Site-specific proteomic analysis of lipoxidation adducts in cardiac mitochondria reveals chemical diversity of 2-alkenal adduction

J Proteomics. 2011 Oct 19;74(11):2417-29. doi: 10.1016/j.jprot.2011.03.031. Epub 2011 Apr 13.


The modification of proteins by lipid peroxidation products has been linked to numerous diseases and age-related disorders. Here we report on the identification of endogenous protein targets of electrophilic 2-alkenals in cardiac mitochondria. An aldehyde/keto-specific chemical labeling and affinity strategy in combination with LC-MS/MS resulted in 39 unique lipoxidation sites on 27 proteins. Several of the target sites were modified by a variety of 2-alkenal products including acrolein, β-hydroxyacrolein, crotonaldehyde, 4-hydroxy-2-hexenal, 4-hydroxy-2-nonenal and 4-oxo-2-nonenal. Many of the adduction sites are implicated in the catalytic function of key mitochondrial enzymes suggesting potential impact on pathways and overall mitochondrial function.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Aldehydes / chemistry
  • Aldehydes / metabolism*
  • Amino Acid Sequence
  • Animals
  • Chromatography, Liquid
  • Lipid Peroxidation / drug effects*
  • Lipid Peroxidation / physiology
  • Male
  • Mitochondria, Heart / chemistry
  • Mitochondria, Heart / drug effects*
  • Mitochondria, Heart / metabolism*
  • Models, Biological
  • Models, Molecular
  • Oxidation-Reduction / drug effects
  • Peptide Mapping / methods*
  • Protein Processing, Post-Translational / drug effects
  • Proteomics / methods*
  • Rats
  • Rats, Inbred F344
  • Swine
  • Tandem Mass Spectrometry


  • Aldehydes