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

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

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1
Department of Chemistry, Oregon State University, Corvallis, OR 97331, USA.

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.

PMID:
21513823
PMCID:
PMC3199298
DOI:
10.1016/j.jprot.2011.03.031
[Indexed for MEDLINE]
Free PMC Article
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