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

• Published in: Scientific reports Vol. 11; no. 1; p. 2184
• Main Authors: Bagwan, Navratan, El Ali, Henrik H., Lundby, Alicia
• Format: Journal Article
• Language: English
• Published: London Nature Publishing Group UK 26.01.2021; Nature Publishing Group; Nature Portfolio
• Subjects: 631/114/2784; 631/114/663; 631/1647/296; 631/337/458; 631/337/458/1275; 631/337/458/1524; 631/337/458/1648; 631/337/458/1733; 631/337/458/2133; 631/337/458/2288; 631/337/458/2386; 631/337/458/582; 631/337/475; 631/45/475; 631/92/611; Amino acids; Glycosylation; Heart; Humanities and Social Sciences; Kinases; Mass spectrometry; Mass spectroscopy; multidisciplinary; Phosphorylation; Proteins; Proteomes; Science; Science (multidisciplinary); Translation
• ISSN: 2045-2322; 2045-2322
• DOI: 10.1038/s41598-021-81986-y

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.