Quantitative Analysis of the Cardiac Phosphoproteome in Response to Acute β-Adrenergic Receptor Stimulation In Vivo

β-adrenergic receptor (β-AR) stimulation represents a major mechanism of modulating cardiac output. In spite of its fundamental importance, its molecular basis on the level of cell signalling has not been characterised in detail yet. We employed mass spectrometry-based proteome and phosphoproteome a...

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Autores principales:	Alican Güran, Yanlong Ji, Pan Fang, Kuan-Ting Pan, Henning Urlaub, Metin Avkiran, Christof Lenz
Formato:	article
Lenguaje:	EN
Publicado:	MDPI AG 2021
Materias:	phosphorylation cell signalling mass spectrometry β-adrenergic receptor SILAC Biology (General) QH301-705.5 Chemistry QD1-999
Acceso en línea:	https://doaj.org/article/b1c1a91be2a84b30b4b7f5302b692782
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spelling	oai:doaj.org-article:b1c1a91be2a84b30b4b7f5302b6927822021-11-25T17:58:10ZQuantitative Analysis of the Cardiac Phosphoproteome in Response to Acute β-Adrenergic Receptor Stimulation In Vivo10.3390/ijms2222125841422-00671661-6596https://doaj.org/article/b1c1a91be2a84b30b4b7f5302b6927822021-11-01T00:00:00Zhttps://www.mdpi.com/1422-0067/22/22/12584https://doaj.org/toc/1661-6596https://doaj.org/toc/1422-0067β-adrenergic receptor (β-AR) stimulation represents a major mechanism of modulating cardiac output. In spite of its fundamental importance, its molecular basis on the level of cell signalling has not been characterised in detail yet. We employed mass spectrometry-based proteome and phosphoproteome analysis using SuperSILAC (spike-in stable isotope labelling by amino acids in cell culture) standardization to generate a comprehensive map of acute phosphoproteome changes in mice upon administration of isoprenaline (ISO), a synthetic β-AR agonist that targets both β1-AR and β2-AR subtypes. Our data describe 8597 quantitated phosphopeptides corresponding to 10,164 known and novel phospho-events from 2975 proteins. In total, 197 of these phospho-events showed significantly altered phosphorylation, indicating an intricate signalling network activated in response to β-AR stimulation. In addition, we unexpectedly detected significant cardiac expression and ISO-induced fragmentation of junctophilin-1, a junctophilin isoform hitherto only thought to be expressed in skeletal muscle. Data are available via ProteomeXchange with identifier PXD025569.Alican GüranYanlong JiPan FangKuan-Ting PanHenning UrlaubMetin AvkiranChristof LenzMDPI AGarticlephosphorylationcell signallingmass spectrometryβ-adrenergic receptorSILACBiology (General)QH301-705.5ChemistryQD1-999ENInternational Journal of Molecular Sciences, Vol 22, Iss 12584, p 12584 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	phosphorylation cell signalling mass spectrometry β-adrenergic receptor SILAC Biology (General) QH301-705.5 Chemistry QD1-999
spellingShingle	phosphorylation cell signalling mass spectrometry β-adrenergic receptor SILAC Biology (General) QH301-705.5 Chemistry QD1-999 Alican Güran Yanlong Ji Pan Fang Kuan-Ting Pan Henning Urlaub Metin Avkiran Christof Lenz Quantitative Analysis of the Cardiac Phosphoproteome in Response to Acute β-Adrenergic Receptor Stimulation In Vivo
description	β-adrenergic receptor (β-AR) stimulation represents a major mechanism of modulating cardiac output. In spite of its fundamental importance, its molecular basis on the level of cell signalling has not been characterised in detail yet. We employed mass spectrometry-based proteome and phosphoproteome analysis using SuperSILAC (spike-in stable isotope labelling by amino acids in cell culture) standardization to generate a comprehensive map of acute phosphoproteome changes in mice upon administration of isoprenaline (ISO), a synthetic β-AR agonist that targets both β1-AR and β2-AR subtypes. Our data describe 8597 quantitated phosphopeptides corresponding to 10,164 known and novel phospho-events from 2975 proteins. In total, 197 of these phospho-events showed significantly altered phosphorylation, indicating an intricate signalling network activated in response to β-AR stimulation. In addition, we unexpectedly detected significant cardiac expression and ISO-induced fragmentation of junctophilin-1, a junctophilin isoform hitherto only thought to be expressed in skeletal muscle. Data are available via ProteomeXchange with identifier PXD025569.
format	article
author	Alican Güran Yanlong Ji Pan Fang Kuan-Ting Pan Henning Urlaub Metin Avkiran Christof Lenz
author_facet	Alican Güran Yanlong Ji Pan Fang Kuan-Ting Pan Henning Urlaub Metin Avkiran Christof Lenz
author_sort	Alican Güran
title	Quantitative Analysis of the Cardiac Phosphoproteome in Response to Acute β-Adrenergic Receptor Stimulation In Vivo
title_short	Quantitative Analysis of the Cardiac Phosphoproteome in Response to Acute β-Adrenergic Receptor Stimulation In Vivo
title_full	Quantitative Analysis of the Cardiac Phosphoproteome in Response to Acute β-Adrenergic Receptor Stimulation In Vivo
title_fullStr	Quantitative Analysis of the Cardiac Phosphoproteome in Response to Acute β-Adrenergic Receptor Stimulation In Vivo
title_full_unstemmed	Quantitative Analysis of the Cardiac Phosphoproteome in Response to Acute β-Adrenergic Receptor Stimulation In Vivo
title_sort	quantitative analysis of the cardiac phosphoproteome in response to acute β-adrenergic receptor stimulation in vivo
publisher	MDPI AG
publishDate	2021
url	https://doaj.org/article/b1c1a91be2a84b30b4b7f5302b692782
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Quantitative Analysis of the Cardiac Phosphoproteome in Response to Acute β-Adrenergic Receptor Stimulation In Vivo

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