Precision Profiling of the Cardiovascular Post-Translationally Modified Proteome: Where There Is a Will, There Is a Way
Open accessAbstract
There is an exponential increase in biological complexity as initial gene transcripts are spliced, translated into amino acid sequence, and post-translationally modified. Each protein can exist as multiple chemical or sequence-specific proteoforms, and each has the potential to be a critical mediator of a physiological or pathophysiological signaling cascade. Here, we provide an overview of how different proteoforms come about in biological systems and how they are most commonly measured using mass spectrometry-based proteomics and bioinformatics. Our goal is to present this information at a level accessible to every scientist interested in mass spectrometry and its application to proteome profiling. We will specifically discuss recent data linking various protein post-translational modifications to cardiovascular disease and conclude with a discussion for enablement and democratization of proteomics across the cardiovascular and scientific community. The aim is to inform and inspire the readership to explore a larger breadth of proteoform, particularity post-translational modifications, related to their particular areas of expertise in cardiovascular physiology.
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Over the decade, cardiovascular disease proteomics has broadened from identifying single canonical proteins to mapping proteoforms derived from combinations of alternative splicing, cleavage, and post-translational modifications.
“Over the decade, CVD proteomics has broadened from identifying single canonical proteins to mapping proteoforms derived from combinations of alternative splicing, cleavage, and PTMs33,83.”
From A high-stringency blueprint of the human proteome (2020) · cites this paper as [33]
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References 193 · Cited by 45
Research works printed but not linked: 12
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- Authors
- Fert-Bober, J., Murray, C. I., Parker, S. J., & Van Eyk, J. E.
- Affiliations
- From the Advanced Clinical BioSystems Research Institute, Smidt Heart Institute, Department of Medicine, Cedars Sinai Medical Center, Los Angeles, CA.
- Cedars-Sinai Medical Center (US)
- Venue
- Circulation Research
- Published
- 2018-04-27
- Volume
- 122
- Issue
- 9
- Pages
- 1221-1237
- ISSN
- 0009-7330 (ISSN-L)
- 1524-4571
- PMC
- PMC5963703
- OpenAlex
- W2799848176
- Cited by
- 45
- References
- 193
- Citations by year
- 2026: 3 · 2025: 3 · 2024: 7 · 2023: 5 · 2022: 5 · 2021: 8 · 2020: 6 · 2019: 5 · 2018: 3
- FWCI
- 0.69
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Circulation Research (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Heart, Lung, and Blood Institute (K99HL128787, R01HL111362)
- Topics
- Physical Sciences › Chemistry › Spectroscopy › Advanced Proteomics Techniques and Applications
- Physical Sciences › Chemistry › Spectroscopy › Mass Spectrometry Techniques and Applications
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Keywords
- post-translational modification, proteoforms, cardiovascular disease, mass spectrometry-based proteomics, bioinformatics
- MeSH terms
- Amino Acid Sequence, Cardiovascular Diseases, Cardiovascular System, Cardiovascular Physiological Phenomena, Chromatography, Liquid, Humans, Protein Processing, Post-Translational, Proteins, Proteome, Proteomics, Tandem Mass Spectrometry
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