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

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Proteome-wide profiling and mapping of post translational modifications in human hearts. / Bagwan, Navratan; El Ali, Henrik H.; Lundby, Alicia.

In: Scientific Reports, Vol. 11, No. 1, 2184, 2021.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Bagwan, N, El Ali, HH & Lundby, A 2021, 'Proteome-wide profiling and mapping of post translational modifications in human hearts', Scientific Reports, vol. 11, no. 1, 2184. https://doi.org/10.1038/s41598-021-81986-y

APA

Bagwan, N., El Ali, H. H., & Lundby, A. (2021). Proteome-wide profiling and mapping of post translational modifications in human hearts. Scientific Reports, 11(1), [2184]. https://doi.org/10.1038/s41598-021-81986-y

Vancouver

Bagwan N, El Ali HH, Lundby A. Proteome-wide profiling and mapping of post translational modifications in human hearts. Scientific Reports. 2021;11(1). 2184. https://doi.org/10.1038/s41598-021-81986-y

Author

Bagwan, Navratan ; El Ali, Henrik H. ; Lundby, Alicia. / Proteome-wide profiling and mapping of post translational modifications in human hearts. In: Scientific Reports. 2021 ; Vol. 11, No. 1.

Bibtex

@article{7b998291469642bcb763b83e2de6c60f,

title = "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 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.",

author = "Navratan Bagwan and {El Ali}, {Henrik H.} and Alicia Lundby",

note = "Publisher Copyright: {\textcopyright} 2021, The Author(s).",

year = "2021",

doi = "10.1038/s41598-021-81986-y",

language = "English",

volume = "11",

journal = "Scientific Reports",

issn = "2045-2322",

publisher = "nature publishing group",

number = "1",

}

RIS

TY - JOUR

T1 - Proteome-wide profiling and mapping of post translational modifications in human hearts

AU - Bagwan, Navratan

AU - El Ali, Henrik H.

AU - Lundby, Alicia

PY - 2021

Y1 - 2021

N2 - 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.

AB - 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.

U2 - 10.1038/s41598-021-81986-y

DO - 10.1038/s41598-021-81986-y

M3 - Journal article

C2 - 33500497

AN - SCOPUS:85099834575

VL - 11

JO - Scientific Reports

JF - Scientific Reports

SN - 2045-2322

IS - 1

M1 - 2184

ER -

ID: 274061187

Department of Biomedical Sciences