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Protein Adducts of Aldehydic Lipid Peroxidation Products: Identification and Characterization of Protein Adducts Using an Aldehyde/Keto Reactive Probe in Combination with Mass Spectrometry

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  • This chapter describes a mass spectrometry-based strategy that facilitates the unambiguous identification and characterization of proteins modified by lipid peroxidation-derived 2-alkenals. The approach employs a biotinylated hydroxyl amine derivative as an aldehyde/keto reactive probe in conjunction with selective enrichment and tandem mass spectrometric analysis. Methodological details are given for model studies involving a distinct protein and 4-hydroxy-2-nonenal (HNE). The method was also evaluated for an exposure study of a cell culture system with HNE that yielded the major protein targets of HNE in human monocytic THP-1 cells. The application of the approach to complex biological systems is demonstrated for the identification and characterization of endogenous protein targets of aldehydic lipid peroxidation products present in cardiac mitochondria.
  • This is an author's manuscript, as accepted by the publisher. The published chapter 16 is copyrighted by Elsevier.
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  • Maier, C. S., Chavez, J., Wang, J., & Wu, J. (2010). Protein adducts of aldehydic lipid peroxidation products: identification and characterization of protein adducts using an aldehyde/keto-reactive probe in combination with mass spectrometry. Methods in Enzymology, 473, 305-330. doi:10.1016/S0076-6879(10)73016-0
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  • This work was supported by grants from the NIH (AG025372, HL081721, ES00210) and the Oregon Medical Research Foundation. The Mass Spectrometry Facility of the Environmental Health Sciences Center at Oregon State University is supported in part by NIH/NIEHS grant P30ES00210.
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