The continuing evolution of cardiac troponin I biomarker analysis: from protein to proteoform
Open accessAbstract
INTRODUCTION: The troponin complex consists of three proteins that fundamentally couple excitation with contraction. Circulating cardiac-specific Troponin I (cTnI) serves as diagnostic biomarker tools for risk stratification of acute coronary syndromes and acute myocardial infarction (MI). Within the heart, cTnI oscillates between inactive and active conformations to either block or disinhibit actinomyosin formation. This molecular mechanism is fine-tuned through extensive protein modifications whose profiles are maladaptively altered with co-morbidities including hypertrophic cardiomyopathy, diabetes, and heart failure. Technological advances in analytical platforms over the last decade enable routine baseline cTnI analysis in patients without cardiovascular complications, and hold potential to expand cTnI readouts that include modified cTnI proteoforms. Areas covered: This review covers the current state, advances, and prospects of analytical platforms that now enable routine baseline cTnI analysis in patients. In parallel, improved mass spectrometry instrumentation and workflows already reveal an array of modified cTnI proteoforms with promising diagnostic implications. Expert commentary: New analytical capabilities provide clinicians and researchers with an opportunity to address important questions surrounding circulating cTnI in the improved diagnosis of specific patient cohorts. These techniques also hold considerable promise for new predictive and prescriptive applications for individualized profiling and improve patient care.
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Circulating cTnI released into the blood after myocardial infarction is a known cardiac protein biomarker.
“circulating cTnI released into the blood upon myocardial infarction is a known cardiac protein biomarker [144–146].”
From Top-down proteomics: challenges, innovations, and applications in basic and clinical research (2020) · cites this paper as [145]
cTnI proteoforms arising from various PTMs can provide new insights to the molecular mechanisms underlying cardiovascular diseases.
“Recent studies have shown that cTnI is heavily modified and its proteoforms arising from various PTMs can provide new insights to the molecular mechanisms underlying cardiovascular diseases27–31.”
From Nanoproteomics enables proteoform-resolved analysis of low-abundance proteins in human serum (2020) · cites this paper as [27]
The PTM profiles of cTnI can function as molecular fingerprints of cellular signaling pathway activity with the potential to serve as next-generation biomarkers.
“The PTM profiles of cTnI can function as molecular fingerprints of cellular signaling pathway activity with the potential to serve as the next-generation biomarkers27,32,33.”
From Nanoproteomics enables proteoform-resolved analysis of low-abundance proteins in human serum (2020) · cites this paper as [27]
ppcTnI was the predominant cTnI proteoform in the non-diseased donor heart, whereas non-phosphorylated cTnI was the most abundant cTnI proteoform in the dilated cardiomyopathy heart.
“We found ppcTnI to be the predominant cTnI proteoform in the non-diseased donor heart (Fig. 2f), whereas non-phosphorylated cTnI was found to be the most abundant cTnI proteoform in the dilated cardiomyopathy heart (Fig. 2g), consistent with previous reports suggesting phosphorylation of cTnI as a potential biomarker for heart diseases27,31,32.”
From Nanoproteomics enables proteoform-resolved analysis of low-abundance proteins in human serum (2020) · cites this paper as [27]
The estimated levels of cTnI released after cardiac injury events such as AMI are typically in the range of 0.5-50 ng/mL.
“Note that the estimated levels of cTnI released after cardiac injury events such as AMI are typically in the range of 0.5–50 ng/mL25,27.”
From Nanoproteomics enables proteoform-resolved analysis of low-abundance proteins in human serum (2020) · cites this paper as [27]
The concurrent enrichment of cTnI and depletion of HSA together with reliable preservation of cTnI proteoform fingerprints during NP enrichment solves the major challenge in MS detection of cTnI proteoforms directly from blood.
“The concurrent enrichment of cTnI and depletion of HSA together with the reliable preservation of the cTnI proteoform fingerprints during the NP enrichment solves the major challenge in the MS detection of cTnI proteoforms directly from the blood27 and will enable the application of this top-down nanoproteomics strategy to clinical samples to eventually establish a proteoform-resolved cTnI assay.”
From Nanoproteomics enables proteoform-resolved analysis of low-abundance proteins in human serum (2020) · cites this paper as [27]
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Analysis of Cardiac Troponin Proteoforms by Top-Down Mass Spectrometry
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- Authors
- Soetkamp, D., Raedschelders, K., Mastali, M., Sobhani, K., Bairey Merz, C. N., & Van Eyk, J.
- Affiliations
- Cedars-Sinai Medical Center (US)
- Women’s Heart Center, Cedars-Sinai Medical Center, Los Angeles, CA, USA
- Heart Institute, Cedars-Sinai Medical Center, Los Angeles, CA, USA
- Corresponding author
- Soetkamp, Daniel
- Venue
- Expert Review of Proteomics
- Publisher
- Informa UK Limited
- Published
- 2017-10-16
- Volume
- 14
- Issue
- 11
- Pages
- 973-986
- ISSN
- 1478-9450 (ISSN-L)
- 1744-8387
- PMC
- PMC6174071
- OpenAlex
- W2761284362
- Cited by
- 36
- References
- 157
- Citations by year
- 2026: 3 · 2025: 2 · 2024: 2 · 2023: 6 · 2022: 3 · 2021: 3 · 2020: 10 · 2019: 4 · 2018: 3
- FWCI
- 0.53
- Type
- journal article
- Language
- en
- Update notices
- correction (2017-11-21)
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Expert Review of Proteomics (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Heart, Lung, and Blood Institute (HL0107153-06)
- U.S. Department of Defense (16W81XWH-16-1-0592)
- Topics
- Physical Sciences › Chemistry › Spectroscopy › Advanced Proteomics Techniques and Applications
- Health Sciences › Medicine › Cardiology and Cardiovascular Medicine › Acute Myocardial Infarction Research
- Physical Sciences › Chemistry › Spectroscopy › Mass Spectrometry Techniques and Applications
- Keywords
- cardiac troponin I, troponin complex, cardiac biomarkers, acute myocardial infarction, acute coronary syndrome, risk stratification, mass spectrometry, protein modification, hypertrophic cardiomyopathy, diabetes mellitus, heart failure
- MeSH terms
- Female, Heart Diseases, Humans, Male, Myocardial Infarction, Mass Spectrometry, Biomarkers, Troponin I, Proteomics
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