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Article

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

by 1,†, 2,3,4,†, 2,5, 2,3,4, 2,6, 1 and 2,6,*
1
British Heart Foundation Centre of Research Excellence, School of Cardiovascular Medicine and Sciences, King’s College London, St Thomas’ Hospital, Westminster Bridge Road, London SE1 7EH, UK
2
Bioanalytical Mass Spectrometry Group, Max Planck Institute for Biophysical Chemistry, 37077 Goettingen, Germany
3
Hematology/Oncology, Department of Medicine II, Johann Wolfgang Goethe University, 60590 Frankfurt am Main, Germany
4
Frankfurt Cancer Institute, Johann Wolfgang Goethe University, 60590 Frankfurt am Main, Germany
5
Department of Biochemistry and Molecular Biology, Soochow University Medical College, Suzhou 215123, China
6
Department of Clinical Chemistry, University Medical Center Goettingen, 37075 Goettingen, Germany
*
Author to whom correspondence should be addressed.
Both authors contributed equally to this work.
Academic Editors: Maria Gonzalez Barderas and Fernando de la Cuesta
Int. J. Mol. Sci. 2021, 22(22), 12584; https://doi.org/10.3390/ijms222212584
Received: 1 September 2021 / Revised: 12 November 2021 / Accepted: 15 November 2021 / Published: 22 November 2021
(This article belongs to the Special Issue Molecular Mechanisms and Pathophysiology of Cardiovascular Disease)
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. View Full-Text
Keywords: phosphorylation; cell signalling; mass spectrometry; β-adrenergic receptor; SILAC phosphorylation; cell signalling; mass spectrometry; β-adrenergic receptor; SILAC
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MDPI and ACS Style

Güran, A.; Ji, Y.; Fang, P.; Pan, K.-T.; Urlaub, H.; Avkiran, M.; Lenz, C. Quantitative Analysis of the Cardiac Phosphoproteome in Response to Acute β-Adrenergic Receptor Stimulation In Vivo. Int. J. Mol. Sci. 2021, 22, 12584. https://doi.org/10.3390/ijms222212584

AMA Style

Güran A, Ji Y, Fang P, Pan K-T, Urlaub H, Avkiran M, Lenz C. Quantitative Analysis of the Cardiac Phosphoproteome in Response to Acute β-Adrenergic Receptor Stimulation In Vivo. International Journal of Molecular Sciences. 2021; 22(22):12584. https://doi.org/10.3390/ijms222212584

Chicago/Turabian Style

Güran, Alican, Yanlong Ji, Pan Fang, Kuan-Ting Pan, Henning Urlaub, Metin Avkiran, and Christof Lenz. 2021. "Quantitative Analysis of the Cardiac Phosphoproteome in Response to Acute β-Adrenergic Receptor Stimulation In Vivo" International Journal of Molecular Sciences 22, no. 22: 12584. https://doi.org/10.3390/ijms222212584

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