. urotensin II (U-II) and urotensin II-related peptide (URP). Extensive expression of the two ligands uncovers the diversified pathophysiological effects mediated by the urotensinergic system such as cardiovascular disorders, smooth muscle cell proliferation, renal disease, diabetes, and tumour growth. As newly reported, U-II and URP have distinct effects on transcriptional activity, cell proliferation, and myocardial contractile activities supporting the idea that U-II and URP interact with UTR in a distinct manner (biased agonism). To shed light on the origin of the divergent activities of the two endogenous ligands, we performed a conformational study on URP by solution NMR in sodium dodecyl sulfate micelle solution and compared the obtained NMR structure of URP with that of hU-II previously determined. Finally, we undertook docking studies between URP, hU-II, and an UT receptor model. Copyright © 2015 European Peptide Society and John Wiley & Sons, Ltd.
The urotensin II receptor (UTR) has long been studied mainly for its involvement in the cardiovascular homeostasis both in health and disease state. Two endogenous ligands activate UTR, i.e. urotensin II (U‐II) and urotensin II‐related peptide (URP). Extensive expression of the two ligands uncovers the diversified pathophysiological effects mediated by the urotensinergic system such as cardiovascular disorders, smooth muscle cell proliferation, renal disease, diabetes, and tumour growth. As newly reported, U‐II and URP have distinct effects on transcriptional activity, cell proliferation, and myocardial contractile activities supporting the idea that U‐II and URP interact with UTR in a distinct manner (biased agonism). To shed light on the origin of the divergent activities of the two endogenous ligands, we performed a conformational study on URP by solution NMR in sodium dodecyl sulfate micelle solution and compared the obtained NMR structure of URP with that of h U‐II previously determined. Finally, we undertook docking studies between URP, h U‐II, and an UT receptor model. Copyright © 2015 European Peptide Society and John Wiley & Sons, Ltd.
Author Brancaccio, Diego
Limatola, Antonio
Yousif, Ali Munaim
Carotenuto, Alfonso
Gomez-Monterrey, Isabel
Campiglia, Pietro
Merlino, Francesco
Novellino, Ettore
Grieco, Paolo
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  surname: Carotenuto
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Keywords conformation by NMR
docking studies
biased agonism
urotensin II-related peptide
urotensin-II
therapeutic peptide
Language English
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Snippet The urotensin II receptor (UTR) has long been studied mainly for its involvement in the cardiovascular homeostasis both in health and disease state. Two...
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SubjectTerms Amino Acid Sequence
Animals
biased agonism
conformation by NMR
docking studies
Humans
Magnetic Resonance Spectroscopy
Models, Molecular
Molecular Docking Simulation
Peptide Hormones - agonists
Peptide Hormones - chemical synthesis
Peptide Hormones - chemistry
Peptide Hormones - metabolism
Peptides
Protein Conformation
Receptors, G-Protein-Coupled - chemistry
Receptors, G-Protein-Coupled - metabolism
Sodium Dodecyl Sulfate - chemistry
Structure-Activity Relationship
therapeutic peptide
urotensin II-related peptide
urotensin-II
Urotensins - agonists
Urotensins - chemistry
Urotensins - metabolism
Title An investigation into the origin of the biased agonism associated with the urotensin II receptor activation
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https://onlinelibrary.wiley.com/doi/abs/10.1002%2Fpsc.2740
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https://search.proquest.com/docview/1680435545
Volume 21
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