The application of multiple reaction monitoring to assess ApoA-I methionine oxidations in diabetes and cardiovascular disease

Hussein N. Yassine, Angela M. Jackson, Peter D. Reaven, Dobrin Nedelkov, Randall W. Nelson, Serrine S. Lau, Christoph H. Borchers

Research output: Contribution to journalArticlepeer-review

20 Scopus citations

Abstract

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.

Original languageEnglish (US)
Pages (from-to)18-24
Number of pages7
JournalTranslational Proteomics
Volume4-5
DOIs
StatePublished - 2014

Keywords

  • Cardiovascular disease
  • Diabetes
  • HDL
  • Multiple reaction monitoring
  • Proteomics

ASJC Scopus subject areas

  • Biochemistry

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