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Updated: Jun 5, 2026

Isolation and Analysis of Plasma Lipoproteins by Ultracentrifugation
Published on: January 28, 2021
Isoforms of apolipoprotein C-I associated with individuals with coronary artery disease
D'Vesharronne Moore1, Catherine McNeal, Ronald Macfarlane
1Laboratory for Cardiovascular Chemistry, Department of Chemistry, Texas A&M University, College Station, TX 77843-3255, USA.
Insights
New Apolipoprotein C-I (apoC-I) isoforms were found in individuals with coronary artery disease (CAD). These novel apoC-I variants, potentially from genetic mutations and oxidative stress, were absent in non-CAD subjects.
Area of Science:
- Biochemistry
- Cardiovascular Science
- Proteomics
Background:
- Apolipoprotein C-I (apoC-I) is a serum protein linked to high-density lipoproteins (HDL) and triglyceride-rich lipoproteins.
- Dysregulation of apoC-I may play a role in cardiovascular health.
Purpose of the Study:
- To investigate apoC-I in high-density lipoprotein (HDL) subfractions from individuals with and without coronary artery disease (CAD).
- To identify novel apoC-I isoforms and their potential origins in CAD patients.
Main Methods:
- Mass spectrometry was employed to analyze apoC-I in HDL subfractions.
- Comparative analysis of apoC-I mass spectra between CAD and non-CAD cohorts.
Main Results:
- Novel apoC-I isoforms were detected in individuals with CAD, while expected isoforms were absent.
- Mass spectra from the CAD cohort showed satellite peaks, suggesting oxidative processes.
- Analysis indicated potential genetic mutations as the source of new apoC-I isoforms.
Conclusions:
- Coronary artery disease is associated with the presence of novel apoC-I isoforms.
- Oxidative stress and potential genetic mutations may contribute to the formation of these aberrant apoC-I variants.
- These findings suggest a potential role for altered apoC-I in the pathophysiology of CAD.
Abstract:
Apolipoprotein C-I (apoC-I) is a 6.6kDa serum protein associated with high density lipoproteins (HDL) and triglyceride-rich lipoproteins. In this study, apoC-I was examined in high density lipoprotein subfractions from individuals with and without coronary artery disease (CAD). New isoforms of apoC-I, were detected in the cohort of individuals with CAD using mass spectrometry while the expected apoC-I isoforms were absent. In addition, the apoC-I mass spectra for the CAD cohort had satellite peaks indicative of the involvement of oxidative processes. Further analysis of the mass spectra of the CAD and non-CAD cohorts suggest that the origin of these new isoforms may be due to genetic mutations that could compromise the function of apoC-I.
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