The oxidative modification of apolipoprotein A-I’s methionine148 (M148) is associated with defective HDL function in vitro. Multiple reaction monitoring (MRM) is a mass spectrometric technique that can be used to quantitate post-translational modifications. In this study, we developed an MRM assay to monitor the abundance ratio of the peptide containing oxidized M148 to the native peptide in ApoA-I. Measurement of the oxidized-to-unoxidized-M148 ratio was reproducible (CV < 5%). The extent of methionine M148 oxidation in the HDL of healthy controls, and type 2 diabetic participants with and without prior cardiovascular events (CVD) were then examined. The results suggest a significant increase in the relative ratio of the peptide containing oxidized M148 to the unmodified peptide in the HDL of participants with diabetes and CVD (p < 0.001), compared to participants without CVD. Monitoring the abundance ratio of the peptides containing oxidized and unoxidized M148 by MRM provides a means of examining the relationship between M148 oxidation and vascular complications in CVD.
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- The Application of Multiple Reaction Monitoring to Assess ApoA-I Methionine Oxidations in Diabetes and Cardiovascular Disease
- Yassine, Hussein N. (Author)
- Jackson, Angela M. (Author)
- Reaven, Peter D. (Author)
- Nedelkov, Dobrin (Author)
- Nelson, Randall (Author)
- Lau, Serrine S. (Author)
- Borchers, Christoph H. (Author)
- Biodesign Institute (Contributor)
- Digital object identifier: 10.1016/j.trprot.2014.10.001
- Identifier TypeInternational standard serial numberIdentifier Value2212-9626
- Identifier TypeInternational standard serial numberIdentifier Value2212-9634
- The final version of this article, as published in Translational Proteomics, can be viewed online at: http://www.sciencedirect.com/science/article/pii/S2212963414000102?via%3Dihub
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Yassine, H. N., Jackson, A. M., Reaven, P. D., Nedelkov, D., Nelson, R. W., Lau, S. S., & Borchers, C. H. (2014). The application of multiple reaction monitoring to assess ApoA-I methionine oxidations in diabetes and cardiovascular disease. Translational Proteomics, 4-5, 18-24. doi:10.1016/j.trprot.2014.10.001