Article ID Journal Published Year Pages File Type
1225411 Journal of Proteomics 2011 13 Pages PDF
Abstract

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.

Graphical abstractFigure optionsDownload full-size imageDownload high-quality image (78 K)Download as PowerPoint slideHighlights► Endogenous protein targets of electrophilic 2-alkenals in cardiac mitochondria. ► Aldehyde/keto-specific labeling and affinity strategy in conjunction with LC-MS/MS. ► Distinct target sites were modified by a variety of 2-alkenal products.

Related Topics
Physical Sciences and Engineering Chemistry Analytical Chemistry
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