Proteome-wide profiling and mapping of post translational modifications in human hearts

Abstract Post translational modifications (PTMs) are covalent modifications of proteins that can range from small chemical modifications to addition of entire proteins. PTMs contribute to regulation of protein function and thereby greatly increase the functional diversity of the proteome. In the hea...

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Autores principales: Navratan Bagwan, Henrik H. El Ali, Alicia Lundby
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Lenguaje:EN
Publicado: Nature Portfolio 2021
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Acceso en línea:https://doaj.org/article/a132d662f1604d1b8f12973716e6e4c7
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spelling oai:doaj.org-article:a132d662f1604d1b8f12973716e6e4c72021-12-02T10:48:03ZProteome-wide profiling and mapping of post translational modifications in human hearts10.1038/s41598-021-81986-y2045-2322https://doaj.org/article/a132d662f1604d1b8f12973716e6e4c72021-01-01T00:00:00Zhttps://doi.org/10.1038/s41598-021-81986-yhttps://doaj.org/toc/2045-2322Abstract Post translational modifications (PTMs) are covalent modifications of proteins that can range from small chemical modifications to addition of entire proteins. PTMs contribute to regulation of protein function and thereby greatly increase the functional diversity of the proteome. In the heart, a few well-studied PTMs, such as phosphorylation and glycosylation, are known to play essential roles for cardiac function. Yet, only a fraction of the ~ 300 known PTMs have been studied in a cardiac context. Here we investigated the proteome-wide map of PTMs present in human hearts by utilizing high-resolution mass spectrometry measurements and a suite of PTM identification algorithms. Our approach led to identification of more than 150 different PTMs across three of the chambers in human hearts. This finding underscores that decoration of cardiac proteins by PTMs is much more diverse than hitherto appreciated and provides insights in cardiac protein PTMs not yet studied. The results presented serve as a catalogue of which PTMs are present in human hearts and outlines the particular protein and the specific amino acid modified, and thereby provides a detail-rich resource for exploring protein modifications in human hearts beyond the most studied PTMs.Navratan BagwanHenrik H. El AliAlicia LundbyNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 11, Iss 1, Pp 1-10 (2021)
institution DOAJ
collection DOAJ
language EN
topic Medicine
R
Science
Q
spellingShingle Medicine
R
Science
Q
Navratan Bagwan
Henrik H. El Ali
Alicia Lundby
Proteome-wide profiling and mapping of post translational modifications in human hearts
description Abstract Post translational modifications (PTMs) are covalent modifications of proteins that can range from small chemical modifications to addition of entire proteins. PTMs contribute to regulation of protein function and thereby greatly increase the functional diversity of the proteome. In the heart, a few well-studied PTMs, such as phosphorylation and glycosylation, are known to play essential roles for cardiac function. Yet, only a fraction of the ~ 300 known PTMs have been studied in a cardiac context. Here we investigated the proteome-wide map of PTMs present in human hearts by utilizing high-resolution mass spectrometry measurements and a suite of PTM identification algorithms. Our approach led to identification of more than 150 different PTMs across three of the chambers in human hearts. This finding underscores that decoration of cardiac proteins by PTMs is much more diverse than hitherto appreciated and provides insights in cardiac protein PTMs not yet studied. The results presented serve as a catalogue of which PTMs are present in human hearts and outlines the particular protein and the specific amino acid modified, and thereby provides a detail-rich resource for exploring protein modifications in human hearts beyond the most studied PTMs.
format article
author Navratan Bagwan
Henrik H. El Ali
Alicia Lundby
author_facet Navratan Bagwan
Henrik H. El Ali
Alicia Lundby
author_sort Navratan Bagwan
title Proteome-wide profiling and mapping of post translational modifications in human hearts
title_short Proteome-wide profiling and mapping of post translational modifications in human hearts
title_full Proteome-wide profiling and mapping of post translational modifications in human hearts
title_fullStr Proteome-wide profiling and mapping of post translational modifications in human hearts
title_full_unstemmed Proteome-wide profiling and mapping of post translational modifications in human hearts
title_sort proteome-wide profiling and mapping of post translational modifications in human hearts
publisher Nature Portfolio
publishDate 2021
url https://doaj.org/article/a132d662f1604d1b8f12973716e6e4c7
work_keys_str_mv AT navratanbagwan proteomewideprofilingandmappingofposttranslationalmodificationsinhumanhearts
AT henrikhelali proteomewideprofilingandmappingofposttranslationalmodificationsinhumanhearts
AT alicialundby proteomewideprofilingandmappingofposttranslationalmodificationsinhumanhearts
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