ArticleJournal of the American Heart Association2021
Spectrum of Apolipoprotein AI and Apolipoprotein AII Proteoforms and Their Associations With Indices of Cardiometabolic Health: The CARDIA Study.
Article in Journal of the American Heart Association, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
19 citing papers in PubMed, 26 citations in OpenAlex.
- Automating Middle-Down Mass Spectrometry Analysis for Extensive Antibody Characterization.Analytical chemistry · 2026Article
- The Structural and Functional Journey of Apolipoprotein A-I Through the Human Body.Current atherosclerosis reports · 2026Review
- Sample preparation and cleanup methods for clinical top-down proteomics.Expert review of proteomics · 2025Review
- HDL proteome: from its characterization to quantitative measurements in particle subspecies and functional associations.Expert review of proteomics · 2025Review
- Deep Profiling of Plasma Proteoforms with Engineered Nanoparticles for Top-Down Proteomics.Journal of proteome research · 2024Article
- Trypsin Partially Cleaves Apolipoprotein A-I (ApoA-I) Precursor into Mature ApoA-I Hindering the Quantification of Naturally Occurring ApoA-I Proteoforms by Liquid Chromatography in Multiple Reaction Monitoring Mode Mass Spectrometry (LC-MRM-MS).Journal of the American Society for Mass Spectrometry · 2024Article
- Mass Spectrometry-Based Top-Down Proteomics in Nanomedicine: Proteoform-Specific Measurement of Protein Corona.ACS nano · 2024Article
- Comparative analysis of human tear fluid and aqueous humor proteomes.The ocular surface · 2024Article
- Machine learning-based health environmental-clinical risk scores in European children.Communications medicine · 2024Article
- Targeted Quantification of Proteoforms in Complex Samples by Proteoform Reaction Monitoring.Analytical chemistry · 2024Article
- Top-down proteomics.Nature reviews. Methods primers · 2024Article
- Orbitrap Mass Spectrometry and High-Field Asymmetric Waveform Ion Mobility Spectrometry (FAIMS) Enable the in-Depth Analysis of Human Serum Proteoforms.Journal of proteome research · 2023Article
- Preparative Electrophoresis for HDL Particle Size Separation and Intact-Mass Apolipoprotein Proteoform Analysis.Journal of proteome research · 2023Article
- Mass spectrometry-based proteomics for advancing solid organ transplantation research.Frontiers in transplantation · 2023Review
- Deciphering combinatorial post-translational modifications by top-down mass spectrometry.Current opinion in chemical biology · 2022Review
- Review
- Resolution of apolipoprotein A1 and A2 proteoforms: their cardiometabolic correlates and implications for future research.Current opinion in lipidology · 2022Review
- Native Mass Spectrometry at the Convergence of Structural Biology and Compositional Proteomics.Accounts of chemical research · 2022Article
- Apolipoprotein A-II, a Player in Multiple Processes and Diseases.Biomedicines · 2022Review
Corrections and comments
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Authors and funding
12 authors at 4 institutions in 2 countries.
Funding
Abstract
Background ApoAI (apolipoproteins AI) and apoAII (apolipoprotein AII) are structural and functional proteins of high-density lipoproteins (HDL) which undergo post-translational modifications at specific residues, creating distinct proteoforms. While specific post-translational modifications have been reported to alter apolipoprotein function, the full spectrum of apoAI and apoAII proteoforms and their associations with cardiometabolic phenotype remains unknown. Herein, we comprehensively characterize apoAI and apoAII proteoforms detectable in serum and their post-translational modifications and quantify their associations with cardiometabolic health indices. Methods and Results Using top-down proteomics (mass-spectrometric analysis of intact proteins), we analyzed paired serum samples from 150 CARDIA (Coronary Artery Risk Development in Young Adults) study participants from year 20 and 25 exams. Measuring 15 apoAI and 9 apoAII proteoforms, 6 of which carried novel post-translational modifications, we quantified associations between percent proteoform abundance and key cardiometabolic indices. Canonical (unmodified) apoAI had inverse associations with HDL cholesterol and HDL-cholesterol efflux, and positive associations with obesity indices (body mass index, waist circumference), and triglycerides, whereas glycated apoAI showed positive associations with serum glucose and diabetes mellitus. Fatty-acid‒modified ApoAI proteoforms had positive associations with HDL cholesterol and efflux, and inverse associations with obesity indices and triglycerides. Truncated and dimerized proteoforms of apoAII were associated with HDL cholesterol (positively) and obesity indices (inversely). Several proteoforms had no significant associations with phenotype. Conclusions Associations between apoAI and AII and cardiometabolic indices are proteoform-specific. These results provide "proof-of-concept" that precise chemical characterization of human apolipoproteins will yield improved insights into the complex pathways through which proteins signify and mediate health and disease.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.